GenomeNet

Database: UniProt
Entry: A2RUV0
LinkDB: A2RUV0
Original site: A2RUV0 
ID   NOTC1_XENTR             Reviewed;        2522 AA.
AC   A2RUV0; F7CY31;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 2.
DT   10-APR-2019, entry version 84.
DE   RecName: Full=Neurogenic locus notch homolog protein 1;
DE            Short=Notch 1;
DE   Contains:
DE     RecName: Full=Notch 1 extracellular truncation;
DE              Short=NEXT;
DE   Contains:
DE     RecName: Full=Notch 1 intracellular domain;
DE              Short=NICD;
DE   Flags: Precursor;
GN   Name=notch1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L.,
RA   Blitz I.L., Blumberg B., Dichmann D.S., Dubchak I., Amaya E.,
RA   Detter J.C., Fletcher R., Gerhard D.S., Goodstein D., Graves T.,
RA   Grigoriev I.V., Grimwood J., Kawashima T., Lindquist E., Lucas S.M.,
RA   Mead P.E., Mitros T., Ogino H., Ohta Y., Poliakov A.V., Pollet N.,
RA   Robert J., Salamov A., Sater A.K., Schmutz J., Terry A., Vize P.D.,
RA   Warren W.C., Wells D., Wills A., Wilson R.K., Zimmerman L.B.,
RA   Zorn A.M., Grainger R., Grammer T., Khokha M.K., Richardson P.M.,
RA   Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, AND GLYCOSYLATION AT THR-231 AND THR-1400.
RX   PubMed=24226769; DOI=10.1038/nature12723;
RA   Boskovski M.T., Yuan S., Pedersen N.B., Goth C.K., Makova S.,
RA   Clausen H., Brueckner M., Khokha M.K.;
RT   "The heterotaxy gene GALNT11 glycosylates Notch to orchestrate cilia
RT   type and laterality.";
RL   Nature 504:456-459(2013).
CC   -!- FUNCTION: Functions as a receptor for membrane-bound ligands
CC       Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate
CC       cell-fate determination. Upon ligand activation through the
CC       released notch intracellular domain (NICD) it forms a
CC       transcriptional activator complex with RBPJ/RBPSUH and activates
CC       genes of the enhancer of split locus. Affects the implementation
CC       of differentiation, proliferation and apoptotic programs. Involved
CC       in angiogenesis; negatively regulates endothelial cell
CC       proliferation and migration and angiogenic sprouting. Involved in
CC       the maturation of both CD4(+) and CD8(+) cells in the thymus.
CC       Important for follicular differentiation and possibly cell fate
CC       selection within the follicle. During cerebellar development,
CC       functions as a receptor for neuronal DNER and is involved in the
CC       differentiation of Bergmann glia. Represses neuronal and myogenic
CC       differentiation. May play an essential role in postimplantation
CC       development, probably in some aspect of cell specification and/or
CC       differentiation. May be involved in mesoderm development, somite
CC       formation and neurogenesis (By similarity). Involved in
CC       determination of left/right symmetry by modulating the balance
CC       between motile and immotile (sensory) cilia at the left-right
CC       organiser (LRO). {ECO:0000250|UniProtKB:Q01705,
CC       ECO:0000269|PubMed:24226769}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:Q01705}; Single-pass type I membrane
CC       protein {ECO:0000250|UniProtKB:Q01705}.
CC   -!- SUBCELLULAR LOCATION: Notch 1 intracellular domain: Nucleus
CC       {ECO:0000250|UniProtKB:Q01705}. Note=Following proteolytical
CC       processing NICD is translocated to the nucleus.
CC       {ECO:0000250|UniProtKB:Q01705}.
CC   -!- PTM: O-glycosylated on the EGF-like domains. Contains both O-
CC       linked fucose and O-linked glucose. O-linked glycosylation by
CC       galnt11 is involved in determination of left/right symmetry:
CC       glycosylation promotes activation of notch1, possibly by promoting
CC       cleavage by adam17, modulating the balance between motile and
CC       immotile (sensory) cilia at the left-right organiser (LRO).
CC       {ECO:0000269|PubMed:24226769}.
CC   -!- PTM: Synthesized in the endoplasmic reticulum as an inactive form
CC       which is proteolytically cleaved by a furin-like convertase in the
CC       trans-Golgi network before it reaches the plasma membrane to yield
CC       an active, ligand-accessible form. Cleavage results in a C-
CC       terminal fragment N(TM) and a N-terminal fragment N(EC). Following
CC       ligand binding, it is cleaved by adam17 to yield a membrane-
CC       associated intermediate fragment called notch extracellular
CC       truncation (NEXT). Following endocytosis, this fragment is then
CC       cleaved by presenilin dependent gamma-secretase to release a
CC       Notch-derived peptide containing the intracellular domain (NICD)
CC       from the membrane (By similarity). {ECO:0000250|UniProtKB:Q01705}.
CC   -!- SIMILARITY: Belongs to the NOTCH family. {ECO:0000305}.
DR   EMBL; AAMC01043423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAMC01043424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAMC01043425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAMC01043426; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC133053; AAI33054.1; -; mRNA.
DR   RefSeq; NP_001090757.1; NM_001097288.1.
DR   UniGene; Str.51150; -.
DR   UniGene; Str.59603; -.
DR   SMR; A2RUV0; -.
DR   STRING; 8364.ENSXETP00000001676; -.
DR   PaxDb; A2RUV0; -.
DR   GeneID; 100037842; -.
DR   KEGG; xtr:100037842; -.
DR   CTD; 4851; -.
DR   Xenbase; XB-GENE-479318; notch1.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; ENOG410XP6K; LUCA.
DR   HOVERGEN; HBG052650; -.
DR   KO; K02599; -.
DR   OrthoDB; 7525at2759; -.
DR   TreeFam; TF351641; -.
DR   Proteomes; UP000008143; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR   GO; GO:0061314; P:Notch signaling involved in heart development; IMP:UniProtKB.
DR   GO; GO:0050793; P:regulation of developmental process; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00204; ANK; 2.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR024600; DUF3454_notch.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR008297; Notch.
DR   InterPro; IPR035993; Notch-like_dom_sf.
DR   InterPro; IPR022362; Notch_1.
DR   InterPro; IPR000800; Notch_dom.
DR   InterPro; IPR010660; Notch_NOD_dom.
DR   InterPro; IPR011656; Notch_NODP_dom.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF11936; DUF3454; 1.
DR   Pfam; PF00008; EGF; 29.
DR   Pfam; PF07645; EGF_CA; 3.
DR   Pfam; PF12661; hEGF; 1.
DR   Pfam; PF06816; NOD; 1.
DR   Pfam; PF07684; NODP; 1.
DR   Pfam; PF00066; Notch; 3.
DR   PIRSF; PIRSF002279; Notch; 1.
DR   PRINTS; PR01452; LNOTCHREPEAT.
DR   PRINTS; PR01984; NOTCH1.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM01334; DUF3454; 1.
DR   SMART; SM00181; EGF; 36.
DR   SMART; SM00179; EGF_CA; 33.
DR   SMART; SM00004; NL; 3.
DR   SMART; SM01338; NOD; 1.
DR   SMART; SM01339; NODP; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF57184; SSF57184; 6.
DR   SUPFAM; SSF90193; SSF90193; 3.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 23.
DR   PROSITE; PS00022; EGF_1; 34.
DR   PROSITE; PS01186; EGF_2; 29.
DR   PROSITE; PS50026; EGF_3; 36.
DR   PROSITE; PS01187; EGF_CA; 22.
DR   PROSITE; PS50258; LNR; 4.
PE   1: Evidence at protein level;
KW   Activator; Angiogenesis; ANK repeat; Calcium; Cell membrane;
KW   Complete proteome; Developmental protein; Differentiation;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW   Metal-binding; Notch signaling pathway; Nucleus; Receptor;
KW   Reference proteome; Repeat; Signal; Transcription;
KW   Transcription regulation; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20   2522       Neurogenic locus notch homolog protein 1.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000425209.
FT   CHAIN      1715   2522       Notch 1 extracellular truncation.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000425210.
FT   CHAIN      1749   2522       Notch 1 intracellular domain.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000425211.
FT   TOPO_DOM     20   1730       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1731   1751       Helical. {ECO:0000250|UniProtKB:P46531}.
FT   TOPO_DOM   1752   2522       Cytoplasmic. {ECO:0000305}.
FT   DOMAIN       20     57       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       58     99       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      102    140       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      141    177       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      179    215       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      217    254       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      256    292       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      294    332       EGF-like 8; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      334    370       EGF-like 9; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      371    409       EGF-like 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      411    449       EGF-like 11; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      451    487       EGF-like 12; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      489    525       EGF-like 13; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      527    563       EGF-like 14; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      565    600       EGF-like 15; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      602    638       EGF-like 16; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      640    675       EGF-like 17; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      677    713       EGF-like 18; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      715    750       EGF-like 19; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      752    788       EGF-like 20; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      790    826       EGF-like 21; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      828    866       EGF-like 22. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      868    904       EGF-like 23; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      906    942       EGF-like 24; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      944    980       EGF-like 25; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      982   1018       EGF-like 26. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1020   1056       EGF-like 27; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1058   1094       EGF-like 28. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1105   1142       EGF-like 29. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1144   1180       EGF-like 30; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1182   1218       EGF-like 31; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1220   1264       EGF-like 32; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1266   1304       EGF-like 33. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1306   1345       EGF-like 34. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1347   1383       EGF-like 35. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1386   1424       EGF-like 36. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT     1447   1487       LNR 1.
FT   REPEAT     1488   1529       LNR 2.
FT   REPEAT     1530   1564       LNR 3.
FT   REPEAT     1877   1920       ANK 1.
FT   REPEAT     1925   1954       ANK 2.
FT   REPEAT     1958   1988       ANK 3.
FT   REPEAT     1992   2021       ANK 4.
FT   REPEAT     2025   2054       ANK 5.
FT   REPEAT     2058   2087       ANK 6.
FT   METAL       431    431       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   METAL       434    434       Calcium 1; via amide nitrogen.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   METAL       451    451       Calcium 2.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   METAL       452    452       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   METAL       454    454       Calcium 2.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   METAL       468    468       Calcium 2.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   METAL       469    469       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   METAL       489    489       Calcium 3.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   METAL       490    490       Calcium 3; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   METAL       492    492       Calcium 3.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   METAL       506    506       Calcium 3.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   METAL       507    507       Calcium 3; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   METAL      1458   1458       Calcium 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00525}.
FT   METAL      1473   1473       Calcium 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00525}.
FT   METAL      1476   1476       Calcium 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00525}.
FT   METAL      1500   1500       Calcium 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00525}.
FT   METAL      1515   1515       Calcium 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00525}.
FT   METAL      1518   1518       Calcium 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00525}.
FT   METAL      1540   1540       Calcium 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00525}.
FT   METAL      1555   1555       Calcium 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00525}.
FT   METAL      1558   1558       Calcium 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00525}.
FT   SITE       1658   1659       Cleavage; by furin-like protease.
FT                                {ECO:0000250|UniProtKB:Q01705}.
FT   SITE       1714   1715       Cleavage; by adam17.
FT                                {ECO:0000250|UniProtKB:Q01705}.
FT   CARBOHYD    231    231       O-linked (Fuc...) threonine; alternate.
FT                                {ECO:0000250|UniProtKB:Q01705}.
FT   CARBOHYD    231    231       O-linked (GalNAc...) threonine;
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:Q01705}.
FT   CARBOHYD    434    434       O-linked (Glc...) serine.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   CARBOHYD    457    457       O-linked (Glc...) serine.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   CARBOHYD    465    465       O-linked (Fuc...) threonine.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   CARBOHYD    495    495       O-linked (Glc...) serine.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   CARBOHYD    887    887       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    958    958       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1178   1178       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1400   1400       O-linked (Fuc...) threonine; alternate.
FT                                {ECO:0000250|UniProtKB:Q01705}.
FT   CARBOHYD   1400   1400       O-linked (GalNAc...) threonine;
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:Q01705}.
FT   CARBOHYD   1487   1487       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1508   1508       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1584   1584       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     22     35       {ECO:0000250}.
FT   DISULFID     29     45       {ECO:0000250}.
FT   DISULFID     47     56       {ECO:0000250}.
FT   DISULFID     62     74       {ECO:0000250}.
FT   DISULFID     68     87       {ECO:0000250}.
FT   DISULFID     89     98       {ECO:0000250}.
FT   DISULFID    106    117       {ECO:0000250}.
FT   DISULFID    111    128       {ECO:0000250}.
FT   DISULFID    130    139       {ECO:0000250}.
FT   DISULFID    145    156       {ECO:0000250}.
FT   DISULFID    150    165       {ECO:0000250}.
FT   DISULFID    167    176       {ECO:0000250}.
FT   DISULFID    183    194       {ECO:0000250}.
FT   DISULFID    188    203       {ECO:0000250}.
FT   DISULFID    205    214       {ECO:0000250}.
FT   DISULFID    221    232       {ECO:0000250}.
FT   DISULFID    226    242       {ECO:0000250}.
FT   DISULFID    244    253       {ECO:0000250}.
FT   DISULFID    260    271       {ECO:0000250}.
FT   DISULFID    265    280       {ECO:0000250}.
FT   DISULFID    282    291       {ECO:0000250}.
FT   DISULFID    298    311       {ECO:0000250}.
FT   DISULFID    305    320       {ECO:0000250}.
FT   DISULFID    322    331       {ECO:0000250}.
FT   DISULFID    338    349       {ECO:0000250}.
FT   DISULFID    343    358       {ECO:0000250}.
FT   DISULFID    360    369       {ECO:0000250}.
FT   DISULFID    375    386       {ECO:0000250}.
FT   DISULFID    380    397       {ECO:0000250}.
FT   DISULFID    399    408       {ECO:0000250}.
FT   DISULFID    415    428       {ECO:0000250|UniProtKB:Q07008}.
FT   DISULFID    422    437       {ECO:0000250|UniProtKB:Q07008}.
FT   DISULFID    439    448       {ECO:0000250|UniProtKB:Q07008}.
FT   DISULFID    455    466       {ECO:0000250|UniProtKB:Q07008}.
FT   DISULFID    460    475       {ECO:0000250|UniProtKB:Q07008}.
FT   DISULFID    477    486       {ECO:0000250|UniProtKB:Q07008}.
FT   DISULFID    493    504       {ECO:0000250|UniProtKB:Q07008}.
FT   DISULFID    498    513       {ECO:0000250|UniProtKB:Q07008}.
FT   DISULFID    515    524       {ECO:0000250|UniProtKB:Q07008}.
FT   DISULFID    531    542       {ECO:0000250}.
FT   DISULFID    536    551       {ECO:0000250}.
FT   DISULFID    553    562       {ECO:0000250}.
FT   DISULFID    569    579       {ECO:0000250}.
FT   DISULFID    574    588       {ECO:0000250}.
FT   DISULFID    590    599       {ECO:0000250}.
FT   DISULFID    606    617       {ECO:0000250}.
FT   DISULFID    611    626       {ECO:0000250}.
FT   DISULFID    628    637       {ECO:0000250}.
FT   DISULFID    644    654       {ECO:0000250}.
FT   DISULFID    649    663       {ECO:0000250}.
FT   DISULFID    665    674       {ECO:0000250}.
FT   DISULFID    681    692       {ECO:0000250}.
FT   DISULFID    686    701       {ECO:0000250}.
FT   DISULFID    703    712       {ECO:0000250}.
FT   DISULFID    719    729       {ECO:0000250}.
FT   DISULFID    724    738       {ECO:0000250}.
FT   DISULFID    740    749       {ECO:0000250}.
FT   DISULFID    756    767       {ECO:0000250}.
FT   DISULFID    761    776       {ECO:0000250}.
FT   DISULFID    778    787       {ECO:0000250}.
FT   DISULFID    794    805       {ECO:0000250}.
FT   DISULFID    799    814       {ECO:0000250}.
FT   DISULFID    816    825       {ECO:0000250}.
FT   DISULFID    832    843       {ECO:0000250}.
FT   DISULFID    837    854       {ECO:0000250}.
FT   DISULFID    856    865       {ECO:0000250}.
FT   DISULFID    872    883       {ECO:0000250}.
FT   DISULFID    877    892       {ECO:0000250}.
FT   DISULFID    894    903       {ECO:0000250}.
FT   DISULFID    910    921       {ECO:0000250}.
FT   DISULFID    915    930       {ECO:0000250}.
FT   DISULFID    932    941       {ECO:0000250}.
FT   DISULFID    948    959       {ECO:0000250}.
FT   DISULFID    953    968       {ECO:0000250}.
FT   DISULFID    970    979       {ECO:0000250}.
FT   DISULFID    986    997       {ECO:0000250}.
FT   DISULFID    991   1006       {ECO:0000250}.
FT   DISULFID   1008   1017       {ECO:0000250}.
FT   DISULFID   1024   1035       {ECO:0000250}.
FT   DISULFID   1029   1044       {ECO:0000250}.
FT   DISULFID   1046   1055       {ECO:0000250}.
FT   DISULFID   1062   1073       {ECO:0000250}.
FT   DISULFID   1067   1082       {ECO:0000250}.
FT   DISULFID   1084   1093       {ECO:0000250}.
FT   DISULFID   1115   1130       {ECO:0000250}.
FT   DISULFID   1132   1141       {ECO:0000250}.
FT   DISULFID   1148   1159       {ECO:0000250}.
FT   DISULFID   1153   1168       {ECO:0000250}.
FT   DISULFID   1170   1179       {ECO:0000250}.
FT   DISULFID   1186   1197       {ECO:0000250}.
FT   DISULFID   1191   1206       {ECO:0000250}.
FT   DISULFID   1208   1217       {ECO:0000250}.
FT   DISULFID   1224   1243       {ECO:0000250}.
FT   DISULFID   1237   1252       {ECO:0000250}.
FT   DISULFID   1254   1263       {ECO:0000250}.
FT   DISULFID   1270   1283       {ECO:0000250}.
FT   DISULFID   1275   1292       {ECO:0000250}.
FT   DISULFID   1294   1303       {ECO:0000250}.
FT   DISULFID   1310   1321       {ECO:0000250}.
FT   DISULFID   1315   1333       {ECO:0000250}.
FT   DISULFID   1335   1344       {ECO:0000250}.
FT   DISULFID   1351   1362       {ECO:0000250}.
FT   DISULFID   1356   1371       {ECO:0000250}.
FT   DISULFID   1373   1382       {ECO:0000250}.
FT   DISULFID   1390   1401       {ECO:0000250}.
FT   DISULFID   1395   1412       {ECO:0000250}.
FT   DISULFID   1414   1423       {ECO:0000250}.
FT   DISULFID   1447   1470       {ECO:0000250}.
FT   DISULFID   1452   1465       {ECO:0000250}.
FT   DISULFID   1461   1477       {ECO:0000250}.
FT   DISULFID   1488   1512       {ECO:0000250}.
FT   DISULFID   1494   1507       {ECO:0000250}.
FT   DISULFID   1503   1519       {ECO:0000250}.
FT   DISULFID   1534   1547       {ECO:0000250}.
FT   DISULFID   1543   1559       {ECO:0000250}.
FT   CONFLICT    527    527       D -> H (in Ref. 2; AAI33054).
FT                                {ECO:0000305}.
FT   CONFLICT   1015   1015       N -> D (in Ref. 2; AAI33054).
FT                                {ECO:0000305}.
FT   CONFLICT   1244   1244       F -> I (in Ref. 2; AAI33054).
FT                                {ECO:0000305}.
FT   CONFLICT   2239   2239       L -> P (in Ref. 2; AAI33054).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2522 AA;  274530 MW;  1425E154A4BC5BCD CRC64;
     MYRIGLLVLI WSLLGLAQGL RCTQTAEMCL NGGRCEMTPG GTGVCLCSSS YFGERCQYPN
     PCALKNQCMN FGTCEPVLLG NAIDFTCHCP VGFTDKVCLT PVDNACVNNP CRNGGTCELL
     SSVSDYRCRC PPGWTGDSCQ QADPCASNPC ANGGKCLPFE TQYICKCPSG FHGATCKQDI
     NECSQNPCRN GGQCLNEFGS YRCNCQNRFT GRNCEEPYVP CNPSPCLNGG TCRQTDDTSY
     ECTCLPGFSG QNCEENIDDC PSNNCRNGGT CVDGVNTYNC QCPPDWTGQY CTEDVDECQL
     MPNACQNGGT CHNTYGGYNC VCVNGWTGED CSENIDDCAN AACHSGATCH DRVASFFCEC
     PHGRTGLLCH LDNACISNPC NEGSNCDTNP VNGKAICTCP PGYTGPACNN DVDECSLGAN
     PCEHGGRCTN TLGSFQCNCP QGYAGPRCEI DVNECLSNPC QNDATCLDQI GEFQCICMPG
     YEGLYCETNI DECASNPCLH NGKCVDKINE FHCECPTGFN GNLCQHDVDE CASTPCKNGA
     KCLDGPNSYT CQCTEGFTGR HCEQDINECI PDPCHYGTCK DGIATFTCLC RPGYTGRLCD
     NDINECLSQP CQNGGQCTDR ENGYICTCPK GTTGVNCETN LDDCASNPCD YGKCIDKIDG
     YECTCEPGYT GKMCNINIDE CASNPCRNGG TCKDKINGFT CVCPDGYHDH MCLSEVNECN
     SNPCIHGTCH DGINGYKCDC DAGWSGSNCD VNNNECESNP CMNGGTCKDM TGAYICTCRA
     GFSGPNCQTN INECASNPCL NRGTCIDDVA GYKCNCMLPY TGAICEAVLA PCSGSPCKNG
     GRCKESEDYE TFSCECPPGW QGQTCEIDMN ECVNRPCRNG AMCQNTNGSY KCNCKPGYAG
     RHCETDIDDC QPNPCHNGGS CSDGINMFFC NCPAGFRGPK CEEDINECAS NPCKNGANCT
     DCVNSYTCTC QPGFSGIHCE NNTPDCTESS CFNGGTCIDG INTFSCQCPP GFTGNYCQHD
     INECDSKPCL NGGTCQDSYG AYKCTCPQGY TGLNCQNLVR WCDSSPCKNG GKCWQTNNFY
     RCECKSGWTG VYCDVPSVSC EVAAKQQGVD IAHLCRNSGM CVDTGNTHFC RCQAGYTGSY
     CEEQVDECSP NPCQNGATCT DYLGGYSCEC VAGYHGVNCS EEINECLSHP CHNGGTCIDL
     INTYKCSCPR GTQGVHCEIN VDDCTPFYDS VSLEPKCFNN GKCFDRVGGY NCICPPGFVG
     ERCEGDVNEC LSNPCDPRGT QNCIQLVNDY RCECRQGFTG RRCDSVVDGC KGLPCRNGGT
     CAVASNTERG FICKCPPGFD GATCEYDART CGNLRCQNGG TCISVLKSSK CVCSEGYTGA
     TCQYPVVSPC ASRPCYNGGT CQFSPEEPFF QCFCPTNFNG LFCHILDYGF IGGLGKNITP
     PDNEEICENE QCAELADNKI CNANCNNHAC GWDGGDCSLN FNDPWKNCTQ SLQCWKYFND
     GKCDSQCNNS GCLYDGFDCQ KVEVQCNPLY DQYCRDHFQD GHCDQGCNNA ECEWDGLDCD
     NMPENLAEGT LLIVVLMPPE KLKNNSVNFL RELSRVLHTN VVFKKDSKGE YKIYPYYGNE
     EELKKHHIKK RSAASWSDAP TAIFSTMKES VLPGRRRREL DQMEVRGSIV YLEIDNRQCY
     KSSSQCFTSA TDVAAFLGAL ATHGNLNIPY KIEAVKSEIV ETAKPPPPLY AMFSMLVIPL
     LIIFVIMVVI VNKKRRREHG QLWFPEGFIP KEPSKKKRRE PLGEDSVGLK PLKNLTDGSF
     MDDNQNEWGD EETLENKRFR FEEQVMLPEL VDDQTDHRQW TQQHLDAADL RIPSMAPTPP
     QGEIDADCMD VNVRGPDGFT PLMIAACSGG GLETGNSEEE EDASANMISD FIGQGAQLHN
     QTDRTGETAL HLAARYARAD AAKRLLESSA DANVPDNMGR TPLHAAVAAD AQGVFQILIR
     NRATDLDARM CDGTTPLILA ARLAVEGMVE ELINAHADVN AVDEFGKSAL HWAAAVNNVD
     AAAVLLKSSA NKDMQNNKEE TPLFLAAREG SYETAKVLLD HYANRDITDH MDRLPRDIAQ
     ERMHHDIVHL LDEHNLVKSP TLHGGPLGAP TLSPPICSPN GYMGNMKPSV QSKKARKPSI
     KGNGCKEAKE LKARRKKSQD GKTSLLDSGS SGVLSPVDSL ESPHGYLSDV ASPPLMTSPF
     QQSPSMPLNH LTSMQDSHLG LNHMTMANKQ EMASNRMAFD GMTPRLTHLN VSSPNTIMTN
     GSMHFTVGGA PAMNGQCDWF ARLQNGMVQN QYNPIRNGIQ QGNAQQALQH GLMSSLHNGL
     PATTLSQMMT YQAMPNTRMA NQPHLMQAQQ MQQQQNLQLH QSVQQQQHQN SNATSTHIGS
     PFCSNDISQT DLQQMSGNNI HSVMPQDTQI FTNSLPPTLT QSMATTQFLT PPSQHSYSSP
     MDNTPSHQLQ VPDHPFLTPS PESPDQWSSS SPHSNMSDWS EGISSPPTSM QPQRTHIPEA
     FK
//
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