FBLN2_HUMAN
ID FBLN2_HUMAN Reviewed; 1184 AA.
AC P98095; B7Z9C5; Q8IUI0; Q8IUI1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Fibulin-2;
DE Short=FIBL-2;
DE Flags: Precursor;
GN Name=FBLN2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-854.
RC TISSUE=Fibroblast;
RX PubMed=7806230; DOI=10.1006/geno.1994.1404;
RA Zhang R.-Z., Pan T.-C., Zhang Z.-Y., Mattei M.-G., Timpl R., Chu M.-L.;
RT "Fibulin-2 (FBLN2): human cDNA sequence, mRNA expression, and mapping of
RT the gene on human and mouse chromosomes.";
RL Genomics 22:425-430(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), AND ALTERNATIVE
RP SPLICING.
RA Li D., Marian A.J., Roberts R.;
RT "Identification of a novel alternatively spliced isoform of human fibulin-2
RT gene abundantly expressed in heart and genetic evaluation in patients with
RT ARVD.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=8737292; DOI=10.1007/bf02331415;
RA Miosge N., Gotz W., Sasaki T., Chu M.-L., Timpl R., Herken R.;
RT "The extracellular matrix proteins fibulin-1 and fibulin-2 in the early
RT human embryo.";
RL Histochem. J. 28:109-116(1996).
RN [6]
RP FUNCTION, AND INTERACTION WITH FBN1 AND ELN.
RX PubMed=17255108; DOI=10.1074/jbc.m608204200;
RA El-Hallous E., Sasaki T., Hubmacher D., Getie M., Tiedemann K.,
RA Brinckmann J., Baetge B., Davis E.C., Reinhardt D.P.;
RT "Fibrillin-1 interactions with fibulins depend on the first hybrid domain
RT and provide an adaptor function to tropoelastin.";
RL J. Biol. Chem. 282:8935-8946(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1035.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [9]
RP GLYCOSYLATION, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=22171320; DOI=10.1074/mcp.m111.013649;
RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT "Human urinary glycoproteomics; attachment site specific analysis of N- and
RT O-linked glycosylations by CID and ECD.";
RL Mol. Cell. Proteomics 11:1-17(2012).
CC -!- FUNCTION: Its binding to fibronectin and some other ligands is calcium
CC dependent. May act as an adapter that mediates the interaction between
CC FBN1 and ELN (PubMed:17255108). {ECO:0000269|PubMed:17255108}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked. Interacts with LAMA2 (By
CC similarity). Interacts with FBN1 (via N-terminal domain). Forms a
CC ternary complex with ELN and FBN1 (PubMed:17255108).
CC {ECO:0000250|UniProtKB:P37889, ECO:0000269|PubMed:17255108}.
CC -!- INTERACTION:
CC P98095; P27658: COL8A1; NbExp=3; IntAct=EBI-947973, EBI-747133;
CC P98095; Q969U6: FBXW5; NbExp=3; IntAct=EBI-947973, EBI-741068;
CC P98095; Q9H2F3: HSD3B7; NbExp=3; IntAct=EBI-947973, EBI-3918847;
CC P98095; Q15040: JOSD1; NbExp=3; IntAct=EBI-947973, EBI-2510602;
CC P98095; Q9BYE3: LCE3D; NbExp=3; IntAct=EBI-947973, EBI-6658837;
CC P98095; P32242: OTX1; NbExp=3; IntAct=EBI-947973, EBI-740446;
CC P98095; Q96IQ9: ZNF414; NbExp=3; IntAct=EBI-947973, EBI-744257;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P98095-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P98095-2; Sequence=VSP_041404;
CC -!- TISSUE SPECIFICITY: Component of both basement membranes and other
CC connective tissues. Expressed in heart, placenta and ovary.
CC -!- DEVELOPMENTAL STAGE: Widely expressed during embryonic development.
CC Primarily detected within the neuropithelium, spinal ganglia and
CC peripheral nerves. {ECO:0000269|PubMed:8737292}.
CC -!- PTM: O-glycosylated with core 1 or possibly core 8 glycans. It is
CC unsure if the O-glycosylation is on Thr-347 or Ser-348.
CC {ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22171320}.
CC -!- SIMILARITY: Belongs to the fibulin family. {ECO:0000305}.
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DR EMBL; X82494; CAA57876.1; -; mRNA.
DR EMBL; AY130458; AAN05435.1; -; Genomic_DNA.
DR EMBL; AY130456; AAN05435.1; JOINED; Genomic_DNA.
DR EMBL; AY130457; AAN05435.1; JOINED; Genomic_DNA.
DR EMBL; AY130459; AAN05436.1; -; mRNA.
DR EMBL; AK304827; BAH14261.1; -; mRNA.
DR EMBL; AC090509; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS46761.1; -. [P98095-2]
DR CCDS; CCDS46762.1; -. [P98095-1]
DR PIR; A55184; A55184.
DR RefSeq; NP_001004019.1; NM_001004019.1. [P98095-2]
DR RefSeq; NP_001158507.1; NM_001165035.1. [P98095-2]
DR RefSeq; NP_001989.2; NM_001998.2. [P98095-1]
DR AlphaFoldDB; P98095; -.
DR BioGRID; 108493; 53.
DR CORUM; P98095; -.
DR IntAct; P98095; 16.
DR MINT; P98095; -.
DR STRING; 9606.ENSP00000384169; -.
DR GlyConnect; 751; 8 N-Linked glycans (2 sites).
DR GlyGen; P98095; 19 sites, 7 N-linked glycans (2 sites), 5 O-linked glycans (16 sites).
DR iPTMnet; P98095; -.
DR PhosphoSitePlus; P98095; -.
DR BioMuta; FBLN2; -.
DR DMDM; 224471827; -.
DR EPD; P98095; -.
DR jPOST; P98095; -.
DR MassIVE; P98095; -.
DR MaxQB; P98095; -.
DR PaxDb; P98095; -.
DR PeptideAtlas; P98095; -.
DR PRIDE; P98095; -.
DR ProteomicsDB; 57790; -. [P98095-1]
DR ProteomicsDB; 57791; -. [P98095-2]
DR Antibodypedia; 1165; 273 antibodies from 32 providers.
DR DNASU; 2199; -.
DR Ensembl; ENST00000295760.11; ENSP00000295760.7; ENSG00000163520.14. [P98095-1]
DR Ensembl; ENST00000404922.8; ENSP00000384169.3; ENSG00000163520.14. [P98095-2]
DR Ensembl; ENST00000492059.5; ENSP00000420042.1; ENSG00000163520.14. [P98095-2]
DR GeneID; 2199; -.
DR KEGG; hsa:2199; -.
DR MANE-Select; ENST00000404922.8; ENSP00000384169.3; NM_001004019.2; NP_001004019.1. [P98095-2]
DR UCSC; uc011ava.3; human. [P98095-1]
DR CTD; 2199; -.
DR DisGeNET; 2199; -.
DR GeneCards; FBLN2; -.
DR HGNC; HGNC:3601; FBLN2.
DR HPA; ENSG00000163520; Tissue enhanced (heart).
DR MIM; 135821; gene.
DR neXtProt; NX_P98095; -.
DR OpenTargets; ENSG00000163520; -.
DR PharmGKB; PA28014; -.
DR VEuPathDB; HostDB:ENSG00000163520; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000156047; -.
DR HOGENOM; CLU_268948_0_0_1; -.
DR InParanoid; P98095; -.
DR OMA; ICTRWTS; -.
DR PhylomeDB; P98095; -.
DR TreeFam; TF317514; -.
DR PathwayCommons; P98095; -.
DR Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
DR SignaLink; P98095; -.
DR BioGRID-ORCS; 2199; 7 hits in 1072 CRISPR screens.
DR ChiTaRS; FBLN2; human.
DR GeneWiki; FBLN2; -.
DR GenomeRNAi; 2199; -.
DR Pharos; P98095; Tbio.
DR PRO; PR:P98095; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P98095; protein.
DR Bgee; ENSG00000163520; Expressed in right atrium auricular region and 159 other tissues.
DR ExpressionAtlas; P98095; baseline and differential.
DR Genevisible; P98095; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; TAS:ProtInc.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
DR GO; GO:0050840; F:extracellular matrix binding; IBA:GO_Central.
DR GO; GO:0030023; F:extracellular matrix constituent conferring elasticity; ISS:BHF-UCL.
DR GO; GO:0005201; F:extracellular matrix structural constituent; TAS:ProtInc.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IBA:GO_Central.
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; IPR037286; Fibulin-2.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR PANTHER; PTHR24039:SF32; PTHR24039:SF32; 2.
DR Pfam; PF01821; ANATO; 1.
DR Pfam; PF12662; cEGF; 2.
DR Pfam; PF07645; EGF_CA; 5.
DR SMART; SM00104; ANATO; 3.
DR SMART; SM00181; EGF; 11.
DR SMART; SM00179; EGF_CA; 9.
DR SUPFAM; SSF57184; SSF57184; 4.
DR PROSITE; PS01177; ANAPHYLATOXIN_1; 3.
DR PROSITE; PS01178; ANAPHYLATOXIN_2; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 5.
DR PROSITE; PS01186; EGF_2; 5.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 9.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Phosphoprotein; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1184
FT /note="Fibulin-2"
FT /id="PRO_0000007568"
FT DOMAIN 445..480
FT /note="Anaphylatoxin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 488..519
FT /note="Anaphylatoxin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 521..553
FT /note="Anaphylatoxin-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 604..645
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 679..718
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 719..763
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 764..809
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 810..857
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 858..900
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 901..942
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 943..981
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 982..1024
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1025..1069
FT /note="EGF-like 10; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 28..444
FT /note="N"
FT REGION 28..177
FT /note="Subdomain NA (Cys-rich)"
FT REGION 178..444
FT /note="Subdomain NB (Cys-free)"
FT REGION 221..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1184
FT /note="Domain III"
FT COMPBIAS 409..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1035
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT DISULFID 445..472
FT /evidence="ECO:0000250"
FT DISULFID 446..479
FT /evidence="ECO:0000250"
FT DISULFID 459..480
FT /evidence="ECO:0000250"
FT DISULFID 489..518
FT /evidence="ECO:0000250"
FT DISULFID 502..519
FT /evidence="ECO:0000250"
FT DISULFID 521..545
FT /evidence="ECO:0000250"
FT DISULFID 522..552
FT /evidence="ECO:0000250"
FT DISULFID 535..553
FT /evidence="ECO:0000250"
FT DISULFID 608..620
FT /evidence="ECO:0000250"
FT DISULFID 616..629
FT /evidence="ECO:0000250"
FT DISULFID 631..644
FT /evidence="ECO:0000250"
FT DISULFID 683..693
FT /evidence="ECO:0000250"
FT DISULFID 689..702
FT /evidence="ECO:0000250"
FT DISULFID 704..717
FT /evidence="ECO:0000250"
FT DISULFID 723..736
FT /evidence="ECO:0000250"
FT DISULFID 730..745
FT /evidence="ECO:0000250"
FT DISULFID 751..762
FT /evidence="ECO:0000250"
FT DISULFID 768..781
FT /evidence="ECO:0000250"
FT DISULFID 775..790
FT /evidence="ECO:0000250"
FT DISULFID 796..808
FT /evidence="ECO:0000250"
FT DISULFID 814..827
FT /evidence="ECO:0000250"
FT DISULFID 821..836
FT /evidence="ECO:0000250"
FT DISULFID 843..856
FT /evidence="ECO:0000250"
FT DISULFID 862..875
FT /evidence="ECO:0000250"
FT DISULFID 869..884
FT /evidence="ECO:0000250"
FT DISULFID 886..899
FT /evidence="ECO:0000250"
FT DISULFID 905..917
FT /evidence="ECO:0000250"
FT DISULFID 913..926
FT /evidence="ECO:0000250"
FT DISULFID 928..941
FT /evidence="ECO:0000250"
FT DISULFID 947..956
FT /evidence="ECO:0000250"
FT DISULFID 952..965
FT /evidence="ECO:0000250"
FT DISULFID 967..980
FT /evidence="ECO:0000250"
FT DISULFID 986..998
FT /evidence="ECO:0000250"
FT DISULFID 994..1007
FT /evidence="ECO:0000250"
FT DISULFID 1009..1023
FT /evidence="ECO:0000250"
FT DISULFID 1029..1042
FT /evidence="ECO:0000250"
FT DISULFID 1036..1051
FT /evidence="ECO:0000250"
FT DISULFID 1056..1068
FT /evidence="ECO:0000250"
FT VAR_SEQ 718
FT /note="E -> EDQDECLMGAHDCSRRQFCVNTLGSFYCVNHTVLCADGYILNAHRKC
FT V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_041404"
FT VARIANT 45
FT /note="I -> V (in dbSNP:rs60850813)"
FT /id="VAR_061159"
FT VARIANT 144
FT /note="H -> R (in dbSNP:rs28587534)"
FT /id="VAR_061160"
FT VARIANT 361
FT /note="S -> G (in dbSNP:rs3732666)"
FT /id="VAR_059266"
FT VARIANT 387
FT /note="N -> T (in dbSNP:rs3796318)"
FT /id="VAR_059267"
FT VARIANT 854
FT /note="T -> A (in dbSNP:rs9843344)"
FT /evidence="ECO:0000269|PubMed:7806230"
FT /id="VAR_059268"
FT VARIANT 1114
FT /note="G -> R (in dbSNP:rs1061375)"
FT /id="VAR_055722"
FT CONFLICT 145
FT /note="K -> E (in Ref. 1; CAA57876 and 2; AAN05436)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="E -> G (in Ref. 3; BAH14261)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1184 AA; 126573 MW; D46890D93518B343 CRC64;
MVLLWEPAGA WLALGLALAL GPSVAAAAPR QDCTGVECPP LENCIEEALE PGACCATCVQ
QGCACEGYQY YDCLQGGFVR GRVPAGQSYF VDFGSTECSC PPGGGKISCQ FMLCPELPPN
CIEAVVVADS CPQCGQVGCV HAGHKYAAGH TVHLPPCRAC HCPDAGGELI CYQLPGCHGN
FSDAEEGDPE RHYEDPYSYD QEVAEVEAAT ALGGEVQAGA VQAGAGGPPA ALGGGSQPLS
TIQAPPWPAV LPRPTAAAAL GPPAPVQAKA RRVTEDSEEE EEEEEEREEM AVTEQLAAGG
HRGLDGLPTT APAGPSLPIQ EERAEAGARA EAGARPEENL ILDAQATSRS TGPEGVTHAP
SLGKAALVPT QAVPGSPRDP VKPSPHNILS TSLPDAAWIP PTREVPRKPQ VLPHSHVEED
TDPNSVHSIP RSSPEGSTKD LIETCCAAGQ QWAIDNDECL EIPESGTEDN VCRTAQRHCC
VSYLQEKSCM AGVLGAKEGE TCGAEDNDSC GISLYKQCCD CCGLGLRVRA EGQSCESNPN
LGYPCNHVML SCCEGEEPLI VPEVRRPPEP AAAPRRVSEA EMAGREALSL GTEAELPNSL
PGDDQDECLL LPGELCQHLC INTVGSYHCA CFPGFSLQDD GRTCRPEGHP PQPEAPQEPA
LKSEFSQVAS NTIPLPLPQP NTCKDNGPCK QVCSTVGGSA ICSCFPGYAI MADGVSCEDI
NECVTDLHTC SRGEHCVNTL GSFHCYKALT CEPGYALKDG ECEDVDECAM GTHTCQPGFL
CQNTKGSFYC QARQRCMDGF LQDPEGNCVD INECTSLSEP CRPGFSCINT VGSYTCQRNP
LICARGYHAS DDGTKCVDVN ECETGVHRCG EGQVCHNLPG SYRCDCKAGF QRDAFGRGCI
DVNECWASPG RLCQHTCENT LGSYRCSCAS GFLLAADGKR CEDVNECEAQ RCSQECANIY
GSYQCYCRQG YQLAEDGHTC TDIDECAQGA GILCTFRCLN VPGSYQCACP EQGYTMTANG
RSCKDVDECA LGTHNCSEAE TCHNIQGSFR CLRFECPPNY VQVSKTKCER TTCHDFLECQ
NSPARITHYQ LNFQTGLLVP AHIFRIGPAP AFTGDTIALN IIKGNEEGYF GTRRLNAYTG
VVYLQRAVLE PRDFALDVEM KLWRQGSVTT FLAKMHIFFT TFAL
