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   27-MAR-2024, entry version 206.
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; 54.
DR   CORUM; P98095; -.
DR   IntAct; P98095; 16.
DR   MINT; P98095; -.
DR   STRING; 9606.ENSP00000384169; -.
DR   GlyConnect; 751; 8 N-Linked glycans (2 sites).
DR   GlyCosmos; P98095; 19 sites, 12 glycans.
DR   GlyGen; P98095; 27 sites, 7 N-linked glycans (2 sites), 8 O-linked glycans (24 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; 9606-ENSP00000384169; -.
DR   PeptideAtlas; P98095; -.
DR   ProteomicsDB; 57790; -. [P98095-1]
DR   ProteomicsDB; 57791; -. [P98095-2]
DR   Antibodypedia; 1165; 289 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   AGR; HGNC:3601; -.
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; MNTCRDI; -.
DR   OrthoDB; 19806at2759; -.
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 1152 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 161 other cell types or tissues.
DR   ExpressionAtlas; P98095; baseline and differential.
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:0010811; P:positive regulation of cell-substrate adhesion; IBA:GO_Central.
DR   CDD; cd00017; ANATO; 2.
DR   CDD; cd00054; EGF_CA; 7.
DR   Gene3D; 2.10.25.10; Laminin; 10.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR   PANTHER; PTHR24034; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24034:SF158; FIBULIN 2; 1.
DR   Pfam; PF01821; ANATO; 2.
DR   Pfam; PF12662; cEGF; 2.
DR   Pfam; PF07645; EGF_CA; 5.
DR   Pfam; PF14670; FXa_inhibition; 1.
DR   SMART; SM00104; ANATO; 3.
DR   SMART; SM00181; EGF; 11.
DR   SMART; SM00179; EGF_CA; 9.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 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.
DR   Genevisible; P98095; HS.
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
//