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 27-MAR-2024, entry version 212. 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 PIERS 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 NPHS5 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). RN [11] RP VARIANTS NPHS5 HIS-644 AND VAL-1258, AND VARIANTS GLU-700; HIS-1148 AND RP THR-1765. RX PubMed=23595123; DOI=10.1038/jhg.2013.27; RA Al-Hamed M.H., Al-Sabban E., Al-Mojalli H., Al-Harbi N., Faqeih E., RA Al Shaya H., Alhasan K., Al-Hissi S., Rajab M., Edwards N., Al-Abbad A., RA Al-Hassoun I., Sayer J.A., Meyer B.F.; RT "A molecular genetic analysis of childhood nephrotic syndrome in a cohort RT of Saudi Arabian families."; RL J. Hum. Genet. 58:480-489(2013). 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 (PIERS) [MIM:609049]: An autosomal recessive CC disorder characterized by nephrotic syndrome with neonatal onset, CC diffuse mesangial sclerosis, and eye abnormalities with microcoria and CC hypoplasia of the ciliary and pupillary muscles. Death usually occurs CC within the first weeks of life. Patients who survive tend to show CC neurodevelopmental delay and visual loss. CC {ECO:0000269|PubMed:15367484}. Note=The disease is caused by variants CC affecting the gene represented in this 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:16912710, ECO:0000269|PubMed:20798252, CC ECO:0000269|PubMed:21236492, ECO:0000269|PubMed:23595123}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 164. 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.ENSP00000307156; -. DR ChEMBL; CHEMBL2364187; -. DR GlyConnect; 1443; 4 N-Linked glycans (4 sites). DR GlyCosmos; P55268; 10 sites, 6 glycans. 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; 9606-ENSP00000388325; -. DR PeptideAtlas; P55268; -. DR ProteomicsDB; 56831; -. DR Pumba; P55268; -. DR Antibodypedia; 995; 428 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 AGR; HGNC:6487; -. 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; SCRDHTG; -. DR OrthoDB; 90222at2759; -. 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 1160 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 180 other cell types or tissues. DR ExpressionAtlas; P55268; baseline and differential. 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: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; NAS: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; IEA:Ensembl. DR GO; GO:0150043; F:structural constituent of synapse-associated extracellular matrix; IEA:Ensembl. DR GO; GO:0005198; F:structural molecule activity; NAS:ProtInc. 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:0007155; P:cell adhesion; IEA:UniProtKB-KW. 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; NAS:ComplexPortal. DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; NAS:ComplexPortal. DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; NAS:ComplexPortal. DR GO; GO:0110011; P:regulation of basement membrane organization; NAS: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:0007601; P:visual perception; IEA:Ensembl. DR CDD; cd22299; cc_LAMB2_C; 1. DR CDD; cd00055; EGF_Lam; 13. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR Gene3D; 2.10.25.10; Laminin; 9. DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 2. DR InterPro; IPR000742; EGF-like_dom. 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; 13. DR Pfam; PF21199; LAMININ_IV_B; 1. DR Pfam; PF00055; Laminin_N; 1. DR PRINTS; PR00011; EGFLAMININ. DR SMART; SM00181; EGF; 9. 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; 12. DR PROSITE; PS50027; EGF_LAM_2; 13. DR PROSITE; PS51116; LAMININ_IVB; 1. DR PROSITE; PS51117; LAMININ_NTER; 1. DR Genevisible; P55268; HS. 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 NPHS5; dbSNP:rs121912491)" FT /evidence="ECO:0000269|PubMed:16912710" FT /id="VAR_031968" FT VARIANT 246 FT /note="R -> W (in PIERS; dbSNP:rs121912488)" FT /evidence="ECO:0000269|PubMed:15367484" FT /id="VAR_031969" FT VARIANT 321 FT /note="C -> R (in NPHS5; dbSNP:rs121912492)" FT /evidence="ECO:0000269|PubMed:16912710, FT ECO:0000269|PubMed:20798252" FT /id="VAR_031970" FT VARIANT 644 FT /note="R -> H (in NPHS5; uncertain significance; FT dbSNP:rs200738080)" FT /evidence="ECO:0000269|PubMed:23595123" FT /id="VAR_087602" FT VARIANT 700 FT /note="G -> E (in dbSNP:rs142860588)" FT /evidence="ECO:0000269|PubMed:23595123" FT /id="VAR_087603" FT VARIANT 987 FT /note="E -> K (in dbSNP:rs34759087)" FT /id="VAR_031971" FT VARIANT 1148 FT /note="R -> H (in dbSNP:rs138774635)" FT /evidence="ECO:0000269|PubMed:23595123" FT /id="VAR_087604" FT VARIANT 1258 FT /note="L -> V (in NPHS5; uncertain significance; FT dbSNP:rs771785818)" FT /evidence="ECO:0000269|PubMed:23595123" FT /id="VAR_087605" FT VARIANT 1380 FT /note="N -> K (in NPHS5; associated in cis with F-1393; FT 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 NPHS5; associated in cis with K-1380; FT dbSNP:rs267607208)" FT /evidence="ECO:0000269|PubMed:16912710, FT ECO:0000269|PubMed:20798252" FT /id="VAR_031973" FT VARIANT 1765 FT /note="A -> T (in dbSNP:rs74951356)" FT /evidence="ECO:0000269|PubMed:23595123" FT /id="VAR_087606" 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 //