GenomeNet

Database: UniProt
Entry: P98133
LinkDB: P98133
Original site: P98133 
ID   FBN1_BOVIN              Reviewed;        2871 AA.
AC   P98133; F1N4K8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   06-JUL-2016, sequence version 2.
DT   10-APR-2019, entry version 149.
DE   RecName: Full=Fibrillin-1 {ECO:0000250|UniProtKB:P35555};
DE   AltName: Full=MP340;
DE   Contains:
DE     RecName: Full=Asprosin {ECO:0000250|UniProtKB:P35555};
DE   Flags: Precursor;
GN   Name=FBN1 {ECO:0000250|UniProtKB:P35555};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skin;
RX   PubMed=7835900; DOI=10.1006/geno.1994.1527;
RA   Tilstra D.J., Potter K.A., Byers P.H.;
RT   "Sequence of the coding region of the bovine fibrillin cDNA and
RT   localization to bovine chromosome 10.";
RL   Genomics 23:480-485(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C.,
RA   Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S.,
RA   Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=8557636; DOI=10.1074/jbc.271.2.1096;
RA   Gibson M.A., Hatzinikolas G., Kumaratilake J.S., Sandberg L.B.,
RA   Nicholl J.K., Sutherland G.R., Cleary E.G.;
RT   "Further characterization of proteins associated with elastic fiber
RT   microfibrils including the molecular cloning of MAGP-2 (MP25).";
RL   J. Biol. Chem. 271:1096-1103(1996).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=21989719; DOI=10.1167/iovs.10-5955;
RA   Gabriel L.A., Wang L.W., Bader H., Ho J.C., Majors A.K.,
RA   Hollyfield J.G., Traboulsi E.I., Apte S.S.;
RT   "ADAMTSL4, a secreted glycoprotein widely distributed in the eye,
RT   binds Fibrillin-1 microfibrils and accelerates microfibril
RT   biogenesis.";
RL   Invest. Ophthalmol. Vis. Sci. 53:461-469(2012).
CC   -!- FUNCTION: Fibrillin-1: Structural component of the 10-12 nm
CC       diameter microfibrils of the extracellular matrix, which conveys
CC       both structural and regulatory properties to load-bearing
CC       connective tissues. Fibrillin-1-containing microfibrils provide
CC       long-term force bearing structural support. In tissues such as the
CC       lung, blood vessels and skin, microfibrils form the periphery of
CC       the elastic fiber, acting as a scaffold for the deposition of
CC       elastin. In addition, microfibrils can occur as elastin-
CC       independent networks in tissues such as the ciliary zonule,
CC       tendon, cornea and glomerulus where they provide tensile strength
CC       and have anchoring roles. Fibrillin-1 also plays a key role in
CC       tissue homeostasis through specific interactions with growth
CC       factors, such as the bone morphogenetic proteins (BMPs), growth
CC       and differentiation factors (GDFs) and latent transforming growth
CC       factor-beta-binding proteins (LTBPs), cell-surface integrins and
CC       other extracellular matrix protein and proteoglycan components.
CC       Regulates osteoblast maturation by controlling TGF-beta
CC       bioavailability and calibrating TGF-beta and BMP levels,
CC       respectively. Negatively regulates osteoclastogenesis by binding
CC       and sequestering an osteoclast differentiation and activation
CC       factor TNFSF11. This leads to disruption of TNFSF11-induced Ca(2+)
CC       signaling and impairment of TNFSF11-mediated nuclear translocation
CC       and activation of transcription factor NFATC1 which regulates
CC       genes important for osteoclast differentiation and function.
CC       Mediates cell adhesion via its binding to cell surface receptors
CC       integrins ITGAV:ITGB3 and ITGA5:ITGB1. Binds heparin and this
CC       interaction plays an important role in the assembly of
CC       microfibrils. {ECO:0000250|UniProtKB:P35555,
CC       ECO:0000250|UniProtKB:Q61554}.
CC   -!- FUNCTION: Asprosin: Hormone that targets the liver to increase
CC       plasma glucose levels. Secreted by white adipose tissue and
CC       circulates in the plasma. Acts in response to fasting and promotes
CC       blood glucose elevation by binding to the surface of hepatocytes.
CC       Promotes hepatocyte glucose release by activating the protein
CC       kinase A activity in the liver, resulting in rapid glucose release
CC       into the circulation. {ECO:0000250|UniProtKB:P35555}.
CC   -!- SUBUNIT: Interacts with COL16A1. Interacts with integrin alpha-
CC       V/beta-3. Interacts with ADAMTS10; this interaction promotes
CC       microfibril assembly. Interacts with THSD4; this interaction
CC       promotes fibril formation. Interacts (via N-terminal domain) with
CC       FBLN2, FBLN4 and FBLN5. Interacts with ELN. Forms a ternary
CC       complex with ELN and FBLN2 or FBLN5 and a significant interaction
CC       with ELN seen only in the presence of FBLN2 or FBLN5. Interacts
CC       (via N-terminal domain) with LTBP2 (via C-terminal domain) in a
CC       Ca(+2)-dependent manner. Interacts (via N-terminal domain) with
CC       LTBP1 (via C-terminal domain). Interacts with integrins
CC       ITGA5:ITGB1, ITGAV:ITGB3 and ITGAV:ITGB6. Interacts (via N-
CC       terminal domain) with BMP2, BMP4, BMP7, BMP10 and GDF5. Interacts
CC       (via N-terminal domain) with MFAP2 and MFAP5. Interacts with
CC       ADAMTSL5. Interacts with MFAP4. Interacts (via N-terminal domain)
CC       with TNFSF11 in a Ca(+2)-dependent manner.
CC       {ECO:0000250|UniProtKB:P35555, ECO:0000250|UniProtKB:Q61554}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P35555}.
CC       Note=Fibrillin-1 and Asprosin chains are still linked together
CC       during the secretion from cells, but are subsequently separated by
CC       furin. {ECO:0000250|UniProtKB:P35555}.
CC   -!- SUBCELLULAR LOCATION: Asprosin: Secreted
CC       {ECO:0000250|UniProtKB:P35555}. Note=Secreted into the plasma.
CC       {ECO:0000250|UniProtKB:P35555}.
CC   -!- SUBCELLULAR LOCATION: Fibrillin-1: Secreted, extracellular space,
CC       extracellular matrix {ECO:0000250|UniProtKB:P35555}.
CC   -!- PTM: Fibrillin-1: Cleavage of N- and C-terminus by furin is
CC       required for incorporation into the extracellular matrix and
CC       assembly into microfibrils. The C-terminus, which corresponds to
CC       the Asprosin chain, was initially thought to constitute a
CC       propeptide. Fibrillin-1 and Asprosin chains are still linked
CC       together during the secretion from cells, but are subsequently
CC       separated by furin, an essential step for incorporation of
CC       Fibrillin-1 into the nascent microfibrils.
CC       {ECO:0000250|UniProtKB:P35555}.
CC   -!- PTM: Fibrillin-1: Forms intermolecular disulfide bonds either with
CC       other fibrillin-1 molecules or with other components of the
CC       microfibrils. {ECO:0000250|UniProtKB:P35555}.
CC   -!- SIMILARITY: Belongs to the fibrillin family. {ECO:0000305}.
DR   EMBL; L28748; AAA74122.1; -; mRNA.
DR   EMBL; DAAA02029120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DAAA02029121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DAAA02029122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A55567; A55567.
DR   RefSeq; NP_776478.1; NM_174053.2.
DR   RefSeq; XP_015328665.1; XM_015473179.1.
DR   UniGene; Bt.107024; -.
DR   ProteinModelPortal; P98133; -.
DR   SMR; P98133; -.
DR   STRING; 9913.ENSBTAP00000002944; -.
DR   PaxDb; P98133; -.
DR   PeptideAtlas; P98133; -.
DR   PRIDE; P98133; -.
DR   Ensembl; ENSBTAT00000002944; ENSBTAP00000002944; ENSBTAG00000002278.
DR   GeneID; 281154; -.
DR   KEGG; bta:281154; -.
DR   CTD; 2200; -.
DR   VGNC; VGNC:28885; FBN1.
DR   eggNOG; ENOG410IR7H; Eukaryota.
DR   eggNOG; ENOG410XSTY; LUCA.
DR   GeneTree; ENSGT00950000183158; -.
DR   HOGENOM; HOG000231768; -.
DR   HOVERGEN; HBG005643; -.
DR   InParanoid; P98133; -.
DR   KO; K06825; -.
DR   OMA; RPPVEYP; -.
DR   OrthoDB; 1174178at2759; -.
DR   TreeFam; TF316849; -.
DR   Reactome; R-BTA-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-BTA-1566948; Elastic fibre formation.
DR   Reactome; R-BTA-2129379; Molecules associated with elastic fibres.
DR   Reactome; R-BTA-216083; Integrin cell surface interactions.
DR   Reactome; R-BTA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-BTA-8957275; Post-translational protein phosphorylation.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000002278; Expressed in 10 organ(s), highest expression level in colon.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0001527; C:microfibril; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR   GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR   GO; GO:0005179; F:hormone activity; ISS:UniProtKB.
DR   GO; GO:0034199; P:activation of protein kinase A activity; ISS:UniProtKB.
DR   GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR   GO; GO:0006006; P:glucose metabolic process; ISS:UniProtKB.
DR   GO; GO:0010737; P:protein kinase A signaling; ISS:UniProtKB.
DR   Gene3D; 3.90.290.10; -; 9.
DR   InterPro; IPR026823; cEGF.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR011398; FBN.
DR   InterPro; IPR040872; Fibrillin_U_N.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR017878; TB_dom.
DR   InterPro; IPR036773; TB_dom_sf.
DR   PANTHER; PTHR24039; PTHR24039; 1.
DR   Pfam; PF12662; cEGF; 2.
DR   Pfam; PF07645; EGF_CA; 39.
DR   Pfam; PF18193; Fibrillin_U_N; 1.
DR   Pfam; PF00683; TB; 9.
DR   SMART; SM00181; EGF; 47.
DR   SMART; SM00179; EGF_CA; 44.
DR   SUPFAM; SSF57184; SSF57184; 10.
DR   SUPFAM; SSF57581; SSF57581; 9.
DR   PROSITE; PS00010; ASX_HYDROXYL; 43.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 38.
DR   PROSITE; PS50026; EGF_3; 45.
DR   PROSITE; PS01187; EGF_CA; 43.
DR   PROSITE; PS51364; TB; 9.
PE   1: Evidence at protein level;
KW   Calcium; Complete proteome; Direct protein sequencing; Disulfide bond;
KW   EGF-like domain; Extracellular matrix; Glycoprotein; Hormone;
KW   Phosphoprotein; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000250|UniProtKB:P35555}.
FT   PROPEP       25     44       {ECO:0000250|UniProtKB:P35555}.
FT                                /FTId=PRO_0000436879.
FT   CHAIN        45   2731       Fibrillin-1.
FT                                {ECO:0000250|UniProtKB:P35555}.
FT                                /FTId=PRO_0000007580.
FT   CHAIN      2732   2871       Asprosin. {ECO:0000250|UniProtKB:P35555}.
FT                                /FTId=PRO_0000436880.
FT   DOMAIN       81    112       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      115    146       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      147    178       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      184    236       TB 1.
FT   DOMAIN      246    287       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      288    329       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      334    389       TB 2.
FT   DOMAIN      449    489       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      490    529       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      530    571       EGF-like 8; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      572    612       EGF-like 9; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      613    653       EGF-like 10; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      659    711       TB 3.
FT   DOMAIN      723    764       EGF-like 11; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      765    806       EGF-like 12; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      807    846       EGF-like 13; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      851    902       TB 4.
FT   DOMAIN      910    951       EGF-like 14; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      956   1008       TB 5.
FT   DOMAIN     1028   1069       EGF-like 15; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1070   1112       EGF-like 16; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1113   1154       EGF-like 17; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1155   1196       EGF-like 18; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1197   1237       EGF-like 19; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1238   1279       EGF-like 20; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1280   1321       EGF-like 21; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1322   1362       EGF-like 22; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1363   1403       EGF-like 23; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1404   1445       EGF-like 24; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1446   1486       EGF-like 25; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1487   1527       EGF-like 26; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1532   1589       TB 6.
FT   DOMAIN     1606   1647       EGF-like 27; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1648   1688       EGF-like 28; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1693   1748       TB 7.
FT   DOMAIN     1766   1807       EGF-like 29; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1808   1848       EGF-like 30; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1849   1890       EGF-like 31; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1891   1929       EGF-like 32; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1930   1972       EGF-like 33; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1973   2012       EGF-like 34; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     2013   2054       EGF-like 35; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     2059   2111       TB 8.
FT   DOMAIN     2127   2165       EGF-like 36; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     2166   2205       EGF-like 37; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     2206   2246       EGF-like 38; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     2247   2290       EGF-like 39; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     2291   2332       EGF-like 40; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     2337   2390       TB 9.
FT   DOMAIN     2402   2443       EGF-like 41; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     2444   2484       EGF-like 42; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     2485   2523       EGF-like 43; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     2524   2566       EGF-like 44; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     2567   2606       EGF-like 45; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     2607   2647       EGF-like 46; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     2648   2687       EGF-like 47; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   REGION       45    450       N-terminal domain.
FT                                {ECO:0000250|UniProtKB:P35555}.
FT   REGION       45     81       Fibrillin unique N-terminal (FUN) domain.
FT                                {ECO:0000250|UniProtKB:P35555}.
FT   REGION      119    329       Interaction with MFAP4.
FT                                {ECO:0000250|UniProtKB:P35555}.
FT   REGION      195    221       Hybrid domain 1.
FT                                {ECO:0000250|UniProtKB:P35555}.
FT   REGION      862    887       Hybrid domain 2.
FT                                {ECO:0000250|UniProtKB:P35555}.
FT   REGION     1528   2731       C-terminal domain.
FT                                {ECO:0000250|UniProtKB:P35555}.
FT   MOTIF      1541   1543       Cell attachment site.
FT                                {ECO:0000250|UniProtKB:P35555}.
FT   COMPBIAS    392    446       Pro-rich.
FT   SITE         44     45       Cleavage; by furin.
FT                                {ECO:0000250|UniProtKB:P35555}.
FT   SITE       2731   2732       Cleavage; by furin.
FT                                {ECO:0000250|UniProtKB:P35555}.
FT   MOD_RES    2702   2702       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P35555}.
FT   MOD_RES    2709   2709       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q61554}.
FT   CARBOHYD    448    448       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1067   1067       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1149   1149       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1369   1369       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1484   1484       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1581   1581       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1669   1669       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1703   1703       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1713   1713       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1902   1902       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2077   2077       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2178   2178       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2734   2734       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2750   2750       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2767   2767       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     59     68       {ECO:0000250|UniProtKB:P35555}.
FT   DISULFID     67     80       {ECO:0000250|UniProtKB:P35555}.
FT   DISULFID     85     94       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     89    100       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    102    111       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    119    129       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    123    134       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    136    145       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    150    160       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    154    166       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    168    177       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    250    262       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    257    271       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    273    286       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    292    304       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    299    313       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    315    328       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    453    465       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    460    474       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    476    488       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    494    504       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    499    513       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    515    528       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    534    546       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    541    555       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    557    570       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    576    587       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    582    596       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    598    611       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    617    628       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    623    637       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    639    652       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    727    739       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    734    748       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    750    763       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    769    781       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    776    790       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    792    805       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    811    821       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    816    830       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    832    845       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    853    875       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    862    887       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    876    890       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    896    908       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    914    926       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    921    935       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    937    950       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1032   1044       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1039   1053       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1055   1068       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1074   1086       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1081   1095       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1097   1111       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1117   1129       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1124   1138       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1140   1153       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1159   1171       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1166   1180       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1182   1195       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1201   1212       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1208   1221       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1223   1236       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1242   1254       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1249   1263       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1265   1278       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1284   1296       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1291   1305       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1307   1320       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1326   1339       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1333   1348       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1350   1361       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1367   1380       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1374   1389       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1391   1402       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1408   1420       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1415   1429       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1431   1444       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1450   1461       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1456   1470       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1472   1485       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1491   1502       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1497   1511       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1513   1526       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1534   1562       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1549   1574       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1563   1577       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1564   1589       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1610   1622       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1617   1631       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1633   1646       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1652   1663       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1658   1672       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1674   1687       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1770   1782       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1777   1791       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1793   1806       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1812   1824       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1818   1833       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1835   1847       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1853   1865       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1860   1874       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1876   1889       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1895   1905       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1900   1914       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1916   1928       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1934   1947       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1942   1956       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1958   1971       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1977   1989       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1984   1998       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2000   2011       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2017   2029       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2024   2038       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2040   2053       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2061   2083       {ECO:0000250|UniProtKB:P35555,
FT                                ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2070   2096       {ECO:0000250|UniProtKB:P35555,
FT                                ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2084   2099       {ECO:0000250|UniProtKB:P35555,
FT                                ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2085   2111       {ECO:0000250|UniProtKB:P35555,
FT                                ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2131   2142       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2137   2151       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2153   2164       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2170   2181       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2176   2190       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2192   2204       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2210   2221       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2217   2230       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2232   2245       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2251   2265       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2258   2274       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2276   2289       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2295   2307       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2302   2316       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2318   2331       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2406   2418       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2413   2427       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2429   2442       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2448   2459       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2455   2468       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2470   2483       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2489   2500       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2496   2509       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2511   2522       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2528   2541       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2535   2550       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2552   2565       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2571   2581       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2577   2590       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2592   2605       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2611   2622       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2617   2631       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2633   2646       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2652   2663       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2659   2672       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2674   2686       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   CONFLICT     51     51       D -> N (in Ref. 1; AAA74122).
FT                                {ECO:0000305}.
FT   CONFLICT    362    362       V -> A (in Ref. 1; AAA74122).
FT                                {ECO:0000305}.
FT   CONFLICT    620    620       P -> L (in Ref. 1; AAA74122).
FT                                {ECO:0000305}.
FT   CONFLICT   2561   2561       S -> T (in Ref. 1; AAA74122).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2871 AA;  312249 MW;  D49E971A8176D3B8 CRC64;
     MRRGGLLEVA LGFTVLLASY TSHGADTNLE AGNVKETRAN RAKRRGGGGH DALKGPNVCG
     SRYNAYCCPG WKTLPGGNQC IVPICRHSCG DGFCSRPNMC TCPSGQIAPS CGSRSIQHCN
     IRCMNGGSCS DDHCLCQKGY IGTHCGQPVC ESGCLNGGRC VAPNRCACTY GFTGPQCERD
     YRTGPCFTVI SNQMCQGQLS GIVCTKTLCC ATVGRAWGHP CEMCPAQPHP CRRGFIPNIR
     TGACQDVDEC QAIPGLCQGG NCINTVGSFE CKCPAGHKFN EVSQKCEDID ECSTIPGICD
     GGECTNTVSS YFCKCPPGFY TSPDGTRCID VRPGYCYTAL ANGRCSNQLP QSITKMQCCC
     DVGRCWSPGV TVAPEMCPIR ATEDFNKLCS VPMVIPERPG YPPPPLGPVP PVQPVPPGFP
     PGPQIMIPRP PVEYPYPSRE PPRVLPVNVT DYCQLFRYLC QNGRCIPTPG SYRCECNKGF
     QLDLRGECID VDECEKNPCA GGECINTQGS YTCQCRPGYQ STLTRTECRD IDECLQNGRI
     CNNGRCINTD GSFHCVCNAG FHVTRDGKNC EDMDECSIRN MCLNGMCINE DGSFKCICKP
     GFQLASDGRY CKDINECETP GICMNGRCVN TDGSYRCECF PGLAVGLDGR VCVDTHMRST
     CYGGYKRGQC VKPLFGAVTK SECCCASTEY AFGEPCQPCP SQNSAEYQAL CSSGPGITSA
     GSDINECALD PDICPNGICE NLRGTYKCIC NSGYEVDSTG KNCVDINECV LNSLLCDNGQ
     CRNTPGSFVC TCPKGFIYKP ELKTCEDIDE CESSPCINGV CKNSPGSFIC ECSSESTLDP
     TKTICIETIK GTCWQTVIDG RCEININGAT LKSQCCSSLG AAWGSPCTPC QVDPICGKGY
     SRIKGTQCED IDECEVFPGV CKNGLCVNSK GSFKCQCPSG MTLDATGRIC LDIRLETCFL
     RYEDEECTLP VAGRHRMDAC CCSVGAAWGT EECEECPVRN TPEYEELCPR GPGFATKEIT
     NGKRFFKDIN ECKMIPNLCT HGKCRNTIGS FKCRCDSGFA LDSEERNCTD IDECRISPDL
     CGRGQCVNTP GDFECKCDEG YESGFMMMKN CMDIDECQRD PLLCRGGVCL NTEGSYRCEC
     PPGHQLAPNI SACIDINECE LSAHLCPHGR CVNLIGKYQC ACNPGYHSTP DRLFCVDIDE
     CSIMNGGCET FCTNSEGSYE CSCQPGFALM PDQRSCTDID ECEDNPNICD GGQCTNIPGE
     YRCLCYDGFM ASEDMKTCVD VNECDLNPNI CLSGTCENTK GSFICHCDMG YSGKKGKTGC
     TDINECEIGA HNCDRHAVCT NTAGSFKCSC SPGWIGDGIK CTDLDECSNG THMCSQHADC
     KNTMGSYRCL CKEGYTGDGF TCTDLDECSE NLNLCGNGQC LNAPGGYRCE CDMGFVPSAD
     GKACEDIDEC SLPNICVFGT CHNLPGLFRC ECEIGYELDR SGGNCTDVNE CLDPTTCISG
     NCVNTPGSYT CDCPPDFELN PTRVGCVDTR SGNCYLDIRP RGDNGDTACS NEIGVGVSKA
     SCCCSLGKAW GTPCELCPPV NTSEYKILCP GGEGFRPNPI TVILEDIDEC QELPGLCQGG
     KCINTFGSFQ CRCPTGYYLN EDTRVCDDVN ECETPGICGP GTCYNTVGNY TCICPPDYMQ
     VNGGNNCMDM RRSLCYRNYY ADNQTCDGEL LFNMTKKMCC CSYNIGRAWN KPCEQCPIPS
     TDEFATLCGS QRPGFVIDIY TGLPVDIDEC REIPGVCENG VCINMVGSFR CECPVGFFYN
     DKLLVCEDID ECQNGPVCQR NAECINTAGS YRCDCKPGYR FTSTGQCNDR NECQEIPNIC
     SHGQCIDTVG SFYCLCHTGF KTNADQTMCL DINECERDAC GNGTCRNTIG SFNCRCNHGF
     ILSHNNDCID VDECATGNGN LCRNGQCINT VGSFQCQCNE GYEVAPDGRT CVDINECLLD
     PRKCAPGTCQ NLDGSYRCIC PPGYSLQNDK CEDIDECVEE PEICALGTCS NTEGSFKCLC
     PDGFSLSSTG RRCQDLRMSY CYAKFEGGKC SSPKSRNHSK QECCCALKGE GWGDPCELCP
     TEPDEAFRQI CPYGSGIIVG PDDSAVDMDE CKEPDVCKHG QCINTDGSYR CECPFGYILQ
     GNECVDTDEC SVGNPCGNGT CKNVIGGFEC TCEEGFEPGP MMTCEDINEC AQNPLLCAFR
     CVNTYGSYEC KCPAGYVLRE DRRMCKDEDE CEEGKHDCAE KQMECKNLIG TYLCICGPGY
     QRRPDGEGCV DENECQTKPG ICENGRCLNT RGSYTCECND GFTASPNQDE CLDNREGYCF
     TEVLQNMCQI GSSNRNPVTK SECCCDGGRG WGPHCEICPF QGTVAFKKLC PHGRGFMTNG
     ADIDECKVIH DVCRNGECVN DRGSYHCICK TGYTPDITGT ACVDLNECNQ APKPCNFICK
     NTEGSYQCSC PKGYILQEDG RSCKDLDECA TKQHNCQFLC VNTIGSFTCK CPPGFTQHHT
     ACIDNNECTS DINLCGSKGI CQNTPGSFTC ECQRGFSLDP SGASCEDVDE CEGNHRCQHG
     CQNIIGGYRC SCPQGYLQHY QWNQCVDENE CLSAHICGGA SCHNTLGSYK CMCPAGFQYE
     QFSGGCQDIN ECGSAQAPCS YGCSNTEGGY LCACPPGYFR IGQGHCVSGM GMGRGNPEPP
     ASGEMDDNSL SPEACYECKI NGYPKRGRKR RSANETDASN IEDQPEIEAN VSLASWDVEK
     TAVFAFNISH ISNKVRILEL LPALTTLTNH NRYLIESGNE NGFFKINQKE GISYLHFTKK
     KPVAGTYSLQ ISSTPLYKKK ELNQLEDKYD KDYLSGELGD NLKMKIQILL H
//
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