ID   LAMB4_HUMAN             Reviewed;        1761 AA.
AC   A4D0S4; A5PKU6; B2RTT3; B5MEB9; Q86TP7; Q86XN2; Q8NBX5;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 130.
DE   RecName: Full=Laminin subunit beta-4;
DE   AltName: Full=Laminin beta-1-related protein;
DE   Flags: Precursor;
GN   Name=LAMB4;
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).
RC   TISSUE=Placenta;
RA   Olson P.F., Koch M., Champliaud M.F., Rowland K., Jin W., Burgeson R.E.;
RT   "Cloning and characterization of the human laminin beta-4 chain.";
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 975-1761 (ISOFORM 3).
RC   TISSUE=Testis;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1528-1761 (ISOFORM 1).
RC   TISSUE=Placenta;
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   [6]
RP   VARIANT CYS-1028.
RX   PubMed=25787250; DOI=10.1073/pnas.1503696112;
RA   Cromer M.K., Choi M., Nelson-Williams C., Fonseca A.L., Kunstman J.W.,
RA   Korah R.M., Overton J.D., Mane S., Kenney B., Malchoff C.D., Stalberg P.,
RA   Akerstroem G., Westin G., Hellman P., Carling T., Bjoerklund P.,
RA   Lifton R.P.;
RT   "Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in
RT   insulin-producing adenomas.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:4062-4067(2015).
CC   -!- FUNCTION: Binding to cells via a high affinity receptor, laminin is
CC       thought to mediate the attachment, migration and organization of cells
CC       into tissues during embryonic development by interacting with other
CC       extracellular matrix components.
CC   -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC       different polypeptide chains (alpha, beta, gamma), which are bound to
CC       each other by disulfide bonds into a cross-shaped molecule comprising
CC       one long and three short arms with globules at each end.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=A4D0S4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A4D0S4-2; Sequence=VSP_029913, VSP_029914;
CC       Name=3;
CC         IsoId=A4D0S4-3; Sequence=VSP_029915, VSP_029916;
CC   -!- DOMAIN: The alpha-helical domains I and II are thought to interact with
CC       other laminin chains to form a coiled coil structure.
CC   -!- DOMAIN: Domains VI and IV are globular.
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DR   EMBL; AF028816; AAC95123.1; -; mRNA.
DR   EMBL; AC005048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH236947; EAL24387.1; -; Genomic_DNA.
DR   EMBL; BC045172; AAH45172.2; -; mRNA.
DR   EMBL; BC140804; AAI40805.1; -; mRNA.
DR   EMBL; BC142619; AAI42620.1; -; mRNA.
DR   EMBL; AK075165; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS34732.1; -. [A4D0S4-1]
DR   CCDS; CCDS83218.1; -. [A4D0S4-2]
DR   RefSeq; NP_001304975.1; NM_001318046.1. [A4D0S4-1]
DR   RefSeq; NP_001304977.1; NM_001318048.1.
DR   RefSeq; NP_031382.2; NM_007356.2. [A4D0S4-1]
DR   RefSeq; XP_011514280.1; XM_011515978.1. [A4D0S4-3]
DR   AlphaFoldDB; A4D0S4; -.
DR   SMR; A4D0S4; -.
DR   BioGRID; 116479; 3.
DR   IntAct; A4D0S4; 1.
DR   STRING; 9606.ENSP00000373433; -.
DR   ChEMBL; CHEMBL2364187; -.
DR   GlyCosmos; A4D0S4; 16 sites, No reported glycans.
DR   GlyGen; A4D0S4; 16 sites.
DR   iPTMnet; A4D0S4; -.
DR   PhosphoSitePlus; A4D0S4; -.
DR   BioMuta; LAMB4; -.
DR   jPOST; A4D0S4; -.
DR   MassIVE; A4D0S4; -.
DR   PaxDb; 9606-ENSP00000373433; -.
DR   PeptideAtlas; A4D0S4; -.
DR   ProteomicsDB; 592; -. [A4D0S4-1]
DR   ProteomicsDB; 593; -. [A4D0S4-2]
DR   ProteomicsDB; 594; -. [A4D0S4-3]
DR   Antibodypedia; 62084; 49 antibodies from 12 providers.
DR   DNASU; 22798; -.
DR   Ensembl; ENST00000205386.8; ENSP00000205386.4; ENSG00000091128.13. [A4D0S4-1]
DR   Ensembl; ENST00000388781.8; ENSP00000373433.3; ENSG00000091128.13. [A4D0S4-1]
DR   GeneID; 22798; -.
DR   KEGG; hsa:22798; -.
DR   MANE-Select; ENST00000388781.8; ENSP00000373433.3; NM_007356.3; NP_031382.2.
DR   UCSC; uc003vey.3; human. [A4D0S4-1]
DR   AGR; HGNC:6491; -.
DR   CTD; 22798; -.
DR   DisGeNET; 22798; -.
DR   GeneCards; LAMB4; -.
DR   HGNC; HGNC:6491; LAMB4.
DR   HPA; ENSG00000091128; Tissue enriched (skin).
DR   MIM; 616380; gene.
DR   neXtProt; NX_A4D0S4; -.
DR   OpenTargets; ENSG00000091128; -.
DR   PharmGKB; PA30279; -.
DR   VEuPathDB; HostDB:ENSG00000091128; -.
DR   eggNOG; KOG0994; Eukaryota.
DR   GeneTree; ENSGT00940000162514; -.
DR   HOGENOM; CLU_001560_1_0_1; -.
DR   InParanoid; A4D0S4; -.
DR   OMA; RRCSCHP; -.
DR   OrthoDB; 90222at2759; -.
DR   PhylomeDB; A4D0S4; -.
DR   TreeFam; TF312903; -.
DR   PathwayCommons; A4D0S4; -.
DR   SignaLink; A4D0S4; -.
DR   BioGRID-ORCS; 22798; 22 hits in 1144 CRISPR screens.
DR   ChiTaRS; LAMB4; human.
DR   GenomeRNAi; 22798; -.
DR   Pharos; A4D0S4; Tbio.
DR   PRO; PR:A4D0S4; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; A4D0S4; Protein.
DR   Bgee; ENSG00000091128; Expressed in skin of abdomen and 113 other cell types or tissues.
DR   ExpressionAtlas; A4D0S4; baseline and differential.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   CDD; cd22301; cc_LAMB4_C; 1.
DR   CDD; cd00055; EGF_Lam; 12.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.10.25.10; Laminin; 11.
DR   Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR   InterPro; IPR013015; Laminin_IV_B.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR002049; LE_dom.
DR   PANTHER; PTHR10574:SF435; LAMININ SUBUNIT GAMMA-1; 1.
DR   PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR   Pfam; PF00053; Laminin_EGF; 12.
DR   Pfam; PF21199; LAMININ_IV_B; 1.
DR   Pfam; PF00055; Laminin_N; 1.
DR   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00180; EGF_Lam; 13.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 13.
DR   PROSITE; PS00022; EGF_1; 10.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS01248; EGF_LAM_1; 11.
DR   PROSITE; PS50027; EGF_LAM_2; 13.
DR   PROSITE; PS51116; LAMININ_IVB; 1.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
DR   Genevisible; A4D0S4; HS.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Basement membrane; Cell adhesion; Coiled coil;
KW   Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Laminin EGF-like domain; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..1761
FT                   /note="Laminin subunit beta-4"
FT                   /id="PRO_0000312857"
FT   DOMAIN          24..264
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT   DOMAIN          265..331
FT                   /note="Laminin EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          332..394
FT                   /note="Laminin EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          395..454
FT                   /note="Laminin EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          455..505
FT                   /note="Laminin EGF-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          506..552
FT                   /note="Laminin EGF-like 5; truncated"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          545..763
FT                   /note="Laminin IV type B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00462"
FT   DOMAIN          769..816
FT                   /note="Laminin EGF-like 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          817..862
FT                   /note="Laminin EGF-like 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          863..910
FT                   /note="Laminin EGF-like 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          911..969
FT                   /note="Laminin EGF-like 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          970..1021
FT                   /note="Laminin EGF-like 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1022..1079
FT                   /note="Laminin EGF-like 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1080..1127
FT                   /note="Laminin EGF-like 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1128..1174
FT                   /note="Laminin EGF-like 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   REGION          1175..1375
FT                   /note="Domain II"
FT   REGION          1376..1408
FT                   /note="Domain alpha"
FT   REGION          1409..1761
FT                   /note="Domain I"
FT   COILED          1243..1301
FT                   /evidence="ECO:0000255"
FT   COILED          1416..1480
FT                   /evidence="ECO:0000255"
FT   COILED          1525..1759
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        229
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        246
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1016
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1055
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1223
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1301
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1326
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1333
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1354
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1469
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1517
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1587
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1596
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1609
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1725
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        265..?274
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        267..295
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        297..306
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        309..329
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        332..341
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        334..359
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        362..371
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        374..392
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        395..408
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        397..423
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        425..434
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        437..452
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        455..468
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        457..475
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        477..486
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        489..503
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        506..518
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        508..525
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        527..536
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        769..781
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        771..788
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        790..799
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        802..814
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        817..829
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        819..836
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        838..847
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        850..860
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        863..872
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        865..879
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        882..891
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        894..908
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        913..938
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        940..949
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        952..967
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        970..984
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        972..991
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        994..1003
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1006..1019
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1022..1043
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1024..1050
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1052..1061
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1064..1077
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1080..1092
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1082..1099
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1101..1110
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1113..1125
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1128..1140
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1130..1147
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1149..1158
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1161..1172
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1175
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   DISULFID        1178
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   DISULFID        1759
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   VAR_SEQ         709..772
FT                   /note="LGLIPQINSLENFCSKQDLDEYQLHNCVEIASAMGPQVLPGACERLIISMSA
FT                   KLHDGAVACKCH -> AAVQWHNLGSLQPPPPECKQFSCFSFPSSWDYRHPPPHLASFC
FT                   IFSRDGVSPHWPGWSRTPDLR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_029913"
FT   VAR_SEQ         773..1761
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_029914"
FT   VAR_SEQ         1716..1723
FT                   /note="DLERKIQD -> GCFQNSAR (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_029915"
FT   VAR_SEQ         1724..1761
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_029916"
FT   VARIANT         44
FT                   /note="M -> T (in dbSNP:rs35644375)"
FT                   /id="VAR_037588"
FT   VARIANT         234
FT                   /note="H -> Y (in dbSNP:rs2074749)"
FT                   /id="VAR_037589"
FT   VARIANT         591
FT                   /note="V -> F (in dbSNP:rs9690688)"
FT                   /id="VAR_037590"
FT   VARIANT         866
FT                   /note="N -> S (in dbSNP:rs2240445)"
FT                   /id="VAR_037591"
FT   VARIANT         1028
FT                   /note="G -> C (in dbSNP:rs1299564647)"
FT                   /evidence="ECO:0000269|PubMed:25787250"
FT                   /id="VAR_074174"
FT   VARIANT         1350
FT                   /note="T -> N (in dbSNP:rs10260756)"
FT                   /id="VAR_037592"
FT   VARIANT         1510
FT                   /note="H -> Y (in dbSNP:rs1627354)"
FT                   /id="VAR_037593"
FT   VARIANT         1612
FT                   /note="R -> S (in dbSNP:rs2528693)"
FT                   /id="VAR_037594"
FT   CONFLICT        70
FT                   /note="F -> S (in Ref. 1; AAC95123)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        93
FT                   /note="I -> T (in Ref. 1; AAC95123)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1542
FT                   /note="L -> S (in Ref. 1; AAC95123)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1761 AA;  193540 MW;  57A740F079CE1FB2 CRC64;
     MQFQLTLFLH LGWLSYSKAQ DDCNRGACHP TTGDLLVGRN TQLMASSTCG LSRAQKYCIL
     SYLEGEQKCF ICDSRFPYDP YDQPNSHTIE NVIVSFEPDR EKKWWQSENG LDHVSIRLDL
     EALFRFSHLI LTFKTFRPAA MLVERSTDYG HNWKVFKYFA KDCATSFPNI TSGQAQGVGD
     IVCDSKYSDI EPSTGGEVVL KVLDPSFEIE NPYSPYIQDL VTLTNLRINF TKLHTLGDAL
     LGRRQNDSLD KYYYALYEMI VRGSCFCNGH ASECRPMQKM RGDVFSPPGM VHGQCVCQHN
     TDGPNCERCK DFFQDAPWRP AADLQDNACR SCSCNSHSSR CHFDMTTYLA SGGLSGGVCE
     DCQHNTEGQH CDRCRPLFYR DPLKTISDPY ACIPCECDPD GTISGGICVS HSDPALGSVA
     GQCLCKENVE GAKCDQCKPN HYGLSATDPL GCQPCDCNPL GSLPFLTCDV DTGQCLCLSY
     VTGAHCEECT VGYWGLGNHL HGCSPCDCDI GGAYSNVCSP KNGQCECRPH VTGRSCSEPA
     PGYFFAPLNF YLYEAEEATT LQGLAPLGSE TFGQSPAVHV VLGEPVPGNP VTWTGPGFAR
     VLPGAGLRFA VNNIPFPVDF TIAIHYETQS AADWTVQIVV NPPGGSEHCI PKTLQSKPQS
     FALPAATRIM LLPTPICLEP DVQYSIDVYF SQPLQGESHA HSHVLVDSLG LIPQINSLEN
     FCSKQDLDEY QLHNCVEIAS AMGPQVLPGA CERLIISMSA KLHDGAVACK CHPQGSVGSS
     CSRLGGQCQC KPLVVGRCCD RCSTGSYDLG HHGCHPCHCH PQGSKDTVCD QVTGQCPCHG
     EVSGRRCDRC LAGYFGFPSC HPCPCNRFAE LCDPETGSCF NCGGFTTGRN CERCIDGYYG
     NPSSGQPCRP CLCPDDPSSN QYFAHSCYQN LWSSDVICNC LQGYTGTQCG ECSTGFYGNP
     RISGAPCQPC ACNNNIDVTD PESCSRVTGE CLRCLHNTQG ANCQLCKPGH YGSALNQTCR
     RCSCHASGVS PMECPPGGGA CLCDPVTGAC PCLPNVTGLA CDRCADGYWN LVPGRGCQSC
     DCDPRTSQSS HCDQLTGQCP CKLGYGGKRC SECQENYYGD PPGRCIPCDC NRAGTQKPIC
     DPDTGMCRCR EGVSGQRCDR CARGHSQEFP TCLQCHLCFD QWDHTISSLS KAVQGLMRLA
     ANMEDKRETL PVCEADFKDL RGNVSEIERI LKHPVFPSGK FLKVKDYHDS VRRQIMQLNE
     QLKAVYEFQD LKDTIERAKN EADLLLEDLQ EEIDLQSSVL NASIADSSEN IKKYYHISSS
     AEKKINETSS TINTSANTRN DLLTILDTLT SKGNLSLERL KQIKIPDIQI LNEKVCGDPG
     NVPCVPLPCG GALCTGRKGH RKCRGPGCHG SLTLSTNALQ KAQEAKSIIR NLDKQVRGLK
     NQIESISEQA EVSKNNALQL REKLGNIRNQ SDSEEENINL FIKKVKNFLL EENVPPEDIE
     KVANGVLDIH LPIPSQNLTD ELVKIQKHMQ LCEDYRTDEN RLNEEADGAQ KLLVKAKAAE
     KAANILLNLD KTLNQLQQAQ ITQGRANSTI TQLTANITKI KKNVLQAENQ TREMKSELEL
     AKQRSGLEDG LSLLQTKLQR HQDHAVNAKV QAESAQHQAG SLEKEFVELK KQYAILQRKT
     STTGLTKETL GKVKQLKDAA EKLAGDTEAK IRRITDLERK IQDLNLSRQA KADQLRILED
     QVVAIKNEIV EQEKKYARCY S
//