GenomeNet

Database: UniProt
Entry: Q08879
LinkDB: Q08879
Original site: Q08879 
ID   FBLN1_MOUSE             Reviewed;         705 AA.
AC   Q08879; Q08878; Q8C3B1; Q91ZC9; Q922K8;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   09-MAY-2003, sequence version 2.
DT   13-FEB-2019, entry version 186.
DE   RecName: Full=Fibulin-1;
DE            Short=FIBL-1;
DE   AltName: Full=Basement-membrane protein 90;
DE            Short=BM-90;
DE   Flags: Precursor;
GN   Name=Fbln1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS C AND D), AND LIGANDS
RP   INTERACTION.
RX   PubMed=8354280; DOI=10.1111/j.1432-1033.1993.tb18086.x;
RA   Pan T.-C., Kluge M., Zhang R.Z., Mayer U., Timpl R., Chu M.-L.;
RT   "Sequence of extracellular mouse protein BM-90/fibulin and its
RT   calcium-dependent binding to other basement-membrane ligands.";
RL   Eur. J. Biochem. 215:733-740(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC   STRAIN=C57BL/6J; TISSUE=Head, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RX   PubMed=11829738; DOI=10.1042/0264-6021:3620041;
RA   Castoldi M., Chu M.-L.;
RT   "Structural and functional characterization of the human and mouse
RT   fibulin-1 gene promoters: role of Sp1 and Sp3.";
RL   Biochem. J. 362:41-50(2002).
RN   [5]
RP   PROTEIN SEQUENCE OF 30-53; 110-117; 231-243; 339-387; 434-439;
RP   469-476; 553-563 AND 574-581.
RX   PubMed=2249686; DOI=10.1111/j.1432-1033.1990.tb19383.x;
RA   Kluge M., Mann K., Dziadek M., Timpl R.;
RT   "Characterization of a novel calcium-binding 90-kDa glycoprotein (BM-
RT   90) shared by basement membranes and serum.";
RL   Eur. J. Biochem. 193:651-659(1990).
RN   [6]
RP   CHARACTERIZATION OF NID AFFINITY.
RX   PubMed=7844816; DOI=10.1006/jmbi.1994.0020;
RA   Sasaki T., Kostka G., Goehring W., Wiedemann H., Mann K., Chu M.-L.,
RA   Timpl R.;
RT   "Structural characterization of two variants of fibulin-1 that differ
RT   in nidogen affinity.";
RL   J. Mol. Biol. 245:241-250(1995).
RN   [7]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=8850569;
RX   DOI=10.1002/(SICI)1097-0177(199603)205:3<348::AID-AJA13>3.0.CO;2-0;
RA   Zhang H.-Y., Timpl R., Sasaki T., Chu M.-L., Ekblom P.;
RT   "Fibulin-1 and fibulin-2 expression during organogenesis in the
RT   developing mouse embryo.";
RL   Dev. Dyn. 205:348-364(1996).
RN   [8]
RP   NID-BINDING SITE.
RC   STRAIN=129/Sv;
RX   PubMed=9299350; DOI=10.1006/jmbi.1997.1244;
RA   Adam S., Goehring W., Wiedemann H., Chu M.-L., Timpl R., Kostka G.;
RT   "Binding of fibulin-1 to nidogen depends on its C-terminal globular
RT   domain and a specific array of calcium-binding epidermal growth
RT   factor-like (EG) modules.";
RL   J. Mol. Biol. 272:226-236(1997).
RN   [9]
RP   INTERACTION WITH LAMA2.
RX   PubMed=10022829; DOI=10.1093/emboj/18.4.863;
RA   Talts J.F., Andac Z., Goehring W., Brancaccio A., Timpl R.;
RT   "Binding of the G domains of laminin alpha1 and alpha2 chains and
RT   perlecan to heparin, sulfatides, alpha-dystroglycan and several
RT   extracellular matrix proteins.";
RL   EMBO J. 18:863-870(1999).
RN   [10]
RP   INTERACTION WITH ACAN AND CSPG2.
RX   PubMed=10400671; DOI=10.1074/jbc.274.29.20444;
RA   Aspberg A., Adam S., Kostka G., Timpl R., Heinegaard D.;
RT   "Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and
RT   versican.";
RL   J. Biol. Chem. 274:20444-20449(1999).
RN   [11]
RP   INTERACTION WITH NID.
RX   PubMed=11589703; DOI=10.1046/j.0014-2956.2001.02437.x;
RA   Ries A., Goehring W., Fox J.W., Timpl R., Sasaki T.;
RT   "Recombinant domains of mouse nidogen-1 and their binding to basement
RT   membrane proteins and monoclonal antibodies.";
RL   Eur. J. Biochem. 268:5119-5128(2001).
RN   [12]
RP   DOWN-REGULATION BY GLUCOCORTICOIDS.
RX   PubMed=11737251; DOI=10.1034/j.1600-0609.2001.5790528.x;
RA   Gu Y.-C., Talts J.F., Gullberg D., Timpl R., Ekblom M.;
RT   "Glucocorticoids down-regulate the extracellular matrix proteins
RT   fibronectin, fibulin-1 and fibulin-2 in bone marrow stroma.";
RL   Eur. J. Haematol. 67:176-184(2001).
RN   [13]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=11238726; DOI=10.1046/j.1471-4159.2001.00144.x;
RA   Ohsawa I., Takamura C., Kohsaka S.;
RT   "Fibulin-1 binds the amino-terminal head of beta-amyloid precursor
RT   protein and modulates its physiological function.";
RL   J. Neurochem. 76:1411-1420(2001).
RN   [14]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=11836357; DOI=10.1136/jmg.39.2.98;
RA   Debeer P., Schoenmakers E.F.P.M., Twal W.O., Argraves W.S.,
RA   De Smet L., Fryns J.-P., Van De Ven W.J.M.;
RT   "The fibulin-1 gene (FBLN1) is disrupted in a t(12;22) associated with
RT   a complex type of synpolydactyly.";
RL   J. Med. Genet. 39:98-104(2002).
RN   [15]
RP   INTERACTION WITH FBLN7.
RX   PubMed=17699513; DOI=10.1074/jbc.M705847200;
RA   de Vega S., Iwamoto T., Nakamura T., Hozumi K., McKnight D.A.,
RA   Fisher L.W., Fukumoto S., Yamada Y.;
RT   "TM14 is a new member of the fibulin family (fibulin-7) that interacts
RT   with extracellular matrix molecules and is active for cell binding.";
RL   J. Biol. Chem. 282:30878-30888(2007).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Incorporated into fibronectin-containing matrix fibers.
CC       May play a role in cell adhesion and migration along protein
CC       fibers within the extracellular matrix (ECM). Could be important
CC       for certain developmental processes and contribute to the
CC       supramolecular organization of ECM architecture, in particular to
CC       those of basement membranes.
CC   -!- SUBUNIT: Homomultimerizes and interacts with various extracellular
CC       matrix components such as FN1, LAMA1, LMA2, NID, ACAN, CSPG2 and
CC       type IV collagen. Binding analysis demonstrated for isoform C a
CC       100-fold stronger binding to the basement membrane protein NID
CC       than for isoform D. Interacts with FBLN7. Interacts with CCN3 (By
CC       similarity). {ECO:0000250|UniProtKB:P23142,
CC       ECO:0000269|PubMed:10022829, ECO:0000269|PubMed:10400671,
CC       ECO:0000269|PubMed:11589703, ECO:0000269|PubMed:17699513}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=D;
CC         IsoId=Q08879-1; Sequence=Displayed;
CC       Name=A;
CC         IsoId=Q08879-3; Sequence=Not described;
CC       Name=B;
CC         IsoId=Q08879-4; Sequence=Not described;
CC       Name=C;
CC         IsoId=Q08879-2; Sequence=VSP_001386;
CC         Note=Ref.1 (CAA50206) sequence is in conflict in position:
CC         571:E->A.;
CC   -!- TISSUE SPECIFICITY: Detected in most organs (brain, heart, lung,
CC       spleen, liver and kidney). Neurons are the predominant source of
CC       production in the brain. Not expressed significantly by astrocytes
CC       or microglia. {ECO:0000269|PubMed:11238726}.
CC   -!- DEVELOPMENTAL STAGE: The differential expression of the fibulin
CC       family contributes to the formation of molecularly distinct
CC       extracellular matrices already during early developmental stages
CC       of a large number of tissues. Increase expression at neonate stage
CC       in the brain. Expressed in interdigital regions of the handplate
CC       of a 12 dpc embryo and in the lateral perichondrial region.
CC       Similar expression persists in the 13 dpc handplate particularly
CC       in the perichondrial regions and apical aspects of the developing
CC       digits. {ECO:0000269|PubMed:11238726, ECO:0000269|PubMed:11836357,
CC       ECO:0000269|PubMed:8850569}.
CC   -!- INDUCTION: Glucocorticoids suppressed mRNA expression and protein
CC       synthesis.
CC   -!- SIMILARITY: Belongs to the fibulin family. {ECO:0000305}.
DR   EMBL; X70854; CAA50207.1; -; mRNA.
DR   EMBL; X70853; CAA50206.1; -; mRNA.
DR   EMBL; AK086451; BAC39669.1; -; mRNA.
DR   EMBL; AK035388; BAC29054.1; -; mRNA.
DR   EMBL; BC007140; AAH07140.1; -; mRNA.
DR   EMBL; AY040588; AAK82944.1; -; Genomic_DNA.
DR   CCDS; CCDS27719.1; -. [Q08879-1]
DR   CCDS; CCDS84186.1; -. [Q08879-2]
DR   PIR; S34968; S34968.
DR   PIR; S78040; S78040.
DR   RefSeq; NP_001334017.1; NM_001347088.1. [Q08879-2]
DR   RefSeq; NP_034310.2; NM_010180.2. [Q08879-1]
DR   UniGene; Mm.297992; -.
DR   ProteinModelPortal; Q08879; -.
DR   SMR; Q08879; -.
DR   BioGrid; 199605; 1.
DR   IntAct; Q08879; 2.
DR   MINT; Q08879; -.
DR   STRING; 10090.ENSMUSP00000054583; -.
DR   PhosphoSitePlus; Q08879; -.
DR   PaxDb; Q08879; -.
DR   PeptideAtlas; Q08879; -.
DR   PRIDE; Q08879; -.
DR   Ensembl; ENSMUST00000057410; ENSMUSP00000054583; ENSMUSG00000006369. [Q08879-1]
DR   Ensembl; ENSMUST00000109432; ENSMUSP00000105058; ENSMUSG00000006369. [Q08879-2]
DR   GeneID; 14114; -.
DR   KEGG; mmu:14114; -.
DR   UCSC; uc007xdb.2; mouse. [Q08879-2]
DR   UCSC; uc011zxk.1; mouse. [Q08879-1]
DR   CTD; 2192; -.
DR   MGI; MGI:95487; Fbln1.
DR   eggNOG; ENOG410IR7F; Eukaryota.
DR   eggNOG; ENOG410Y194; LUCA.
DR   GeneTree; ENSGT00940000156642; -.
DR   HOGENOM; HOG000007079; -.
DR   HOVERGEN; HBG051559; -.
DR   InParanoid; Q08879; -.
DR   KO; K17307; -.
DR   OMA; CHENQEC; -.
DR   OrthoDB; 1174178at2759; -.
DR   PhylomeDB; Q08879; -.
DR   TreeFam; TF317514; -.
DR   Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR   PRO; PR:Q08879; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   Bgee; ENSMUSG00000006369; Expressed in 297 organ(s), highest expression level in ear vesicle.
DR   ExpressionAtlas; Q08879; baseline and differential.
DR   Genevisible; Q08879; MM.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0071953; C:elastic fiber; ISO:MGI.
DR   GO; GO:0031012; C:extracellular matrix; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR   GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
DR   GO; GO:0070051; F:fibrinogen binding; ISO:MGI.
DR   GO; GO:0001968; F:fibronectin binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0005178; F:integrin binding; ISO:MGI.
DR   GO; GO:0016504; F:peptidase activator activity; IDA:MGI.
DR   GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0072378; P:blood coagulation, fibrin clot formation; ISO:MGI.
DR   GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR   GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR   GO; GO:0007162; P:negative regulation of cell adhesion; ISO:MGI.
DR   GO; GO:2000146; P:negative regulation of cell motility; ISO:MGI.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR   GO; GO:2000647; P:negative regulation of stem cell proliferation; ISO:MGI.
DR   GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR   GO; GO:1904188; P:negative regulation of transformation of host cell by virus; ISO:MGI.
DR   GO; GO:2001202; P:negative regulation of transforming growth factor-beta secretion; ISO:MGI.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   GO; GO:1904237; P:positive regulation of substrate-dependent cell migration, cell attachment to substrate; ISO:MGI.
DR   CDD; cd00017; ANATO; 2.
DR   InterPro; IPR000020; Anaphylatoxin/fibulin.
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; IPR017048; Fibulin-1.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   Pfam; PF12662; cEGF; 3.
DR   Pfam; PF07645; EGF_CA; 4.
DR   PIRSF; PIRSF036313; Fibulin-1; 1.
DR   SMART; SM00104; ANATO; 3.
DR   SMART; SM00181; EGF; 9.
DR   SMART; SM00179; EGF_CA; 8.
DR   SUPFAM; SSF57184; SSF57184; 3.
DR   PROSITE; PS01177; ANAPHYLATOXIN_1; 3.
DR   PROSITE; PS01178; ANAPHYLATOXIN_2; 3.
DR   PROSITE; PS00010; ASX_HYDROXYL; 4.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS01187; EGF_CA; 8.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Extracellular matrix; Glycoprotein; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL        1     29       {ECO:0000269|PubMed:2249686}.
FT   CHAIN        30    705       Fibulin-1.
FT                                /FTId=PRO_0000007564.
FT   DOMAIN       36     76       Anaphylatoxin-like 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00022}.
FT   DOMAIN       77    111       Anaphylatoxin-like 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00022}.
FT   DOMAIN      112    144       Anaphylatoxin-like 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00022}.
FT   DOMAIN      178    217       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      218    263       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      264    309       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      310    357       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      358    400       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      401    442       EGF-like 6; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      443    482       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      483    526       EGF-like 8; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      527    580       EGF-like 9; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   REGION      358    442       Self-association and FN1-binding.
FT                                {ECO:0000250}.
FT   CARBOHYD     98     98       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    537    537       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    541    541       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     36     61       {ECO:0000250}.
FT   DISULFID     37     68       {ECO:0000250}.
FT   DISULFID     50     69       {ECO:0000250}.
FT   DISULFID     78    109       {ECO:0000250}.
FT   DISULFID     91    110       {ECO:0000250}.
FT   DISULFID    112    136       {ECO:0000250}.
FT   DISULFID    113    143       {ECO:0000250}.
FT   DISULFID    126    144       {ECO:0000250}.
FT   DISULFID    182    192       {ECO:0000250}.
FT   DISULFID    188    201       {ECO:0000250}.
FT   DISULFID    203    216       {ECO:0000250}.
FT   DISULFID    222    235       {ECO:0000250}.
FT   DISULFID    229    244       {ECO:0000250}.
FT   DISULFID    250    262       {ECO:0000250}.
FT   DISULFID    268    281       {ECO:0000250}.
FT   DISULFID    275    290       {ECO:0000250}.
FT   DISULFID    296    308       {ECO:0000250}.
FT   DISULFID    314    327       {ECO:0000250}.
FT   DISULFID    321    336       {ECO:0000250}.
FT   DISULFID    343    356       {ECO:0000250}.
FT   DISULFID    362    375       {ECO:0000250}.
FT   DISULFID    369    384       {ECO:0000250}.
FT   DISULFID    386    399       {ECO:0000250}.
FT   DISULFID    405    417       {ECO:0000250}.
FT   DISULFID    413    426       {ECO:0000250}.
FT   DISULFID    428    441       {ECO:0000250}.
FT   DISULFID    447    456       {ECO:0000250}.
FT   DISULFID    452    465       {ECO:0000250}.
FT   DISULFID    467    481       {ECO:0000250}.
FT   DISULFID    487    500       {ECO:0000250}.
FT   DISULFID    496    509       {ECO:0000250}.
FT   DISULFID    511    525       {ECO:0000250}.
FT   DISULFID    531    544       {ECO:0000250}.
FT   DISULFID    538    553       {ECO:0000250}.
FT   DISULFID    558    579       {ECO:0000250}.
FT   VAR_SEQ     569    705       FRQEKTDTVRCIKSCRPNDEACVRDPVHTVSHTVISLPTFR
FT                                EFTRPEEIIFLRAVTPLYPANQADIIFDITEGNLRDSFDII
FT                                KRYEDGMTVGVVRQVRPIVGPFYAVLKLEMNYVLGGVVSHR
FT                                NVVNVHIFVSEYWF -> RCERLPCHENQECPRLPLRITYY
FT                                HLSFPTNIQVPAVVFRMGPSSAVPGDSMQLAITAGNEEGFF
FT                                TTRKVSHHSGVVALTKPIPEPRDLLLTVKMDLYRHGTVSSF
FT                                VAKLFIFVSAEL (in isoform C).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:16141072,
FT                                ECO:0000303|PubMed:8354280}.
FT                                /FTId=VSP_001386.
FT   CONFLICT     30     30       D -> N (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     40     40       G -> P (in Ref. 1; CAA50207).
FT                                {ECO:0000305}.
FT   CONFLICT    363    363       S -> A (in Ref. 1; CAA50207).
FT                                {ECO:0000305}.
FT   CONFLICT    385    385       E -> K (in Ref. 2; BAC39669).
FT                                {ECO:0000305}.
FT   CONFLICT    553    553       C -> Q (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    558    558       C -> Q (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
SQ   SEQUENCE   705 AA;  78033 MW;  76C527A12E97D0E1 CRC64;
     MERPVPSRLV PLPLLLLSSL SLLAARANAD ISMEACCTDG NQMANQHRDC SLPYTSESKE
     CRMVQEQCCH NQLEELHCAT GINLASEPEG CASLHSYNSS LETIFIKRCC HCCMLGKASL
     ARDQTCEPIV MISYQCGLVF RACCVKAREN SDFVQGNGAD LQDPAKIPDE EDQEDPYLND
     RCRGGGPCKQ QCRDTGDEVI CSCFVGYQLQ SDGVSCEDIN ECITGSHNCR LGESCINTVG
     SFRCQRDSSC GTGYELTEDN NCKDIDECET GIHNCPPDFI CQNTLGSFRC RPKLQCKSGF
     IQDALGNCID INECLSISAP CPVGQTCINT EGSYTCQKNV PNCGRGYHLN EEGTRCVDVD
     ECSPPAEPCG KGHHCLNSPG SFRCECKAGF YFDGISRTCV DINECQRYPG RLCGHKCENT
     PGSFHCSCSA GFRLSVDGRS CEDVNECLNS PCSQECANVY GSYQCYCRRG YQLSDVDGVT
     CEDIDECALP TGGHICSYRC INIPGSFQCS CPSSGYRLAP NGRNCQDIDE CVTGIHNCSI
     NETCFNIQGS FRCLSFECPE NYRRSADTFR QEKTDTVRCI KSCRPNDEAC VRDPVHTVSH
     TVISLPTFRE FTRPEEIIFL RAVTPLYPAN QADIIFDITE GNLRDSFDII KRYEDGMTVG
     VVRQVRPIVG PFYAVLKLEM NYVLGGVVSH RNVVNVHIFV SEYWF
//
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