ID LAMC1_HUMAN Reviewed; 1609 AA. AC P11047; Q5VYE7; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 3. DT 24-JUL-2024, entry version 244. DE RecName: Full=Laminin subunit gamma-1; DE AltName: Full=Laminin B2 chain; DE AltName: Full=Laminin-1 subunit gamma; DE AltName: Full=Laminin-10 subunit gamma; DE AltName: Full=Laminin-11 subunit gamma; DE AltName: Full=Laminin-2 subunit gamma; DE AltName: Full=Laminin-3 subunit gamma; DE AltName: Full=Laminin-4 subunit gamma; DE AltName: Full=Laminin-6 subunit gamma; DE AltName: Full=Laminin-7 subunit gamma; DE AltName: Full=Laminin-8 subunit gamma; DE AltName: Full=Laminin-9 subunit gamma; DE AltName: Full=S-laminin subunit gamma; DE Short=S-LAM gamma; DE Flags: Precursor; GN Name=LAMC1 {ECO:0000303|PubMed:28397838, ECO:0000312|HGNC:HGNC:6492}; GN Synonyms=LAMB2; 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], AND VARIANTS VAL-458 AND PRO-888. RX PubMed=3360804; DOI=10.1016/s0021-9258(18)68707-1; RA Pikkarainen T., Kallunki T., Tryggvason K.; RT "Human laminin B2 chain. Comparison of the complete amino acid sequence RT with the B1 chain reveals variability in sequence homology between RT different structural domains."; RL J. Biol. Chem. 263:6751-6758(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-458 AND PRO-888. RX PubMed=1985895; DOI=10.1016/s0021-9258(18)52424-8; RA Kallunki T., Ikonen J., Chow L.T., Kallunki P., Tryggvason K.; RT "Structure of the human laminin B2 chain gene reveals extensive divergence RT from the laminin B1 chain gene."; RL J. Biol. Chem. 266:221-228(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1282-1609. RC TISSUE=Endothelial cell; RX PubMed=1806043; DOI=10.3109/10425179109020782; RA Santos C.L.S., Sabbaga J., Brentani R.; RT "Differences in human laminin B2 sequences."; RL DNA Seq. 1:275-277(1991). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1393-1609. RX PubMed=3234037; DOI=10.1159/000132610; RA Fukushima Y., Pikkarainen T., Kallunki T., Eddy R.L., Byers M.G., RA Haley L.L., Henry W.M., Tryggvason K., Shows T.B.; RT "Isolation of a human laminin B2 (LAMB2) cDNA clone and assignment of the RT gene to chromosome region 1q25-->q31."; RL Cytogenet. Cell Genet. 48:137-141(1988). RN [6] RP GLYCOSYLATION AT ASN-650. RX PubMed=12754519; DOI=10.1038/nbt827; RA Zhang H., Li X.-J., Martin D.B., Aebersold R.; RT "Identification and quantification of N-linked glycoproteins using RT hydrazide chemistry, stable isotope labeling and mass spectrometry."; RL Nat. Biotechnol. 21:660-666(2003). RN [7] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1107; ASN-1161; ASN-1175; RP ASN-1223 AND ASN-1395. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-650; ASN-1107; ASN-1241 AND RP ASN-1395. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [9] RP 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1493, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., RA Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [12] 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 [13] RP PHOSPHORYLATION AT SER-1149. 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 [14] RP VARIANT [LARGE SCALE ANALYSIS] HIS-1116. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [15] RP VARIANT LEU-363. RX PubMed=28397838; DOI=10.1038/mp.2017.60; RA Harripaul R., Vasli N., Mikhailov A., Rafiq M.A., Mittal K., RA Windpassinger C., Sheikh T.I., Noor A., Mahmood H., Downey S., Johnson M., RA Vleuten K., Bell L., Ilyas M., Khan F.S., Khan V., Moradi M., Ayaz M., RA Naeem F., Heidari A., Ahmed I., Ghadami S., Agha Z., Zeinali S., Qamar R., RA Mozhdehipanah H., John P., Mir A., Ansar M., French L., Ayub M., RA Vincent J.B.; RT "Mapping autosomal recessive intellectual disability: combined microarray RT and exome sequencing identifies 26 novel candidate genes in 192 RT consanguineous families."; RL Mol. Psychiatry 23:973-984(2018). 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. Gamma-1 is a CC subunit of laminin-1 (laminin-111 or EHS laminin), laminin-2 (laminin- CC 211 or merosin), laminin-3 (laminin-121 or S-laminin), laminin-4 CC (laminin-221 or S-merosin), laminin-6 (laminin-311 or K-laminin), CC laminin-7 (laminin-321 or KS-laminin), laminin-8 (laminin-411), CC laminin-9 (laminin-421), laminin-10 (laminin-511) and laminin-11 CC (laminin-521). Interacts with SVEP1 (By similarity). CC {ECO:0000250|UniProtKB:P02468}. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix, basement membrane. CC -!- TISSUE SPECIFICITY: Found in the basement membranes (major component). 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 --------------------------------------------------------------------------- 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; J03202; AAA59488.1; -; mRNA. DR EMBL; M55210; AAA59492.1; -; Genomic_DNA. DR EMBL; M55217; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; M55201; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; M55211; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; M55212; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; M55213; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; M55214; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; M55215; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; M55216; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; M55192; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; M55193; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; M55194; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; M55195; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; M55196; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; M55197; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; M55198; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; M55199; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; M55200; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; M55202; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; M55203; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; M55204; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; M55205; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; M55206; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; M55207; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; M55208; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; M55209; AAA59492.1; JOINED; Genomic_DNA. DR EMBL; AL354953; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL450304; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X13939; CAA32122.1; -; mRNA. DR EMBL; M27654; AAA59489.1; -; mRNA. DR CCDS; CCDS1351.1; -. DR PIR; S13548; MMHUB2. DR RefSeq; NP_002284.3; NM_002293.3. DR PDB; 5XAU; X-ray; 1.80 A; C/F=1528-1609. DR PDB; 7CEC; EM; 3.90 A; E=1528-1609. DR PDB; 8DMK; EM; 3.70 A; G=37-341. DR PDBsum; 5XAU; -. DR PDBsum; 7CEC; -. DR PDBsum; 8DMK; -. DR AlphaFoldDB; P11047; -. DR EMDB; EMD-27542; -. DR EMDB; EMD-30342; -. DR SMR; P11047; -. DR BioGRID; 110109; 156. DR ComplexPortal; CPX-1770; Laminin-111 complex. DR ComplexPortal; CPX-1771; Laminin-211 complex. DR ComplexPortal; CPX-1772; Laminin-121 complex. DR ComplexPortal; CPX-1773; Laminin-221 complex. DR ComplexPortal; CPX-1775; Laminin-311 complex variant A. DR ComplexPortal; CPX-1776; Laminin-321 complex. DR ComplexPortal; CPX-1777; Laminin-411 complex. DR ComplexPortal; CPX-1778; Laminin-421 complex. DR ComplexPortal; CPX-1779; Laminin-511 complex. DR ComplexPortal; CPX-1780; Laminin-521 complex. DR ComplexPortal; CPX-3166; Laminin-311 complex variant B. DR CORUM; P11047; -. DR IntAct; P11047; 29. DR MINT; P11047; -. DR STRING; 9606.ENSP00000258341; -. DR ChEMBL; CHEMBL2364187; -. DR DrugBank; DB06245; Lanoteplase. DR CarbonylDB; P11047; -. DR GlyConnect; 1444; 60 N-Linked glycans (9 sites). DR GlyCosmos; P11047; 19 sites, 67 glycans. DR GlyGen; P11047; 23 sites, 66 N-linked glycans (9 sites), 5 O-linked glycans (9 sites). DR iPTMnet; P11047; -. DR PhosphoSitePlus; P11047; -. DR SwissPalm; P11047; -. DR BioMuta; LAMC1; -. DR DMDM; 224471885; -. DR jPOST; P11047; -. DR MassIVE; P11047; -. DR PaxDb; 9606-ENSP00000258341; -. DR PeptideAtlas; P11047; -. DR ProteomicsDB; 52689; -. DR Pumba; P11047; -. DR Antibodypedia; 1055; 583 antibodies from 36 providers. DR DNASU; 3915; -. DR Ensembl; ENST00000258341.5; ENSP00000258341.3; ENSG00000135862.6. DR GeneID; 3915; -. DR KEGG; hsa:3915; -. DR MANE-Select; ENST00000258341.5; ENSP00000258341.3; NM_002293.4; NP_002284.3. DR UCSC; uc001gpy.4; human. DR AGR; HGNC:6492; -. DR CTD; 3915; -. DR DisGeNET; 3915; -. DR GeneCards; LAMC1; -. DR HGNC; HGNC:6492; LAMC1. DR HPA; ENSG00000135862; Tissue enhanced (placenta). DR MIM; 150290; gene. DR neXtProt; NX_P11047; -. DR OpenTargets; ENSG00000135862; -. DR PharmGKB; PA30280; -. DR VEuPathDB; HostDB:ENSG00000135862; -. DR eggNOG; KOG1836; Eukaryota. DR GeneTree; ENSGT00940000158069; -. DR HOGENOM; CLU_002471_1_0_1; -. DR InParanoid; P11047; -. DR OMA; QGCTACF; -. DR OrthoDB; 90222at2759; -. DR PhylomeDB; P11047; -. DR TreeFam; TF352481; -. DR PathwayCommons; P11047; -. DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix. 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-373760; L1CAM interactions. 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 Reactome; R-HSA-9619665; EGR2 and SOX10-mediated initiation of Schwann cell myelination. DR SignaLink; P11047; -. DR SIGNOR; P11047; -. DR BioGRID-ORCS; 3915; 11 hits in 1153 CRISPR screens. DR ChiTaRS; LAMC1; human. DR GeneWiki; Laminin,_gamma_1; -. DR GenomeRNAi; 3915; -. DR Pharos; P11047; Tbio. DR PRO; PR:P11047; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P11047; Protein. DR Bgee; ENSG00000135862; Expressed in stromal cell of endometrium and 209 other cell types or tissues. DR ExpressionAtlas; P11047; baseline and differential. DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB. 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:0005615; C:extracellular space; NAS:UniProtKB. DR GO; GO:0005606; C:laminin-1 complex; TAS:HGNC-UCL. DR GO; GO:0043259; C:laminin-10 complex; TAS:BHF-UCL. DR GO; GO:0043260; C:laminin-11 complex; TAS:BHF-UCL. DR GO; GO:0098637; C:protein complex involved in cell-matrix adhesion; NAS:ComplexPortal. DR GO; GO:0005201; F:extracellular matrix structural constituent; IMP:HGNC-UCL. DR GO; GO:0007155; P:cell adhesion; IDA:HGNC-UCL. DR GO; GO:0016477; P:cell migration; IMP:HGNC-UCL. DR GO; GO:0007492; P:endoderm development; TAS:ProtInc. DR GO; GO:0022617; P:extracellular matrix disassembly; IMP:HGNC-UCL. DR GO; GO:0031581; P:hemidesmosome assembly; IMP:HGNC-UCL. DR GO; GO:0035633; P:maintenance of blood-brain barrier; NAS:ARUK-UCL. DR GO; GO:0045785; P:positive regulation of cell adhesion; NAS:ComplexPortal. DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; TAS:HGNC-UCL. 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:0065003; P:protein-containing complex assembly; IDA:HGNC-UCL. DR GO; GO:0110011; P:regulation of basement membrane organization; NAS:ComplexPortal. DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:BHF-UCL. DR CDD; cd00055; EGF_Lam; 10. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR Gene3D; 2.10.25.10; Laminin; 9. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR050440; Laminin/Netrin_ECM. DR InterPro; IPR000034; Laminin_IV. DR InterPro; IPR008211; Laminin_N. DR InterPro; IPR002049; LE_dom. DR PANTHER; PTHR10574:SF270; LAMININ SUBUNIT GAMMA-1; 1. DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1. DR Pfam; PF00052; Laminin_B; 1. DR Pfam; PF00053; Laminin_EGF; 10. DR Pfam; PF00055; Laminin_N; 1. DR PRINTS; PR00011; EGFLAMININ. DR SMART; SM00181; EGF; 8. DR SMART; SM00180; EGF_Lam; 10. DR SMART; SM00281; LamB; 1. DR SMART; SM00136; LamNT; 1. DR SUPFAM; SSF57196; EGF/Laminin; 10. DR SUPFAM; SSF57997; Tropomyosin; 1. DR PROSITE; PS00022; EGF_1; 8. DR PROSITE; PS01186; EGF_2; 2. DR PROSITE; PS01248; EGF_LAM_1; 11. DR PROSITE; PS50027; EGF_LAM_2; 10. DR PROSITE; PS51115; LAMININ_IVA; 1. DR PROSITE; PS51117; LAMININ_NTER; 1. PE 1: Evidence at protein level; KW 3D-structure; Basement membrane; Cell adhesion; Coiled coil; KW Disulfide bond; Extracellular matrix; Glycoprotein; KW Laminin EGF-like domain; Phosphoprotein; Reference proteome; Repeat; KW Secreted; Signal. FT SIGNAL 1..33 FT CHAIN 34..1609 FT /note="Laminin subunit gamma-1" FT /id="PRO_0000017074" FT DOMAIN 46..285 FT /note="Laminin N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466" FT DOMAIN 286..341 FT /note="Laminin EGF-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 342..397 FT /note="Laminin EGF-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 398..444 FT /note="Laminin EGF-like 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 445..494 FT /note="Laminin EGF-like 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 495..504 FT /note="Laminin EGF-like 5; first part" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 514..689 FT /note="Laminin IV type A" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00458" FT DOMAIN 690..723 FT /note="Laminin EGF-like 5; second part" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 724..772 FT /note="Laminin EGF-like 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 773..827 FT /note="Laminin EGF-like 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 828..883 FT /note="Laminin EGF-like 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 884..934 FT /note="Laminin EGF-like 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 935..982 FT /note="Laminin EGF-like 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 983..1030 FT /note="Laminin EGF-like 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT REGION 1030..1609 FT /note="Domain II and I" FT COILED 1038..1609 FT /evidence="ECO:0000255" FT MOD_RES 1149 FT /note="Phosphoserine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039" FT MOD_RES 1493 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT CARBOHYD 60 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 134 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 576 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 650 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12754519, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 1022 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1107 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 1161 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT CARBOHYD 1175 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT CARBOHYD 1205 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1223 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT CARBOHYD 1241 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 1380 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1395 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 1439 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 286..295 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 288..305 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 307..316 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 319..339 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 342..351 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 344..367 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 370..379 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 382..395 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 398..410 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 400..416 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 418..427 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 430..442 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 445..456 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 447..463 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 465..474 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 477..492 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 724..733 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 726..740 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 742..751 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 754..770 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 773..781 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 775..792 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 795..804 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 807..825 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 828..842 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 830..849 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 852..861 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 864..881 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 884..898 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 886..905 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 907..916 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 919..932 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 935..947 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 937..954 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 956..965 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 968..980 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 983..995 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 985..1001 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 1003..1012 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 1015..1028 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 1031 FT /note="Interchain" FT /evidence="ECO:0000305" FT DISULFID 1034 FT /note="Interchain" FT /evidence="ECO:0000305" FT DISULFID 1600 FT /note="Interchain" FT /evidence="ECO:0000305" FT VARIANT 363 FT /note="H -> L (found in a consanguineous family with FT intellectual disability; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28397838" FT /id="VAR_080757" FT VARIANT 458 FT /note="I -> V (in dbSNP:rs20563)" FT /evidence="ECO:0000269|PubMed:1985895, FT ECO:0000269|PubMed:3360804" FT /id="VAR_014700" FT VARIANT 731 FT /note="E -> K (in dbSNP:rs2230157)" FT /id="VAR_054488" FT VARIANT 888 FT /note="L -> P (in dbSNP:rs20558)" FT /evidence="ECO:0000269|PubMed:1985895, FT ECO:0000269|PubMed:3360804" FT /id="VAR_014701" FT VARIANT 1116 FT /note="R -> H (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs548688323)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035821" FT VARIANT 1121 FT /note="R -> Q (in dbSNP:rs20559)" FT /id="VAR_014702" FT CONFLICT 212 FT /note="I -> F (in Ref. 2; AAA59492)" FT /evidence="ECO:0000305" FT HELIX 1536..1552 FT /evidence="ECO:0007829|PDB:5XAU" FT HELIX 1554..1595 FT /evidence="ECO:0007829|PDB:5XAU" SQ SEQUENCE 1609 AA; 177603 MW; 42D9A9958EEBBB01 CRC64; MRGSHRAAPA LRPRGRLWPV LAVLAAAAAA GCAQAAMDEC TDEGGRPQRC MPEFVNAAFN VTVVATNTCG TPPEEYCVQT GVTGVTKSCH LCDAGQPHLQ HGAAFLTDYN NQADTTWWQS QTMLAGVQYP SSINLTLHLG KAFDITYVRL KFHTSRPESF AIYKRTREDG PWIPYQYYSG SCENTYSKAN RGFIRTGGDE QQALCTDEFS DISPLTGGNV AFSTLEGRPS AYNFDNSPVL QEWVTATDIR VTLNRLNTFG DEVFNDPKVL KSYYYAISDF AVGGRCKCNG HASECMKNEF DKLVCNCKHN TYGVDCEKCL PFFNDRPWRR ATAESASECL PCDCNGRSQE CYFDPELYRS TGHGGHCTNC QDNTDGAHCE RCRENFFRLG NNEACSSCHC SPVGSLSTQC DSYGRCSCKP GVMGDKCDRC QPGFHSLTEA GCRPCSCDPS GSIDECNIET GRCVCKDNVE GFNCERCKPG FFNLESSNPR GCTPCFCFGH SSVCTNAVGY SVYSISSTFQ IDEDGWRAEQ RDGSEASLEW SSERQDIAVI SDSYFPRYFI APAKFLGKQV LSYGQNLSFS FRVDRRDTRL SAEDLVLEGA GLRVSVPLIA QGNSYPSETT VKYVFRLHEA TDYPWRPALT PFEFQKLLNN LTSIKIRGTY SERSAGYLDD VTLASARPGP GVPATWVESC TCPVGYGGQF CEMCLSGYRR ETPNLGPYSP CVLCACNGHS ETCDPETGVC NCRDNTAGPH CEKCSDGYYG DSTAGTSSDC QPCPCPGGSS CAVVPKTKEV VCTNCPTGTT GKRCELCDDG YFGDPLGRNG PVRLCRLCQC SDNIDPNAVG NCNRLTGECL KCIYNTAGFY CDRCKDGFFG NPLAPNPADK CKACNCNLYG TMKQQSSCNP VTGQCECLPH VTGQDCGACD PGFYNLQSGQ GCERCDCHAL GSTNGQCDIR TGQCECQPGI TGQHCERCEV NHFGFGPEGC KPCDCHPEGS LSLQCKDDGR CECREGFVGN RCDQCEENYF YNRSWPGCQE CPACYRLVKD KVADHRVKLQ ELESLIANLG TGDEMVTDQA FEDRLKEAER EVMDLLREAQ DVKDVDQNLM DRLQRVNNTL SSQISRLQNI RNTIEETGNL AEQARAHVEN TERLIEIASR ELEKAKVAAA NVSVTQPEST GDPNNMTLLA EEARKLAERH KQEADDIVRV AKTANDTSTE AYNLLLRTLA GENQTAFEIE ELNRKYEQAK NISQDLEKQA ARVHEEAKRA GDKAVEIYAS VAQLSPLDSE TLENEANNIK MEAENLEQLI DQKLKDYEDL REDMRGKELE VKNLLEKGKT EQQTADQLLA RADAAKALAE EAAKKGRDTL QEANDILNNL KDFDRRVNDN KTAAEEALRK IPAINQTITE ANEKTREAQQ ALGSAAADAT EAKNKAHEAE RIASAVQKNA TSTKAEAERT FAEVTDLDNE VNNMLKQLQE AEKELKRKQD DADQDMMMAG MASQAAQEAE INARKAKNSV TSLLSIINDL LEQLGQLDTV DLNKLNEIEG TLNKAKDEMK VSDLDRKVSD LENEAKKQEA AIMDYNRDIE EIMKDIRNLE DIRKTLPSGC FNTPSIEKP //