LAMB2_HUMAN
ID LAMB2_HUMAN Reviewed; 1798 AA.
AC P55268; Q16321;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Laminin subunit beta-2;
DE AltName: Full=Laminin B1s chain;
DE AltName: Full=Laminin-11 subunit beta;
DE AltName: Full=Laminin-14 subunit beta;
DE AltName: Full=Laminin-15 subunit beta;
DE AltName: Full=Laminin-3 subunit beta;
DE AltName: Full=Laminin-4 subunit beta;
DE AltName: Full=Laminin-7 subunit beta;
DE AltName: Full=Laminin-9 subunit beta;
DE AltName: Full=S-laminin subunit beta;
DE Short=S-LAM beta;
DE Flags: Precursor;
GN Name=LAMB2; Synonyms=LAMS;
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 [GENOMIC DNA / MRNA].
RX PubMed=7698745; DOI=10.1006/geno.1994.1612;
RA Wewer U.M., Gerecke D.R., Durkin M.E., Kurtz K.S., Mattei M.-G.,
RA Champliaud M.-F., Burgeson R.E., Albrechtsen R.;
RT "Human beta 2 chain of laminin (formerly S chain): cDNA cloning,
RT chromosomal localization, and expression in carcinomas.";
RL Genomics 24:243-252(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7795887; DOI=10.1016/0945-053x(95)90006-3;
RA Iivanainen A., Vuolteenaho R., Sainio K., Eddy R., Shows T.B., Sariola H.,
RA Tryggvason K.;
RT "The human laminin beta 2 chain (S-laminin): structure, expression in fetal
RT tissues and chromosomal assignment of the LAMB2 gene.";
RL Matrix Biol. 14:489-497(1995).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1308; ASN-1348 AND ASN-1499.
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [6]
RP PHOSPHORYLATION AT SER-1532.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [7]
RP VARIANT PIERSS TRP-246.
RX PubMed=15367484; DOI=10.1093/hmg/ddh284;
RA Zenker M., Aigner T., Wendler O., Tralau T., Muentefering H., Fenski R.,
RA Pitz S., Schumacher V., Royer-Pokora B., Wuehl E., Cochat P., Bouvier R.,
RA Kraus C., Mark K., Madlon H., Doetsch J., Rascher W., Maruniak-Chudek I.,
RA Lennert T., Neumann L.M., Reis A.;
RT "Human laminin beta2 deficiency causes congenital nephrosis with mesangial
RT sclerosis and distinct eye abnormalities.";
RL Hum. Mol. Genet. 13:2625-2632(2004).
RN [8]
RP VARIANTS PIERSS GLN-246; ARG-321; LYS-1380 AND PHE-1393.
RX PubMed=16912710; DOI=10.1038/sj.ki.5001679;
RA Hasselbacher K., Wiggins R.C., Matejas V., Hinkes B.G., Mucha B.,
RA Hoskins B.E., Ozaltin F., Nuernberg G., Becker C., Hangan D., Pohl M.,
RA Kuwertz-Broeking E., Griebel M., Schumacher V., Royer-Pokora B.,
RA Bakkaloglu A., Nuernberg P., Zenker M., Hildebrandt F.;
RT "Recessive missense mutations in LAMB2 expand the clinical spectrum of
RT LAMB2-associated disorders.";
RL Kidney Int. 70:1008-1012(2006).
RN [9]
RP VARIANTS NPHS5 ARG-321; LYS-1380 AND PHE-1393.
RX PubMed=20798252; DOI=10.2215/cjn.01190210;
RA Buescher A.K., Kranz B., Buescher R., Hildebrandt F., Dworniczak B.,
RA Pennekamp P., Kuwertz-Broeking E., Wingen A.M., John U., Kemper M.,
RA Monnens L., Hoyer P.F., Weber S., Konrad M.;
RT "Immunosuppression and renal outcome in congenital and pediatric steroid-
RT resistant nephrotic syndrome.";
RL Clin. J. Am. Soc. Nephrol. 5:2075-2084(2010).
RN [10]
RP VARIANT NPHS5 ARG-147.
RX PubMed=21236492; DOI=10.1016/j.ophtha.2010.10.009;
RA Mohney B.G., Pulido J.S., Lindor N.M., Hogan M.C., Consugar M.B.,
RA Peters J., Pankratz V.S., Nasr S.H., Smith S.J., Gloor J., Kubly V.,
RA Spencer D., Nielson R., Puffenberger E.G., Strauss K.A., Morton D.H.,
RA Eldahdah L., Harris P.C.;
RT "A novel mutation of LAMB2 in a multigenerational mennonite family reveals
RT a new phenotypic variant of Pierson syndrome.";
RL Ophthalmology 118:1137-1144(2011).
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. Beta-2 is a
CC subunit of laminin-3 (laminin-121 or S-laminin), laminin-4 (laminin-221
CC or S-merosin), laminin-7 (laminin-321 or KS-laminin), laminin-9
CC (laminin-421), laminin-11 (laminin-521), laminin-14 (laminin-423) and
CC laminin-15 (laminin-523).
CC -!- INTERACTION:
CC P55268; Q969E8: TSR2; NbExp=3; IntAct=EBI-2529769, EBI-746981;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane. Note=S-laminin is concentrated in the
CC synaptic cleft of the neuromuscular junction.
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.
CC -!- DISEASE: Pierson syndrome (PIERSS) [MIM:609049]: Characterized by
CC nephrotic syndrome with neonatal onset, diffuse mesangial sclerosis and
CC eye abnormalities with microcoria as the leading clinical feature.
CC Death usually occurs within the first weeks of life. Disease severity
CC depends on the mutation type: nontruncating LAMB2 mutations may display
CC variable phenotypes ranging from a milder variant of Pierson syndrome
CC to isolated congenital nephrotic syndrome.
CC {ECO:0000269|PubMed:15367484, ECO:0000269|PubMed:16912710}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Nephrotic syndrome 5 with or without ocular abnormalities
CC (NPHS5) [MIM:614199]: A form of nephrotic syndrome, a renal disease
CC clinically characterized by severe proteinuria, resulting in
CC complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney
CC biopsies show non-specific histologic changes such as focal segmental
CC glomerulosclerosis and diffuse mesangial proliferation. Some affected
CC individuals have an inherited steroid-resistant form and progress to
CC end-stage renal failure. NPHS5 is characterized by very early onset of
CC progressive renal failure. A subset of patients may develop mild ocular
CC anomalies, such as myopia, nystagmus, and strabismus.
CC {ECO:0000269|PubMed:20798252, ECO:0000269|PubMed:21236492}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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DR EMBL; Z68155; CAA92279.1; -; Genomic_DNA.
DR EMBL; Z68156; CAA92279.1; JOINED; Genomic_DNA.
DR EMBL; X79683; CAA56130.1; -; mRNA.
DR EMBL; S77512; AAB34682.2; -; mRNA.
DR CCDS; CCDS2789.1; -.
DR PIR; A55677; A55677.
DR PIR; S53869; S53869.
DR RefSeq; NP_002283.3; NM_002292.3.
DR RefSeq; XP_005265184.1; XM_005265127.3.
DR AlphaFoldDB; P55268; -.
DR SMR; P55268; -.
DR BioGRID; 110107; 157.
DR ComplexPortal; CPX-1772; Laminin-121 complex.
DR ComplexPortal; CPX-1773; Laminin-221 complex.
DR ComplexPortal; CPX-1776; Laminin-321 complex.
DR ComplexPortal; CPX-1778; Laminin-421 complex.
DR ComplexPortal; CPX-1780; Laminin-521 complex.
DR ComplexPortal; CPX-1782; Laminin-423 complex.
DR ComplexPortal; CPX-1783; Laminin-522 complex.
DR ComplexPortal; CPX-1784; Laminin-523 complex.
DR CORUM; P55268; -.
DR DIP; DIP-42106N; -.
DR IntAct; P55268; 39.
DR MINT; P55268; -.
DR STRING; 9606.ENSP00000388325; -.
DR ChEMBL; CHEMBL2364187; -.
DR GlyConnect; 1443; 4 N-Linked glycans (4 sites).
DR GlyGen; P55268; 10 sites, 4 N-linked glycans (4 sites), 2 O-linked glycans (3 sites).
DR iPTMnet; P55268; -.
DR PhosphoSitePlus; P55268; -.
DR SwissPalm; P55268; -.
DR BioMuta; LAMB2; -.
DR DMDM; 156630892; -.
DR EPD; P55268; -.
DR jPOST; P55268; -.
DR MassIVE; P55268; -.
DR MaxQB; P55268; -.
DR PaxDb; P55268; -.
DR PeptideAtlas; P55268; -.
DR PRIDE; P55268; -.
DR ProteomicsDB; 56831; -.
DR Antibodypedia; 995; 390 antibodies from 30 providers.
DR DNASU; 3913; -.
DR Ensembl; ENST00000305544.9; ENSP00000307156.4; ENSG00000172037.14.
DR Ensembl; ENST00000418109.5; ENSP00000388325.1; ENSG00000172037.14.
DR GeneID; 3913; -.
DR KEGG; hsa:3913; -.
DR MANE-Select; ENST00000305544.9; ENSP00000307156.4; NM_002292.4; NP_002283.3.
DR UCSC; uc003cwe.4; human.
DR CTD; 3913; -.
DR DisGeNET; 3913; -.
DR GeneCards; LAMB2; -.
DR GeneReviews; LAMB2; -.
DR HGNC; HGNC:6487; LAMB2.
DR HPA; ENSG00000172037; Low tissue specificity.
DR MalaCards; LAMB2; -.
DR MIM; 150325; gene.
DR MIM; 609049; phenotype.
DR MIM; 614199; phenotype.
DR neXtProt; NX_P55268; -.
DR OpenTargets; ENSG00000172037; -.
DR Orphanet; 2670; Pierson syndrome.
DR Orphanet; 98915; Synaptic congenital myasthenic syndromes.
DR PharmGKB; PA164741827; -.
DR VEuPathDB; HostDB:ENSG00000172037; -.
DR eggNOG; KOG0994; Eukaryota.
DR GeneTree; ENSGT00940000156060; -.
DR HOGENOM; CLU_001560_1_0_1; -.
DR InParanoid; P55268; -.
DR OMA; CFNNWDI; -.
DR OrthoDB; 65841at2759; -.
DR PhylomeDB; P55268; -.
DR TreeFam; TF312903; -.
DR PathwayCommons; P55268; -.
DR Reactome; R-HSA-3000157; Laminin interactions.
DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8874081; MET activates PTK2 signaling.
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; P55268; -.
DR SIGNOR; P55268; -.
DR BioGRID-ORCS; 3913; 14 hits in 1080 CRISPR screens.
DR ChiTaRS; LAMB2; human.
DR GeneWiki; Laminin,_beta_2; -.
DR GenomeRNAi; 3913; -.
DR Pharos; P55268; Tbio.
DR PRO; PR:P55268; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P55268; protein.
DR Bgee; ENSG00000172037; Expressed in apex of heart and 178 other tissues.
DR ExpressionAtlas; P55268; baseline and differential.
DR Genevisible; P55268; HS.
DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0043256; C:laminin complex; IBA:GO_Central.
DR GO; GO:0043260; C:laminin-11 complex; TAS:BHF-UCL.
DR GO; GO:0005608; C:laminin-3 complex; IPI:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0098637; C:protein complex involved in cell-matrix adhesion; IC:ComplexPortal.
DR GO; GO:0043083; C:synaptic cleft; IEA:Ensembl.
DR GO; GO:0005201; F:extracellular matrix structural constituent; ISS:BHF-UCL.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; NAS:ProtInc.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
DR GO; GO:0048677; P:axon extension involved in regeneration; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR GO; GO:0070831; P:basement membrane assembly; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0072274; P:metanephric glomerular basement membrane development; IEA:Ensembl.
DR GO; GO:0072249; P:metanephric podocyte development; IEA:Ensembl.
DR GO; GO:0007528; P:neuromuscular junction development; IEA:Ensembl.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IC:ComplexPortal.
DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IC:ComplexPortal.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; IC:ComplexPortal.
DR GO; GO:0110011; P:regulation of basement membrane organization; IC:ComplexPortal.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0014044; P:Schwann cell development; IEA:Ensembl.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR CDD; cd00055; EGF_Lam; 13.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013015; Laminin_IV_B.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00053; Laminin_EGF; 13.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00181; EGF; 9.
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; 12.
DR PROSITE; PS50027; EGF_LAM_2; 13.
DR PROSITE; PS51116; LAMININ_IVB; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 1: Evidence at protein level;
KW Basement membrane; Cell adhesion; Coiled coil; Disease variant;
KW Disulfide bond; Extracellular matrix; Glycoprotein;
KW Laminin EGF-like domain; Phosphoprotein; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..1798
FT /note="Laminin subunit beta-2"
FT /id="PRO_0000017068"
FT DOMAIN 43..282
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 283..346
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 347..409
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 410..469
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 470..521
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 522..552
FT /note="Laminin EGF-like 5; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 561..777
FT /note="Laminin IV type B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00462"
FT DOMAIN 783..830
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 831..876
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 877..926
FT /note="Laminin EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 927..985
FT /note="Laminin EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 986..1037
FT /note="Laminin EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1038..1094
FT /note="Laminin EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1095..1142
FT /note="Laminin EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1143..1189
FT /note="Laminin EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 1190..1409
FT /note="Domain II"
FT REGION 1338..1364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1410..1442
FT /note="Domain alpha"
FT REGION 1443..1798
FT /note="Domain I"
FT COILED 1253..1319
FT /evidence="ECO:0000255"
FT COILED 1472..1526
FT /evidence="ECO:0000255"
FT COILED 1577..1790
FT /evidence="ECO:0000255"
FT MOD_RES 1532
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1085
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 1348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 1499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT DISULFID 283..292
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 285..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 312..321
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 324..344
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 347..356
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 349..374
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 377..386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 389..407
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 410..423
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 412..438
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 440..449
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 452..467
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 470..484
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 472..491
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 493..502
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 505..519
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 522..534
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 524..541
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 543..552
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 783..795
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 785..802
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 804..813
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 816..828
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 831..843
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 833..850
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 852..861
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 864..874
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 877..886
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 879..893
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 896..905
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 908..924
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 927..943
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 929..954
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 956..965
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 968..983
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 986..1000
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 988..1007
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1010..1019
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1022..1035
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1038..1058
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1040..1065
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1067..1076
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1079..1092
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1095..1107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1097..1114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1116..1125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1128..1140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1143..1155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1145..1162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1164..1173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1176..1187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1190
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 1193
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 1797
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT VARIANT 147
FT /note="H -> R (in NPHS5; dbSNP:rs387906644)"
FT /evidence="ECO:0000269|PubMed:21236492"
FT /id="VAR_066492"
FT VARIANT 246
FT /note="R -> Q (in PIERSS; without ocular abnormalities;
FT dbSNP:rs121912491)"
FT /evidence="ECO:0000269|PubMed:16912710"
FT /id="VAR_031968"
FT VARIANT 246
FT /note="R -> W (in PIERSS; dbSNP:rs121912488)"
FT /evidence="ECO:0000269|PubMed:15367484"
FT /id="VAR_031969"
FT VARIANT 321
FT /note="C -> R (in PIERSS and NPHS5; with mild ocular
FT abnormalities; dbSNP:rs121912492)"
FT /evidence="ECO:0000269|PubMed:16912710,
FT ECO:0000269|PubMed:20798252"
FT /id="VAR_031970"
FT VARIANT 987
FT /note="E -> K (in dbSNP:rs34759087)"
FT /id="VAR_031971"
FT VARIANT 1380
FT /note="N -> K (in PIERSS and NPHS5; with mild ocular
FT abnormalities; associated with F-1393; dbSNP:rs267607207)"
FT /evidence="ECO:0000269|PubMed:16912710,
FT ECO:0000269|PubMed:20798252"
FT /id="VAR_031972"
FT VARIANT 1393
FT /note="L -> F (in PIERSS and NPHS5; with mild ocular
FT abnormalities; associated with K-1380; dbSNP:rs267607208)"
FT /evidence="ECO:0000269|PubMed:16912710,
FT ECO:0000269|PubMed:20798252"
FT /id="VAR_031973"
FT CONFLICT 914
FT /note="G -> R (in Ref. 1; CAA92279)"
FT /evidence="ECO:0000305"
FT CONFLICT 1179
FT /note="G -> A (in Ref. 2; AAB34682)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1798 AA; 195981 MW; FFB3531AD13E1486 CRC64;
MELTSRERGR GQPLPWELRL GLLLSVLAAT LAQAPAPDVP GCSRGSCYPA TGDLLVGRAD
RLTASSTCGL NGPQPYCIVS HLQDEKKCFL CDSRRPFSAR DNPHSHRIQN VVTSFAPQRR
AAWWQSENGI PAVTIQLDLE AEFHFTHLIM TFKTFRPAAM LVERSADFGR TWHVYRYFSY
DCGADFPGVP LAPPRHWDDV VCESRYSEIE PSTEGEVIYR VLDPAIPIPD PYSSRIQNLL
KITNLRVNLT RLHTLGDNLL DPRREIREKY YYALYELVVR GNCFCYGHAS ECAPAPGAPA
HAEGMVHGAC ICKHNTRGLN CEQCQDFYRD LPWRPAEDGH SHACRKCECH GHTHSCHFDM
AVYLASGNVS GGVCDGCQHN TAGRHCELCR PFFYRDPTKD LRDPAVCRSC DCDPMGSQDG
GRCDSHDDPA LGLVSGQCRC KEHVVGTRCQ QCRDGFFGLS ISDRLGCRRC QCNARGTVPG
STPCDPNSGS CYCKRLVTGR GCDRCLPGHW GLSHDLLGCR PCDCDVGGAL DPQCDEGTGQ
CHCRQHMVGR RCEQVQPGYF RPFLDHLIWE AEDTRGQVLD VVERLVTPGE TPSWTGSGFV
RLQEGQTLEF LVASVPKAMD YDLLLRLEPQ VPEQWAELEL IVQRPGPVPA HSLCGHLVPK
DDRIQGTLQP HARYLIFPNP VCLEPGISYK LHLKLVRTGG SAQPETPYSG PGLLIDSLVL
LPRVLVLEMF SGGDAAALER QATFERYQCH EEGLVPSKTS PSEACAPLLI SLSTLIYNGA
LPCQCNPQGS LSSECNPHGG QCLCKPGVVG RRCDLCAPGY YGFGPTGCQA CQCSHEGALS
SLCEKTSGQC LCRTGAFGLR CDRCQRGQWG FPSCRPCVCN GHADECNTHT GACLGCRDHT
GGEHCERCIA GFHGDPRLPY GGQCRPCPCP EGPGSQRHFA TSCHQDEYSQ QIVCHCRAGY
TGLRCEACAP GHFGDPSRPG GRCQLCECSG NIDPMDPDAC DPHTGQCLRC LHHTEGPHCA
HCKPGFHGQA ARQSCHRCTC NLLGTNPQQC PSPDQCHCDP SSGQCPCLPN VQGPSCDRCA
PNFWNLTSGH GCQPCACHPS RARGPTCNEF TGQCHCRAGF GGRTCSECQE LHWGDPGLQC
HACDCDSRGI DTPQCHRFTG HCSCRPGVSG VRCDQCARGF SGIFPACHPC HACFGDWDRV
VQDLAARTQR LEQRAQELQQ TGVLGAFESS FWHMQEKLGI VQGIVGARNT SAASTAQLVE
ATEELRREIG EATEHLTQLE ADLTDVQDEN FNANHALSGL ERDRLALNLT LRQLDQHLDL
LKHSNFLGAY DSIRHAHSQS AEAERRANTS ALAVPSPVSN SASARHRTEA LMDAQKEDFN
SKHMANQRAL GKLSAHTHTL SLTDINELVC GAPGDAPCAT SPCGGAGCRD EDGQPRCGGL
SCNGAAATAD LALGRARHTQ AELQRALAEG GSILSRVAET RRQASEAQQR AQAALDKANA
SRGQVEQANQ ELQELIQSVK DFLNQEGADP DSIEMVATRV LELSIPASAE QIQHLAGAIA
ERVRSLADVD AILARTVGDV RRAEQLLQDA RRARSWAEDE KQKAETVQAA LEEAQRAQGI
AQGAIRGAVA DTRDTEQTLY QVQERMAGAE RALSSAGERA RQLDALLEAL KLKRAGNSLA
ASTAEETAGS AQGRAQEAEQ LLRGPLGDQY QTVKALAERK AQGVLAAQAR AEQLRDEARD
LLQAAQDKLQ RLQELEGTYE ENERALESKA AQLDGLEARM RSVLQAINLQ VQIYNTCQ
