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Q60675 (LAMA2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Laminin subunit alpha-2
Alternative name(s):
Laminin M chain
Laminin-12 subunit alpha
Laminin-2 subunit alpha
Laminin-4 subunit alpha
Merosin heavy chain
Gene names
Name:Lama2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length3118 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.

Subunit structure

Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Alpha-2 is a subunit of laminin-2 (laminin-211 or merosin), laminin-4 (laminin-221 or S-merosin) and laminin-12 (laminin-213). Interacts with FBLN1, FBLN2 and NID2. Ref.6

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane. Note: Major component.

Domain

The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.

Domains VI, IV and G are globular.

Involvement in disease

Defects in Lama2 are a cause of murine muscular dystrophy (dy2J).

Sequence similarities

Contains 17 laminin EGF-like domains.

Contains 5 laminin G-like domains.

Contains 2 laminin IV type A domains.

Contains 1 laminin N-terminal domain.

Sequence caution

The sequence AAC52165.1 differs from that shown. Reason: Frameshift at position 3094.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.5
Chain20 – 31183099Laminin subunit alpha-2
PRO_0000017057

Regions

Domain31 – 282252Laminin N-terminal
Domain283 – 33957Laminin EGF-like 1
Domain340 – 40970Laminin EGF-like 2
Domain410 – 46455Laminin EGF-like 3
Domain465 – 51349Laminin EGF-like 4
Domain514 – 52310Laminin EGF-like 5; first part
Domain527 – 719193Laminin IV type A 1
Domain720 – 75233Laminin EGF-like 5; second part
Domain753 – 80250Laminin EGF-like 6
Domain803 – 86058Laminin EGF-like 7
Domain861 – 91353Laminin EGF-like 8
Domain914 – 96249Laminin EGF-like 9
Domain963 – 100947Laminin EGF-like 10
Domain1010 – 105546Laminin EGF-like 11
Domain1056 – 110146Laminin EGF-like 12
Domain1102 – 116160Laminin EGF-like 13
Domain1162 – 117110Laminin EGF-like 14; first part
Domain1172 – 1375204Laminin IV type A 2
Domain1376 – 141540Laminin EGF-like 14; second part
Domain1416 – 146449Laminin EGF-like 15
Domain1465 – 152258Laminin EGF-like 16
Domain1523 – 156947Laminin EGF-like 17
Domain2141 – 2324184Laminin G-like 1
Domain2336 – 2517182Laminin G-like 2
Domain2522 – 2706185Laminin G-like 3
Domain2759 – 2930172Laminin G-like 4
Domain2929 – 3115187Laminin G-like 5
Region1570 – 2140571Domain II and I
Coiled coil1662 – 1863202 Potential
Coiled coil1923 – 2146224 Potential

Amino acid modifications

Glycosylation511N-linked (GlcNAc...) Potential
Glycosylation851N-linked (GlcNAc...) Potential
Glycosylation2991N-linked (GlcNAc...) Potential
Glycosylation3591N-linked (GlcNAc...) Potential
Glycosylation3761N-linked (GlcNAc...) Potential
Glycosylation4661N-linked (GlcNAc...) Potential
Glycosylation7421N-linked (GlcNAc...) Potential
Glycosylation9191N-linked (GlcNAc...) Potential
Glycosylation10311N-linked (GlcNAc...) Potential
Glycosylation10571N-linked (GlcNAc...) Potential
Glycosylation15931N-linked (GlcNAc...) Potential
Glycosylation16101N-linked (GlcNAc...) Potential
Glycosylation16961N-linked (GlcNAc...) Potential
Glycosylation18061N-linked (GlcNAc...) Potential
Glycosylation18971N-linked (GlcNAc...) Potential
Glycosylation19121N-linked (GlcNAc...) Potential
Glycosylation19161N-linked (GlcNAc...) Potential
Glycosylation20131N-linked (GlcNAc...) Potential
Glycosylation20241N-linked (GlcNAc...) Potential
Glycosylation20411N-linked (GlcNAc...) Potential
Glycosylation21221N-linked (GlcNAc...) Potential
Glycosylation22361N-linked (GlcNAc...) Potential
Glycosylation23561N-linked (GlcNAc...) Potential
Glycosylation24311N-linked (GlcNAc...) Potential
Glycosylation24741N-linked (GlcNAc...) Potential
Glycosylation25471N-linked (GlcNAc...) Potential
Glycosylation25541N-linked (GlcNAc...) Potential
Glycosylation26441N-linked (GlcNAc...) Potential
Glycosylation28891N-linked (GlcNAc...) Potential
Disulfide bond283 ↔ 292 By similarity
Disulfide bond285 ↔ 303 By similarity
Disulfide bond305 ↔ 314 By similarity
Disulfide bond317 ↔ 337 By similarity
Disulfide bond340 ↔ 349 By similarity
Disulfide bond342 ↔ 374 By similarity
Disulfide bond377 ↔ 386 By similarity
Disulfide bond389 ↔ 407 By similarity
Disulfide bond410 ↔ 422 By similarity
Disulfide bond412 ↔ 438 By similarity
Disulfide bond440 ↔ 449 By similarity
Disulfide bond452 ↔ 462 By similarity
Disulfide bond465 ↔ 478 By similarity
Disulfide bond467 ↔ 482 By similarity
Disulfide bond484 ↔ 493 By similarity
Disulfide bond496 ↔ 511 By similarity
Disulfide bond753 ↔ 762 By similarity
Disulfide bond755 ↔ 769 By similarity
Disulfide bond772 ↔ 781 By similarity
Disulfide bond784 ↔ 800 By similarity
Disulfide bond803 ↔ 818 By similarity
Disulfide bond805 ↔ 828 By similarity
Disulfide bond831 ↔ 840 By similarity
Disulfide bond843 ↔ 858 By similarity
Disulfide bond861 ↔ 875 By similarity
Disulfide bond863 ↔ 882 By similarity
Disulfide bond885 ↔ 894 By similarity
Disulfide bond897 ↔ 911 By similarity
Disulfide bond914 ↔ 926 By similarity
Disulfide bond916 ↔ 933 By similarity
Disulfide bond935 ↔ 944 By similarity
Disulfide bond947 ↔ 960 By similarity
Disulfide bond963 ↔ 975 By similarity
Disulfide bond965 ↔ 981 By similarity
Disulfide bond983 ↔ 992 By similarity
Disulfide bond995 ↔ 1007 By similarity
Disulfide bond1010 ↔ 1019 By similarity
Disulfide bond1012 ↔ 1026 By similarity
Disulfide bond1028 ↔ 1037 By similarity
Disulfide bond1040 ↔ 1053 By similarity
Disulfide bond1056 ↔ 1068 By similarity
Disulfide bond1058 ↔ 1075 By similarity
Disulfide bond1077 ↔ 1086 By similarity
Disulfide bond1089 ↔ 1099 By similarity
Disulfide bond1102 ↔ 1114 By similarity
Disulfide bond1104 ↔ 1130 By similarity
Disulfide bond1132 ↔ 1141 By similarity
Disulfide bond1144 ↔ 1159 By similarity
Disulfide bond1378 ↔ 1387 By similarity
Disulfide bond1416 ↔ 1425 By similarity
Disulfide bond1418 ↔ 1432 By similarity
Disulfide bond1435 ↔ 1444 By similarity
Disulfide bond1447 ↔ 1462 By similarity
Disulfide bond1465 ↔ 1480 By similarity
Disulfide bond1467 ↔ 1490 By similarity
Disulfide bond1493 ↔ 1502 By similarity
Disulfide bond1505 ↔ 1520 By similarity
Disulfide bond1523 ↔ 1535 By similarity
Disulfide bond1525 ↔ 1542 By similarity
Disulfide bond1544 ↔ 1553 By similarity
Disulfide bond1556 ↔ 1567 By similarity
Disulfide bond1570Interchain Probable
Disulfide bond1574Interchain Probable
Disulfide bond2298 ↔ 2324 By similarity
Disulfide bond2491 ↔ 2517 By similarity
Disulfide bond2679 ↔ 2706 By similarity
Disulfide bond2905 ↔ 2930 By similarity
Disulfide bond3083 ↔ 3115 By similarity

Experimental info

Sequence conflict6161I → L in AAC52165. Ref.1
Sequence conflict6461I → V in AAC52165. Ref.1
Sequence conflict678 – 6825ERVLM → GEILI in AAC52165. Ref.1
Sequence conflict7041A → P in AAC52165. Ref.1
Sequence conflict8531I → V in AAC52165. Ref.1
Sequence conflict9081A → T in AAC52165. Ref.1
Sequence conflict9171N → D in AAC52165. Ref.1
Sequence conflict9251I → D in AAC52165. Ref.1
Sequence conflict16941Q → K in AAC52165. Ref.1
Sequence conflict18401R → Q in AAC52165. Ref.1
Sequence conflict22051D → I in AAC52165. Ref.1
Sequence conflict2214 – 22152EY → GF in AAC52165. Ref.1
Sequence conflict25231Y → N in AAC52165. Ref.1
Sequence conflict26421M → I in AAC52165. Ref.1
Sequence conflict27291P → S in AAC52165. Ref.1
Sequence conflict27391A → V in AAC52165. Ref.1
Sequence conflict27731A → V in AAC52165. Ref.1
Sequence conflict28021A → G in AAC52165. Ref.1
Sequence conflict28101A → G in AAC52165. Ref.1
Sequence conflict28201Y → F in AAC52165. Ref.1
Sequence conflict2829 – 28313DTS → STR in AAC52165. Ref.1
Sequence conflict28781V → G in AAC52165. Ref.1
Sequence conflict29461A → G in AAC52165. Ref.1
Sequence conflict29531K → I in AAC52165. Ref.1
Sequence conflict29761V → I in AAC52165. Ref.1
Sequence conflict30111G → E in AAC52165. Ref.1
Sequence conflict30221H → Y in AAC52165. Ref.1

Secondary structure

....................................................................................................................................................... 3118
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q60675 [UniParc].

Last modified October 16, 2013. Version 2.
Checksum: CCD31C71B1E0DFD4

FASTA3,118343,815
        10         20         30         40         50         60 
MPAATAGILL LLLLGTLEGS QTQRRQSQAH QQRGLFPAVL NLASNALITT NATCGEKGPE 

        70         80         90        100        110        120 
MYCKLVEHVP GQPVRNPQCR ICNQNSSNPY QRHPITNAID GKNTWWQSPS IKNGVEYHYV 

       130        140        150        160        170        180 
TITLDLQQVF QIAYVIVKAA NSPRPGNWIL ERSLDDVEYK PWQYHAVTDT ECLTLYNIYP 

       190        200        210        220        230        240 
RTGPPSYAKD DEVICTSFYS KIHPLENGEI HISLINGRPS ADDPSPELLE FTSARYIRLR 

       250        260        270        280        290        300 
FQRIRTLNAD LMMFAHKDPR EIDPIVTRRY YYSVKDISVG GMCICYGHAR ACPLDPATNK 

       310        320        330        340        350        360 
SRCECEHNTC GESCDRCCPG FHQKPWRAGT FLTKSECEAC NCHGKAEECY YDETVASRNL 

       370        380        390        400        410        420 
SLNIHGKYIG GGVCINCTHN TAGINCETCV DGFFRPKGVS PNYPRPCQPC HCDPTGSLSE 

       430        440        450        460        470        480 
VCVKDEKYAQ RGLKPGSCHC KTGFGGVNCD RCVRGYHGYP DCQPCNCSGL GSTNEDPCVG 

       490        500        510        520        530        540 
PCSCKENVEG EDCSRCKSGF FNLQEDNQKG CEECFCSGVS NRCQSSYWTY GNIQDMRGWY 

       550        560        570        580        590        600 
LTDLSGRIRM APQLDNPDSP QQISISNSEA RKSLLDGYYW SAPPPYLGNR LPAVGGQLSF 

       610        620        630        640        650        660 
TISYDLEEEE DDTEKILQLM IIFEGNDLRI STAYKEVYLE PSEEHIEEVS LKEEAFTIHG 

       670        680        690        700        710        720 
TNLPVTRKDF MIVLTNLERV LMQITYNLGM DAIFRLSSVN LESAVPYPTD RRIATDVEVC 

       730        740        750        760        770        780 
QCPPGYSGSS CETCWPRHRR VNGTIFGGIC EPCQCFAHAE ACDDITGECL NCKDHTGGPY 

       790        800        810        820        830        840 
CNECLPGFYG DPTRGSPEDC QPCACPLNIP SNNFSPTCHL DRSLGLICDE CPIGYTGPRC 

       850        860        870        880        890        900 
ERCAEGYFGQ PSIPGGSCQP CQCNDNLDYS IPGSCDSLSG SCLICKPGTT GRYCELCADG 

       910        920        930        940        950        960 
YFGDAVNAKN CQPCRCNING SFSEICHTRT GQCECRPNVQ GRHCDECKPE TFGLQLGRGC 

       970        980        990       1000       1010       1020 
LPCNCNSFGS KSFDCEASGQ CWCQPGVAGK KCDRCAHGYF NFQEGGCIAC DCSHLGNNCD 

      1030       1040       1050       1060       1070       1080 
PKTGQCICPP NTTGEKCSEC LPNTWGHSIV TGCKVCNCST VGSLASQCNV NTGQCSCHPK 

      1090       1100       1110       1120       1130       1140 
FSGMKCSECS RGHWNYPLCT LCDCFLPGTD ATTCDLETRK CSCSDQTGQC SCKVNVEGVH 

      1150       1160       1170       1180       1190       1200 
CDRCRPGKFG LDAKNPLGCS SCYCFGVTSQ CSEAKGLIRT WVTLSDEQTI LPLVDEALQH 

      1210       1220       1230       1240       1250       1260 
TTTKGIAFQK PEIVAKMDEV RQELHLEPFY WKLPQQFEGK KLMAYGGKLK YAIYFEARDE 

      1270       1280       1290       1300       1310       1320 
TGFATYKPQV IIRGGTPTHA RIITRHMAAP LIGQLTRHEI EMTEKEWKYY GDDPRISRTV 

      1330       1340       1350       1360       1370       1380 
TREDFLDILY DIHYILIKAT YGNVVRQSRI SEISMEVAEP GHVLAGSPPA HLIERCDCPP 

      1390       1400       1410       1420       1430       1440 
GYSGLSCETC APGFYRLRSE PGGRTPGPTL GTCVPCQCNG HSSQCDPETS VCQNCQHHTA 

      1450       1460       1470       1480       1490       1500 
GDFCERCALG YYGIVRGLPN DCQPCACPLI SPSNNFSPSC VLEGLEDYRC TACPRGYEGQ 

      1510       1520       1530       1540       1550       1560 
YCERCAPGYT GSPSSPGGSC QECECDPYGS LPVPCDRVTG LCTCRPGATG RKCDGCEHWH 

      1570       1580       1590       1600       1610       1620 
AREGAECVFC GDECTGLLLG DLARLEQMTM NINLTGPLPA PYKILYGLEN TTQELKHLLS 

      1630       1640       1650       1660       1670       1680 
PQRAPERLIQ LAEGNVNTLV METNELLTRA TKVTADGEQT GQDAERTNSR AESLEEFIKG 

      1690       1700       1710       1720       1730       1740 
LVQDAEAINE KAVQLNETLG NQDKTAERNL EELQKEIDRM LKELRSKDLQ TQKEVAEDEL 

      1750       1760       1770       1780       1790       1800 
VAAEGLLKRV NKLFGEPRAQ NEDMEKDLQQ KLAEYKNKLD DAWDLLREAT DKTRDANRLS 

      1810       1820       1830       1840       1850       1860 
AANQKNMTIL ETKKEAIEGS KRQIENTLKE GNDILDEANR LLGEINSVID YVDDIKTKLP 

      1870       1880       1890       1900       1910       1920 
PMSEELSDKI DDLAQEIKDR RLAEKVFQAE SHAAQLNDSS AVLDGILDEA KNISFNATAA 

      1930       1940       1950       1960       1970       1980 
FRAYSNIKDY IDEAEKVARE AKELAQGATK LATSPQGLLK EDAKGSLQKS FRILNEAKKL 

      1990       2000       2010       2020       2030       2040 
ANDVKGNHND LNDLKTRLET ADLRNSGLLG ALNDTMDKLS AITNDTAAKL QAVKEKAREA 

      2050       2060       2070       2080       2090       2100 
NDTAKAVLAQ VKDLHQNLDG LKQNYNKLAD SVAKTNAVVK DPSKNKIIAD AGTSVRNLEQ 

      2110       2120       2130       2140       2150       2160 
EADRLIDKLK PIKELEDNLK KNISEIKELI NQARKQANSI KVSVSSGGDC VRTYRPEIKK 

      2170       2180       2190       2200       2210       2220 
GSYNNIVVHV KTAVADNLLF YLGSAKFIDF LAIEMRKGKV SFLWDVGSGV GRVEYPDLTI 

      2230       2240       2250       2260       2270       2280 
DDSYWYRIEA SRTGRNGSIS VRALDGPKAS MVPSTYHSVS PPGYTILDVD ANAMLFVGGL 

      2290       2300       2310       2320       2330       2340 
TGKIKKADAV RVITFTGCMG ETYFDNKPIG LWNFREKEGD CKGCTVSPQV EDSEGTIQFD 

      2350       2360       2370       2380       2390       2400 
GEGYALVSRP IRWYPNISTV MFKFRTFSSS ALLMYLATRD LKDFMSVELS DGHVKVSYDL 

      2410       2420       2430       2440       2450       2460 
GSGMTSVVSN QNHNDGKWKA FTLSRIQKQA NISIVDIDSN QEENVATSSS GNNFGLDLKA 

      2470       2480       2490       2500       2510       2520 
DDKIYFGGLP TLRNLSMKAR PEVNVKKYSG CLKDIEISRT PYNILSSPDY VGVTKGCSLE 

      2530       2540       2550       2560       2570       2580 
NVYTVSFPKP GFVELAAVSI DVGTEINLSF STRNESGIIL LGSGGTLTPP RRKRRQTTQA 

      2590       2600       2610       2620       2630       2640 
YYAIFLNKGR LEVHLSSGTR TMRKIVIKPE PNLFHDGREH SVHVERTRGI FTVQIDEDRR 

      2650       2660       2670       2680       2690       2700 
HMQNLTEEQP IEVKKLFVGG APPEFQPSPL RNIPAFQGCV WNLVINSIPM DFAQPIAFKN 

      2710       2720       2730       2740       2750       2760 
ADIGRCTYQK PREDESEAVP AEVIVQPQPV PTPAFPFPAP TMVHGPCVAE SEPALLTGSK 

      2770       2780       2790       2800       2810       2820 
QFGLSRNSHI AIAFDDTKVK NRLTIELEVR TEAESGLLFY MARINHADFA TVQLRNGFPY 

      2830       2840       2850       2860       2870       2880 
FSYDLGSGDT STMIPTKIND GQWHKIKIVR VKQEGILYVD DASSQTISPK KADILDVVGI 

      2890       2900       2910       2920       2930       2940 
LYVGGLPINY TTRRIGPVTY SLDGCVRNLH MEQAPVDLDQ PTSSFHVGTC FANAESGTYF 

      2950       2960       2970       2980       2990       3000 
DGTGFAKAVG GFKVGLDLLV EFEFRTTRPT GVLLGVSSQK MDGMGIEMID EKLMFHVDNG 

      3010       3020       3030       3040       3050       3060 
AGRFTAIYDA GIPGHMCNGQ WHKVTAKKIK NRLELVVDGN QVDAQSPNSA STSADTNDPV 

      3070       3080       3090       3100       3110 
FVGGFPGGLN QFGLTTNIRF RGCIRSLKLT KGTGKPLEVN FAKALELRGV QPVSCPTT 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of laminin alpha 2 chain (M-chain) in the mouse."
Bernier S.M., Utani A., Sugiyama S., Doi T., Polistina C., Yamada Y.
Matrix Biol. 14:447-455(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: FVB/N.
Tissue: Embryo and Heart.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"Expression of merosin in the thymus and its interaction with thymocytes."
Chang A.C., Wadsworth S., Coligan J.E.
J. Immunol. 151:1789-1801(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2162-2279.
Strain: C57BL/6.
Tissue: Thymus.
[4]"Murine muscular dystrophy caused by a mutation in the laminin alpha 2 (Lama2) gene."
Xu H., Wu X.R., Wewer U.M., Engvall E.
Nat. Genet. 8:297-302(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 64-281.
[5]"Complete sequence, recombinant analysis and binding to laminins and sulphated ligands of the N-terminal domains of laminin alpha3B and alpha5 chains."
Garbe J.H., Gohring W., Mann K., Timpl R., Sasaki T.
Biochem. J. 362:213-221(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-25.
[6]"Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix proteins."
Talts J.F., Andac Z., Goehring W., Brancaccio A., Timpl R.
EMBO J. 18:863-870(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FBLN1; FBLN2 AND NID2.
[7]"The crystal structure of a laminin G-like module reveals the molecular basis of alpha-dystroglycan binding to laminins, perlecan, and agrin."
Hohenester E., Tisi D., Talts J.F., Timpl R.
Mol. Cell 4:783-792(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 2932-3106.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U12147 mRNA. Translation: AAC52165.1. Frameshift.
AC101709 Genomic DNA. No translation available.
AC152982 Genomic DNA. No translation available.
AC153800 Genomic DNA. No translation available.
AC155942 Genomic DNA. No translation available.
AC167232 Genomic DNA. No translation available.
AC171406 Genomic DNA. No translation available.
X69869 mRNA. Translation: CAA49502.1.
S75315 mRNA. Translation: AAB33573.1.
CCDSCCDS48526.1.
PIRS53868. I49077.
RefSeqNP_032507.2. NM_008481.2.
UniGeneMm.256087.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DYKX-ray2.00A2730-3094[»]
1OKQX-ray2.80A2730-3094[»]
1QU0X-ray2.35A/B/C/D2932-3106[»]
2WJSX-ray2.80A2136-2565[»]
A2579-2746[»]
ProteinModelPortalQ60675.
SMRQ60675. Positions 2142-2707, 2744-3117.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-225176.

PTM databases

PhosphoSiteQ60675.

Proteomic databases

MaxQBQ60675.
PaxDbQ60675.
PRIDEQ60675.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000092639; ENSMUSP00000090304; ENSMUSG00000019899.
GeneID16773.
KEGGmmu:16773.

Organism-specific databases

CTD3908.
MGIMGI:99912. Lama2.

Phylogenomic databases

eggNOGCOG0419.
GeneTreeENSGT00750000117374.
HOGENOMHOG000293201.
HOVERGENHBG052298.
KOK05637.
OMAHTTTKGI.
OrthoDBEOG7SR4KJ.
TreeFamTF335359.

Enzyme and pathway databases

ReactomeREACT_206066. Extracellular matrix organization.

Gene expression databases

CleanExMM_LAMA2.
GenevestigatorQ60675.

Family and domain databases

Gene3D2.60.120.200. 5 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR002049. EGF_laminin.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_N_dom.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
IPR010307. Laminin_II.
IPR008211. Laminin_N.
[Graphical view]
PfamPF00052. Laminin_B. 2 hits.
PF00053. Laminin_EGF. 16 hits.
PF00054. Laminin_G_1. 4 hits.
PF02210. Laminin_G_2. 1 hit.
PF06008. Laminin_I. 1 hit.
PF06009. Laminin_II. 1 hit.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTSM00180. EGF_Lam. 15 hits.
SM00281. LamB. 2 hits.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMSSF49785. SSF49785. 1 hit.
SSF49899. SSF49899. 5 hits.
SSF57184. SSF57184. 3 hits.
PROSITEPS00022. EGF_1. 11 hits.
PS01186. EGF_2. 3 hits.
PS01248. EGF_LAM_1. 14 hits.
PS50027. EGF_LAM_2. 16 hits.
PS50025. LAM_G_DOMAIN. 5 hits.
PS51115. LAMININ_IVA. 2 hits.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLAMA2. mouse.
EvolutionaryTraceQ60675.
NextBio290606.
PROQ60675.
SOURCESearch...

Entry information

Entry nameLAMA2_MOUSE
AccessionPrimary (citable) accession number: Q60675
Secondary accession number(s): F8VQ43, Q05003, Q64061
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 16, 2013
Last modified: July 9, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot