FBLN1_MOUSE
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 03-AUG-2022, entry version 204.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS C AND D), AND LIGANDS 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 calcium-
RT 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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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 project:
RT 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 fibulin-
RT 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; 469-476;
RP 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-90)
RT 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 in
RT 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 developing
RT 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 domain
RT and a specific array of calcium-binding epidermal growth factor-like (EG)
RT 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 perlecan
RT to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix
RT 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 protein
RT 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., De Smet L.,
RA Fryns J.-P., Van De Ven W.J.M.;
RT "The fibulin-1 gene (FBLN1) is disrupted in a t(12;22) associated with a
RT 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., Fisher L.W.,
RA Fukumoto S., Yamada Y.;
RT "TM14 is a new member of the fibulin family (fibulin-7) that interacts with
RT 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, Spleen,
RC 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 expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Incorporated into fibronectin-containing matrix fibers. May
CC play a role in cell adhesion and migration along protein fibers within
CC the extracellular matrix (ECM). Could be important for certain
CC developmental processes and contribute to the supramolecular
CC organization of ECM architecture, in particular to those of basement
CC membranes.
CC -!- SUBUNIT: Homomultimerizes and interacts with various extracellular
CC matrix components such as FN1, LAMA1, LMA2, NID, ACAN, CSPG2 and type
CC IV collagen. Binding analysis demonstrated for isoform C a 100-fold
CC stronger binding to the basement membrane protein NID than for isoform
CC D. Interacts with FBLN7. Interacts with CCN3 (By similarity).
CC {ECO:0000250|UniProtKB:P23142, ECO:0000269|PubMed:10022829,
CC ECO:0000269|PubMed:10400671, ECO:0000269|PubMed:11589703,
CC 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 -!- 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 or
CC microglia. {ECO:0000269|PubMed:11238726}.
CC -!- DEVELOPMENTAL STAGE: The differential expression of the fibulin family
CC contributes to the formation of molecularly distinct extracellular
CC matrices already during early developmental stages of a large number of
CC tissues. Increased expression at neonate stage in the brain. Expressed
CC in interdigital regions of the handplate of a 12 dpc embryo and in the
CC lateral perichondrial region. Similar expression persists in the 13 dpc
CC handplate particularly in the perichondrial regions and apical aspects
CC of the developing digits. {ECO:0000269|PubMed:11238726,
CC ECO:0000269|PubMed:11836357, ECO:0000269|PubMed:8850569}.
CC -!- INDUCTION: Glucocorticoids suppressed mRNA expression and protein
CC synthesis.
CC -!- SIMILARITY: Belongs to the fibulin family. {ECO:0000305}.
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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 AlphaFoldDB; Q08879; -.
DR BioGRID; 199605; 7.
DR IntAct; Q08879; 1.
DR MINT; Q08879; -.
DR STRING; 10090.ENSMUSP00000054583; -.
DR GlyGen; Q08879; 3 sites.
DR PhosphoSitePlus; Q08879; -.
DR MaxQB; Q08879; -.
DR PaxDb; Q08879; -.
DR PeptideAtlas; Q08879; -.
DR PRIDE; Q08879; -.
DR ProteomicsDB; 271872; -. [Q08879-1]
DR ProteomicsDB; 271873; -. [Q08879-2]
DR Antibodypedia; 886; 329 antibodies from 34 providers.
DR DNASU; 14114; -.
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 VEuPathDB; HostDB:ENSMUSG00000006369; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000156642; -.
DR HOGENOM; CLU_004826_1_1_1; -.
DR InParanoid; Q08879; -.
DR OMA; LRITHYH; -.
DR PhylomeDB; Q08879; -.
DR TreeFam; TF317514; -.
DR BioGRID-ORCS; 14114; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Fbln1; mouse.
DR PRO; PR:Q08879; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q08879; protein.
DR Bgee; ENSMUSG00000006369; Expressed in aortic valve and 266 other tissues.
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; ISO:MGI.
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:0071635; P:negative regulation of transforming growth factor beta production; 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; 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; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; Extracellular matrix; Glycoprotein; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:2249686"
FT CHAIN 30..705
FT /note="Fibulin-1"
FT /id="PRO_0000007564"
FT DOMAIN 36..76
FT /note="Anaphylatoxin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 77..111
FT /note="Anaphylatoxin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 112..144
FT /note="Anaphylatoxin-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 178..217
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 218..263
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 264..309
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 310..357
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 358..400
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 401..442
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 443..482
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 483..526
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 527..580
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 156..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..442
FT /note="Self-association and FN1-binding"
FT /evidence="ECO:0000250"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..61
FT /evidence="ECO:0000250"
FT DISULFID 37..68
FT /evidence="ECO:0000250"
FT DISULFID 50..69
FT /evidence="ECO:0000250"
FT DISULFID 78..109
FT /evidence="ECO:0000250"
FT DISULFID 91..110
FT /evidence="ECO:0000250"
FT DISULFID 112..136
FT /evidence="ECO:0000250"
FT DISULFID 113..143
FT /evidence="ECO:0000250"
FT DISULFID 126..144
FT /evidence="ECO:0000250"
FT DISULFID 182..192
FT /evidence="ECO:0000250"
FT DISULFID 188..201
FT /evidence="ECO:0000250"
FT DISULFID 203..216
FT /evidence="ECO:0000250"
FT DISULFID 222..235
FT /evidence="ECO:0000250"
FT DISULFID 229..244
FT /evidence="ECO:0000250"
FT DISULFID 250..262
FT /evidence="ECO:0000250"
FT DISULFID 268..281
FT /evidence="ECO:0000250"
FT DISULFID 275..290
FT /evidence="ECO:0000250"
FT DISULFID 296..308
FT /evidence="ECO:0000250"
FT DISULFID 314..327
FT /evidence="ECO:0000250"
FT DISULFID 321..336
FT /evidence="ECO:0000250"
FT DISULFID 343..356
FT /evidence="ECO:0000250"
FT DISULFID 362..375
FT /evidence="ECO:0000250"
FT DISULFID 369..384
FT /evidence="ECO:0000250"
FT DISULFID 386..399
FT /evidence="ECO:0000250"
FT DISULFID 405..417
FT /evidence="ECO:0000250"
FT DISULFID 413..426
FT /evidence="ECO:0000250"
FT DISULFID 428..441
FT /evidence="ECO:0000250"
FT DISULFID 447..456
FT /evidence="ECO:0000250"
FT DISULFID 452..465
FT /evidence="ECO:0000250"
FT DISULFID 467..481
FT /evidence="ECO:0000250"
FT DISULFID 487..500
FT /evidence="ECO:0000250"
FT DISULFID 496..509
FT /evidence="ECO:0000250"
FT DISULFID 511..525
FT /evidence="ECO:0000250"
FT DISULFID 531..544
FT /evidence="ECO:0000250"
FT DISULFID 538..553
FT /evidence="ECO:0000250"
FT DISULFID 558..579
FT /evidence="ECO:0000250"
FT VAR_SEQ 569..705
FT /note="FRQEKTDTVRCIKSCRPNDEACVRDPVHTVSHTVISLPTFREFTRPEEIIFL
FT RAVTPLYPANQADIIFDITEGNLRDSFDIIKRYEDGMTVGVVRQVRPIVGPFYAVLKLE
FT MNYVLGGVVSHRNVVNVHIFVSEYWF -> RCERLPCHENQECPRLPLRITYYHLSFPT
FT NIQVPAVVFRMGPSSAVPGDSMQLAITAGNEEGFFTTRKVSHHSGVVALTKPIPEPRDL
FT LLTVKMDLYRHGTVSSFVAKLFIFVSAEL (in isoform C)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:8354280"
FT /id="VSP_001386"
FT CONFLICT 30
FT /note="D -> N (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="G -> P (in Ref. 1; CAA50207)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="S -> A (in Ref. 1; CAA50207)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="E -> K (in Ref. 2; BAC39669)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="C -> Q (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="C -> Q (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT Q08879-2:571
FT /note="E -> A (in Ref. 1; CAA50206)"
FT /evidence="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
