LAMB4_HUMAN
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 03-AUG-2022, entry version 121.
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 GlyGen; A4D0S4; 16 sites.
DR iPTMnet; A4D0S4; -.
DR PhosphoSitePlus; A4D0S4; -.
DR BioMuta; LAMB4; -.
DR jPOST; A4D0S4; -.
DR MassIVE; A4D0S4; -.
DR PaxDb; A4D0S4; -.
DR PeptideAtlas; A4D0S4; -.
DR PRIDE; A4D0S4; -.
DR ProteomicsDB; 592; -. [A4D0S4-1]
DR ProteomicsDB; 593; -. [A4D0S4-2]
DR ProteomicsDB; 594; -. [A4D0S4-3]
DR Antibodypedia; 62084; 34 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 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; 65841at2759; -.
DR PhylomeDB; A4D0S4; -.
DR TreeFam; TF312903; -.
DR PathwayCommons; A4D0S4; -.
DR SignaLink; A4D0S4; -.
DR BioGRID-ORCS; 22798; 20 hits in 1068 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 111 other tissues.
DR ExpressionAtlas; A4D0S4; baseline and differential.
DR Genevisible; A4D0S4; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0043256; C:laminin complex; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0070831; P:basement membrane assembly; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 12.
DR InterPro; IPR013015; Laminin_IV_B.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00053; Laminin_EGF; 12.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00180; EGF_Lam; 13.
DR SMART; SM00136; LamNT; 1.
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.
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
