ID LMA2_MOUSE STANDARD; PRT; 3106 AA. AC Q60675; Q05003; Q64061; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 05-JUL-2004 (Rel. 44, Last annotation update) DE Laminin alpha-2 chain precursor (Laminin M chain) (Merosin heavy DE chain). GN Name=Lama2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=FVB/N; TISSUE=Embryo, and Heart; RX MEDLINE=95316259; PubMed=7795883; RA Bernier S.M., Utani A., Sugiyama S., Doi T., Polistina C., Yamada Y.; RT "Cloning and expression of laminin alpha 2 chain (M-chain) in the RT mouse."; RL Matrix Biol. 14:447-455(1995). RN [2] RP SEQUENCE OF 2162-2279 FROM N.A. RC STRAIN=C57BL/6; TISSUE=Thymus; RX MEDLINE=93346725; PubMed=8345183; RA Chang A.C., Wadsworth S., Coligan J.E.; RT "Expression of merosin in the thymus and its interaction with RT thymocytes."; RL J. Immunol. 151:1789-1801(1993). RN [3] RP SEQUENCE OF 64-281 FROM N.A. RX MEDLINE=95179178; PubMed=7874173; RA Xu H., Wu X.R., Wewer U.M., Engvall E.; RT "Murine muscular dystrophy caused by a mutation in the laminin alpha 2 RT (Lama2) gene."; RL Nat. Genet. 8:297-302(1994). RN [4] RP SEQUENCE OF 20-25. RX MEDLINE=21818471; PubMed=11829758; RA Garbe J.H., Gohring W., Mann K., Timpl R., Sasaki T.; RT "Complete sequence, recombinant analysis and binding to laminins and RT sulphated ligands of the N-terminal domains of laminin alpha3B and RT alpha5 chains."; RL Biochem. J. 362:213-221(2002). RN [5] RP BINDING TO FBLN1, FBLN2, AND NID2. RX MEDLINE=99146904; PubMed=10022829; RA Talts J.F., Andac Z., Goehring W., Brancaccio A., Timpl R.; RT "Binding of the G domains of laminin alpha1 and alpha2 chains and RT perlecan to heparin, sulfatides, alpha-dystroglycan and several RT extracellular matrix proteins."; RL EMBO J. 18:863-870(1999). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 2932-3106. RX MEDLINE=20085745; PubMed=10619025; RA Hohenester E., Tisi D., Talts J.F., Timpl R.; RT "The crystal structure of a laminin G-like module reveals the RT molecular basis of alpha-dystroglycan binding to laminins, perlecan, RT and agrin."; RL Mol. Cell 4:783-792(1999). CC -!- FUNCTION: Binding to cells via a high affinity receptor, laminin CC is thought to mediate the attachment, migration and organization CC of cells into tissues during embryonic development by interacting CC with other extracellular matrix components. CC -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three CC different polypeptide chains (alpha, beta, gamma), which are bound CC to each other by disulfide bonds into a cross-shaped molecule CC comprising one long and three short arms with globules at each CC end. The alpha-2 chain is a subunit of laminin-2 (Merosin) and CC laminin-4 (S-merosin). Interacts with FBLN1, FBLN2 and NID2. CC -!- SUBCELLULAR LOCATION: Extracellular. CC -!- TISSUE SPECIFICITY: Found in the basement membranes (major CC component). CC -!- DOMAIN: The alpha-helical domains I and II are thought to interact CC with other laminin chains to form a coiled coil structure. CC -!- DOMAIN: Domains VI, IV and G are globular. CC -!- DISEASE: Defects in Lama2 are a cause of murine muscular dystrophy CC (dy2J). CC -!- SIMILARITY: Contains 17 laminin EGF-like domains. CC -!- SIMILARITY: Contains 5 laminin G-like domains. CC -!- SIMILARITY: Contains 2 laminin IV domains. CC -!- SIMILARITY: Contains 1 laminin N-terminal domain. 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; U12147; AAC52165.1; -. DR EMBL; X69869; CAA49502.1; -. DR EMBL; S75315; AAB33573.1; -. DR PIR; I49077; S53868. DR PDB; 1DYK; 04-FEB-01. DR PDB; 1QU0; 03-DEC-99. DR MGD; MGI:99912; Lama2. DR GO; GO:0005604; C:basement membrane; IDA. DR InterPro; IPR008985; ConA_like_lec_gl. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR008979; Gal_bind_like. DR InterPro; IPR009030; Grow_fac_recept. DR InterPro; IPR000034; Laminin_B. DR InterPro; IPR002049; Laminin_EGF. DR InterPro; IPR001791; Laminin_G. DR InterPro; IPR009254; Laminin_I. DR InterPro; IPR010307; Laminin_II. DR InterPro; IPR008211; Laminin_N. DR InterPro; IPR003129; TSP_N. DR Pfam; PF00052; Laminin_B; 2. DR Pfam; PF00053; Laminin_EGF; 14. DR Pfam; PF00054; Laminin_G; 5. DR Pfam; PF06008; Laminin_I; 1. DR Pfam; PF06009; Laminin_II; 1. DR Pfam; PF00055; Laminin_N; 1. DR PRINTS; PR00011; EGFLAMININ. DR ProDom; PD003031; Laminin_B; 1. DR PROSITE; PS00022; EGF_1; 11. DR PROSITE; PS01186; EGF_2; 3. DR PROSITE; PS01248; LAMININ_TYPE_EGF; 14. DR PROSITE; PS50025; LAM_G_DOMAIN; 5. KW 3D-structure; Basement membrane; Cell adhesion; Coiled coil; KW Direct protein sequencing; Extracellular matrix; Glycoprotein; KW Laminin EGF-like domain; Repeat; Signal. FT SIGNAL 1 19 FT CHAIN 20 3106 Laminin alpha-2 chain. FT DOMAIN 20 282 Laminin N-terminal (domain VI). FT DOMAIN 283 339 Laminin EGF-like 1. FT DOMAIN 340 409 Laminin EGF-like 2. FT DOMAIN 410 464 Laminin EGF-like 3. FT DOMAIN 465 513 Laminin EGF-like 4. FT DOMAIN 514 523 Laminin EGF-like 5 (N-terminal). FT DOMAIN 524 719 Laminin domain IV 1 (domain IV B). FT DOMAIN 720 752 Laminin EGF-like 5 (C-terminal). FT DOMAIN 753 802 Laminin EGF-like 6. FT DOMAIN 803 860 Laminin EGF-like 7. FT DOMAIN 861 913 Laminin EGF-like 8. FT DOMAIN 914 962 Laminin EGF-like 9. FT DOMAIN 963 1009 Laminin EGF-like 10. FT DOMAIN 1010 1055 Laminin EGF-like 11. FT DOMAIN 1056 1101 Laminin EGF-like 12. FT DOMAIN 1102 1161 Laminin EGF-like 13. FT DOMAIN 1162 1171 Laminin EGF-like 14 (N-terminal). FT DOMAIN 1172 1375 Laminin domain IV 2 (domain IV A). FT DOMAIN 1376 1415 Laminin EGF-like 14 (C-terminal). FT DOMAIN 1416 1464 Laminin EGF-like 15. FT DOMAIN 1465 1522 Laminin EGF-like 16. FT DOMAIN 1523 1569 Laminin EGF-like 17. FT DOMAIN 1570 2140 Domain II and I. FT DOMAIN 2141 2324 Laminin G-like 1. FT DOMAIN 2336 2517 Laminin G-like 2. FT DOMAIN 2522 2706 Laminin G-like 3. FT DOMAIN 2759 2930 Laminin G-like 4. FT DOMAIN 2929 3106 Laminin G-like 5. FT DOMAIN 1662 1863 Coiled coil (Potential). FT DOMAIN 1923 2146 Coiled coil (Potential). FT DISULFID 283 292 By similarity. FT DISULFID 285 303 By similarity. FT DISULFID 305 314 By similarity. FT DISULFID 317 337 By similarity. FT DISULFID 340 349 By similarity. FT DISULFID 342 374 By similarity. FT DISULFID 377 386 By similarity. FT DISULFID 389 407 By similarity. FT DISULFID 410 422 By similarity. FT DISULFID 412 438 By similarity. FT DISULFID 440 449 By similarity. FT DISULFID 452 462 By similarity. FT DISULFID 465 478 By similarity. FT DISULFID 467 482 By similarity. FT DISULFID 484 493 By similarity. FT DISULFID 496 511 By similarity. FT DISULFID 753 762 By similarity. FT DISULFID 755 769 By similarity. FT DISULFID 772 781 By similarity. FT DISULFID 784 800 By similarity. FT DISULFID 803 818 By similarity. FT DISULFID 805 828 By similarity. FT DISULFID 831 840 By similarity. FT DISULFID 843 858 By similarity. FT DISULFID 861 875 By similarity. FT DISULFID 863 882 By similarity. FT DISULFID 885 894 By similarity. FT DISULFID 897 911 By similarity. FT DISULFID 914 926 By similarity. FT DISULFID 916 933 By similarity. FT DISULFID 935 944 By similarity. FT DISULFID 947 960 By similarity. FT DISULFID 963 975 By similarity. FT DISULFID 965 981 By similarity. FT DISULFID 983 992 By similarity. FT DISULFID 995 1007 By similarity. FT DISULFID 1010 1019 By similarity. FT DISULFID 1012 1026 By similarity. FT DISULFID 1028 1037 By similarity. FT DISULFID 1040 1053 By similarity. FT DISULFID 1056 1068 By similarity. FT DISULFID 1058 1075 By similarity. FT DISULFID 1077 1086 By similarity. FT DISULFID 1089 1099 By similarity. FT DISULFID 1416 1425 By similarity. FT DISULFID 1418 1432 By similarity. FT DISULFID 1435 1444 By similarity. FT DISULFID 1447 1462 By similarity. FT DISULFID 1465 1480 By similarity. FT DISULFID 1467 1490 By similarity. FT DISULFID 1493 1502 By similarity. FT DISULFID 1505 1520 By similarity. FT DISULFID 1523 1535 By similarity. FT DISULFID 1525 1542 By similarity. FT DISULFID 1544 1553 By similarity. FT DISULFID 1556 1567 By similarity. FT DISULFID 1570 1570 Interchain (Probable). FT DISULFID 1574 1574 Interchain (Probable). FT CARBOHYD 51 51 N-linked (GlcNAc...) (Potential). FT CARBOHYD 85 85 N-linked (GlcNAc...) (Potential). FT CARBOHYD 299 299 N-linked (GlcNAc...) (Potential). FT CARBOHYD 359 359 N-linked (GlcNAc...) (Potential). FT CARBOHYD 376 376 N-linked (GlcNAc...) (Potential). FT CARBOHYD 466 466 N-linked (GlcNAc...) (Potential). FT CARBOHYD 742 742 N-linked (GlcNAc...) (Potential). FT CARBOHYD 919 919 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1031 1031 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1057 1057 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1593 1593 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1610 1610 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1696 1696 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1806 1806 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1897 1897 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1912 1912 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1916 1916 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2013 2013 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2024 2024 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2041 2041 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2122 2122 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2236 2236 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2356 2356 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2431 2431 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2474 2474 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2547 2547 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2554 2554 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2644 2644 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2889 2889 N-linked (GlcNAc...) (Potential). FT CONFLICT 2205 2205 I -> D (in Ref. 2). FT CONFLICT 2214 2215 GF -> EY (in Ref. 2). SQ SEQUENCE 3106 AA; 342673 MW; 884E0AE0A933CD33 CRC64; MPAATAGILL LLLLGTLEGS QTQRRQSQAH QQRGLFPAVL NLASNALITT NATCGEKGPE MYCKLVEHVP GQPVRNPQCR ICNQNSSNPY QRHPITNAID GKNTWWQSPS IKNGVEYHYV TITLDLQQVF QIAYVIVKAA NSPRPGNWIL ERSLDDVEYK PWQYHAVTDT ECLTLYNIYP RTGPPSYAKD DEVICTSFYS KIHPLENGEI HISLINGRPS ADDPSPELLE FTSARYIRLR FQRIRTLNAD LMMFAHKDPR EIDPIVTRRY YYSVKDISVG GMCICYGHAR ACPLDPATNK SRCECEHNTC GESCDRCCPG FHQKPWRAGT FLTKSECEAC NCHGKAEECY YDETVASRNL SLNIHGKYIG GGVCINCTHN TAGINCETCV DGFFRPKGVS PNYPRPCQPC HCDPTGSLSE VCVKDEKYAQ RGLKPGSCHC KTGFGGVNCD RCVRGYHGYP DCQPCNCSGL GSTNEDPCVG PCSCKENVEG EDCSRCKSGF FNLQEDNQKG CEECFCSGVS NRCQSSYWTY GNIQDMRGWY LTDLSGRIRM APQLDNPDSP QQISISNSEA RKSLLDGYYW SAPPPYLGNR LPAVGGQLSF TISYDLEEEE DDTEKLLQLM IIFEGNDLRI STAYKEVYLE PSEEHVEEVS LKEEAFTIHG TNLPVTRKDF MIVLTNLGEI LIQITYNLGM DAIFRLSSVN LESPVPYPTD RRIATDVEVC QCPPGYSGSS CETCWPRHRR VNGTIFGGIC EPCQCFAHAE ACDDITGECL NCKDHTGGPY CNECLPGFYG DPTRGSPEDC QPCACPLNIP SNNFSPTCHL DRSLGLICDE CPIGYTGPRC ERCAEGYFGQ PSVPGGSCQP CQCNDNLDYS IPGSCDSLSG SCLICKPGTT GRYCELCADG YFGDAVNTKN CQPCRCDING SFSEDCHTRT GQCECRPNVQ GRHCDECKPE TFGLQLGRGC LPCNCNSFGS KSFDCEASGQ CWCQPGVAGK KCDRCAHGYF NFQEGGCIAC DCSHLGNNCD PKTGQCICPP NTTGEKCSEC LPNTWGHSIV TGCKVCNCST VGSLASQCNV NTGQCSCHPK FSGMKCSECS RGHWNYPLCT LCDCFLPGTD ATTCDLETRK CSCSDQTGQC SCKVNVEGVH CDRCRPGKFG LDAKNPLGCS SCYCFGVTSQ CSEAKGLIRT WVTLSDEQTI LPLVDEALQH TTTKGIAFQK PEIVAKMDEV RQELHLEPFY WKLPQQFEGK KLMAYGGKLK YAIYFEARDE TGFATYKPQV IIRGGTPTHA RIITRHMAAP LIGQLTRHEI EMTEKEWKYY GDDPRISRTV TREDFLDILY DIHYILIKAT YGNVVRQSRI SEISMEVAEP GHVLAGSPPA HLIERCDCPP GYSGLSCETC APGFYRLRSE PGGRTPGPTL GTCVPCQCNG HSSQCDPETS VCQNCQHHTA GDFCERCALG YYGIVRGLPN DCQPCACPLI SPSNNFSPSC VLEGLEDYRC TACPRGYEGQ YCERCAPGYT GSPSSPGGSC QECECDPYGS LPVPCDRVTG LCTCRPGATG RKCDGCEHWH AREGAECVFC GDECTGLLLG DLARLEQMTM NINLTGPLPA PYKILYGLEN TTQELKHLLS PQRAPERLIQ LAEGNVNTLV METNELLTRA TKVTADGEQT GQDAERTNSR AESLEEFIKG LVQDAEAINE KAVKLNETLG NQDKTAERNL EELQKEIDRM LKELRSKDLQ TQKEVAEDEL VAAEGLLKRV NKLFGEPRAQ NEDMEKDLQQ KLAEYKNKLD DAWDLLREAT DKTRDANRLS AANQKNMTIL ETKKEAIEGS KRQIENTLKE GNDILDEANQ LLGEINSVID YVDDIKTKLP PMSEELSDKI DDLAQEIKDR RLAEKVFQAE SHAAQLNDSS AVLDGILDEA KNISFNATAA FRAYSNIKDY IDEAEKVARE AKELAQGATK LATSPQGLLK EDAKGSLQKS FRILNEAKKL ANDVKGNHND LNDLKTRLET ADLRNSGLLG ALNDTMDKLS AITNDTAAKL QAVKEKAREA NDTAKAVLAQ VKDLHQNLDG LKQNYNKLAD SVAKTNAVVK DPSKNKIIAD AGTSVRNLEQ EADRLIDKLK PIKELEDNLK KNISEIKELI NQARKQANSI KVSVSSGGDC VRTYRPEIKK GSYNNIVVHV KTAVADNLLF YLGSAKFIDF LAIEMRKGKV SFLWIVGSGV GRVGFPDLTI DDSYWYRIEA SRTGRNGSIS VRALDGPKAS MVPSTYHSVS PPGYTILDVD ANAMLFVGGL TGKIKKADAV RVITFTGCMG ETYFDNKPIG LWNFREKEGD CKGCTVSPQV EDSEGTIQFD GEGYALVSRP IRWYPNISTV MFKFRTFSSS ALLMYLATRD LKDFMSVELS DGHVKVSYDL GSGMTSVVSN QNHNDGKWKA FTLSRIQKQA NISIVDIDSN QEENVATSSS GNNFGLDLKA DDKIYFGGLP TLRNLSMKAR PEVNVKKYSG CLKDIEISRT PYNILSSPDY VGVTKGCSLE NVNTVSFPKP GFVELAAVSI DVGTEINLSF STRNESGIIL LGSGGTLTPP RRKRRQTTQA YYAIFLNKGR LEVHLSSGTR TMRKIVIKPE PNLFHDGREH SVHVERTRGI FTVQIDEDRR HIQNLTEEQP IEVKKLFVGG APPEFQPSPL RNIPAFQGCV WNLVINSIPM DFAQPIAFKN ADIGRCTYQK PREDESEAVP AEVIVQPQSV PTPAFPFPVP TMVHGPCVAE SEPALLTGSK QFGLSRNSHI AIVFDDTKVK NRLTIELEVR TEAESGLLFY MGRINHADFG TVQLRNGFPF FSYDLGSGST RTMIPTKIND GQWHKIKIVR VKQEGILYVD DASSQTISPK KADILDVGGI LYVGGLPINY TTRRIGPVTY SLDGCVRNLH MEQAPVDLDQ PTSSFHVGTC FANAESGTYF DGTGFGKAVG GFIVGLDLLV EFEFRTTRPT GVLLGISSQK MDGMGIEMID EKLMFHVDNG AGRFTAIYDA EIPGHMCNGQ WYKVTAKKIK NRLELVVDGN QVDAQSPNSA STSADTNDPV FVGGFPGGLN QFGLTTNIRF RGCIRSLKLT KGTANRWRLI LPRPWN //