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Protein

Laminin subunit alpha-2

Gene

Lama2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Biological processi

  • axon guidance Source: MGI
  • cell adhesion Source: UniProtKB-KW
  • extracellular matrix organization Source: Reactome
  • myelination in peripheral nervous system Source: Ensembl
  • positive regulation of synaptic transmission, cholinergic Source: MGI
  • regulation of cell adhesion Source: InterPro
  • regulation of cell migration Source: InterPro
  • regulation of embryonic development Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-MMU-3000157. Laminin interactions.
R-MMU-3000171. Non-integrin membrane-ECM interactions.
R-MMU-8874081. MET activates PTK2 signaling.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Lama2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:99912. Lama2.

Subcellular locationi

GO - Cellular componenti

  • basal lamina Source: MGI
  • basement membrane Source: MGI
  • dendritic spine Source: Ensembl
  • extracellular exosome Source: MGI
  • extracellular region Source: Reactome
  • sarcolemma Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
ChainiPRO_000001705720 – 3118Laminin subunit alpha-2Add BLAST3099

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi51N-linked (GlcNAc...)Sequence analysis1
Glycosylationi85N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi283 ↔ 292By similarity
Disulfide bondi285 ↔ 303By similarity
Glycosylationi299N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi305 ↔ 314By similarity
Disulfide bondi317 ↔ 337By similarity
Disulfide bondi340 ↔ 349By similarity
Disulfide bondi342 ↔ 374By similarity
Glycosylationi359N-linked (GlcNAc...)Sequence analysis1
Glycosylationi376N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi377 ↔ 386By similarity
Disulfide bondi389 ↔ 407By similarity
Disulfide bondi410 ↔ 422By similarity
Disulfide bondi412 ↔ 438By similarity
Disulfide bondi440 ↔ 449By similarity
Disulfide bondi452 ↔ 462By similarity
Disulfide bondi465 ↔ 478By similarity
Glycosylationi466N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi467 ↔ 482By similarity
Disulfide bondi484 ↔ 493By similarity
Disulfide bondi496 ↔ 511By similarity
Glycosylationi742N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi753 ↔ 762By similarity
Disulfide bondi755 ↔ 769By similarity
Disulfide bondi772 ↔ 781By similarity
Disulfide bondi784 ↔ 800By similarity
Disulfide bondi803 ↔ 818By similarity
Disulfide bondi805 ↔ 828By similarity
Disulfide bondi831 ↔ 840By similarity
Disulfide bondi843 ↔ 858By similarity
Disulfide bondi861 ↔ 875By similarity
Disulfide bondi863 ↔ 882By similarity
Disulfide bondi885 ↔ 894By similarity
Disulfide bondi897 ↔ 911By similarity
Disulfide bondi914 ↔ 926By similarity
Disulfide bondi916 ↔ 933By similarity
Glycosylationi919N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi935 ↔ 944By similarity
Disulfide bondi947 ↔ 960By similarity
Disulfide bondi963 ↔ 975By similarity
Disulfide bondi965 ↔ 981By similarity
Disulfide bondi983 ↔ 992By similarity
Disulfide bondi995 ↔ 1007By similarity
Disulfide bondi1010 ↔ 1019By similarity
Disulfide bondi1012 ↔ 1026By similarity
Disulfide bondi1028 ↔ 1037By similarity
Glycosylationi1031N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1040 ↔ 1053By similarity
Disulfide bondi1056 ↔ 1068By similarity
Glycosylationi1057N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1058 ↔ 1075By similarity
Disulfide bondi1077 ↔ 1086By similarity
Disulfide bondi1089 ↔ 1099By similarity
Disulfide bondi1102 ↔ 1114By similarity
Disulfide bondi1104 ↔ 1130By similarity
Disulfide bondi1132 ↔ 1141By similarity
Disulfide bondi1144 ↔ 1159By similarity
Disulfide bondi1378 ↔ 1387By similarity
Disulfide bondi1416 ↔ 1425By similarity
Disulfide bondi1418 ↔ 1432By similarity
Disulfide bondi1435 ↔ 1444By similarity
Disulfide bondi1447 ↔ 1462By similarity
Disulfide bondi1465 ↔ 1480By similarity
Disulfide bondi1467 ↔ 1490By similarity
Disulfide bondi1493 ↔ 1502By similarity
Disulfide bondi1505 ↔ 1520By similarity
Disulfide bondi1523 ↔ 1535By similarity
Disulfide bondi1525 ↔ 1542By similarity
Disulfide bondi1544 ↔ 1553By similarity
Disulfide bondi1556 ↔ 1567By similarity
Disulfide bondi1570InterchainCurated
Disulfide bondi1574InterchainCurated
Glycosylationi1593N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1610N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1696N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1806N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1897N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1912N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1916N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2013N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2024N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2041N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2122N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2236N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2298 ↔ 2324By similarity
Glycosylationi2356N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2431N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2474N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2491 ↔ 2517By similarity
Glycosylationi2547N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2554N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2644N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2679 ↔ 2706By similarity
Glycosylationi2889N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2905 ↔ 2930By similarity
Disulfide bondi3083 ↔ 3115By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ60675.
PaxDbiQ60675.
PeptideAtlasiQ60675.
PRIDEiQ60675.

PTM databases

iPTMnetiQ60675.
PhosphoSitePlusiQ60675.

Expressioni

Gene expression databases

BgeeiENSMUSG00000019899.
CleanExiMM_LAMA2.
ExpressionAtlasiQ60675. baseline and differential.
GenevisibleiQ60675. MM.

Interactioni

Subunit structurei

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 NID2.1 Publication

Protein-protein interaction databases

MINTiMINT-225176.
STRINGi10090.ENSMUSP00000090304.

Structurei

Secondary structure

13118
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2151 – 2154Combined sources4
Beta strandi2163 – 2173Combined sources11
Beta strandi2177 – 2183Combined sources7
Beta strandi2190 – 2196Combined sources7
Beta strandi2199 – 2208Combined sources10
Beta strandi2210 – 2214Combined sources5
Beta strandi2226 – 2233Combined sources8
Beta strandi2236 – 2246Combined sources11
Turni2247 – 2250Combined sources4
Beta strandi2256 – 2259Combined sources4
Beta strandi2274 – 2279Combined sources6
Beta strandi2297 – 2299Combined sources3
Beta strandi2303 – 2308Combined sources6
Beta strandi2316 – 2319Combined sources4
Beta strandi2337 – 2348Combined sources12
Beta strandi2357 – 2367Combined sources11
Beta strandi2369 – 2377Combined sources9
Beta strandi2381 – 2390Combined sources10
Beta strandi2393 – 2399Combined sources7
Beta strandi2404 – 2408Combined sources5
Beta strandi2415 – 2417Combined sources3
Beta strandi2419 – 2426Combined sources8
Beta strandi2429 – 2436Combined sources8
Turni2437 – 2439Combined sources3
Beta strandi2442 – 2448Combined sources7
Beta strandi2463 – 2467Combined sources5
Beta strandi2489 – 2497Combined sources9
Beta strandi2500 – 2502Combined sources3
Helixi2504 – 2506Combined sources3
Beta strandi2511 – 2516Combined sources6
Beta strandi2524 – 2526Combined sources3
Beta strandi2528 – 2530Combined sources3
Beta strandi2532 – 2535Combined sources4
Beta strandi2544 – 2553Combined sources10
Beta strandi2555 – 2562Combined sources8
Beta strandi2581 – 2587Combined sources7
Beta strandi2590 – 2596Combined sources7
Beta strandi2603 – 2607Combined sources5
Beta strandi2614 – 2618Combined sources5
Beta strandi2620 – 2626Combined sources7
Beta strandi2628 – 2638Combined sources11
Beta strandi2641 – 2644Combined sources4
Beta strandi2656 – 2659Combined sources4
Beta strandi2678 – 2685Combined sources8
Beta strandi2696 – 2700Combined sources5
Beta strandi2760 – 2762Combined sources3
Beta strandi2769 – 2773Combined sources5
Helixi2776 – 2779Combined sources4
Beta strandi2780 – 2791Combined sources12
Beta strandi2796 – 2802Combined sources7
Beta strandi2806 – 2815Combined sources10
Beta strandi2818 – 2827Combined sources10
Beta strandi2829 – 2833Combined sources5
Beta strandi2840 – 2842Combined sources3
Beta strandi2844 – 2851Combined sources8
Beta strandi2854 – 2859Combined sources6
Beta strandi2862 – 2867Combined sources6
Beta strandi2869 – 2871Combined sources3
Beta strandi2879 – 2885Combined sources7
Beta strandi2903 – 2914Combined sources12
Beta strandi2922 – 2926Combined sources5
Beta strandi2931 – 2952Combined sources22
Beta strandi2955 – 2969Combined sources15
Beta strandi2971 – 2977Combined sources7
Beta strandi2979 – 2981Combined sources3
Beta strandi2983 – 2989Combined sources7
Beta strandi2992 – 3001Combined sources10
Beta strandi3003 – 3008Combined sources6
Helixi3015 – 3017Combined sources3
Beta strandi3018 – 3020Combined sources3
Beta strandi3022 – 3029Combined sources8
Beta strandi3032 – 3037Combined sources6
Beta strandi3040 – 3045Combined sources6
Beta strandi3058 – 3063Combined sources6
Beta strandi3081 – 3094Combined sources14
Helixi3101 – 3103Combined sources3
Beta strandi3105 – 3116Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DYKX-ray2.00A2730-3094[»]
1OKQX-ray2.80A2730-3094[»]
1QU0X-ray2.35A/B/C/D2932-3106[»]
2WJSX-ray2.80A2136-2565[»]
A2579-2746[»]
5IK4X-ray1.27A2730-3118[»]
5IK5X-ray1.39A2730-3118[»]
5IK7X-ray2.00A/B2742-3118[»]
5IK8X-ray2.00A/B2742-3118[»]
ProteinModelPortaliQ60675.
SMRiQ60675.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ60675.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 282Laminin N-terminalPROSITE-ProRule annotationAdd BLAST252
Domaini283 – 339Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST57
Domaini340 – 409Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST70
Domaini410 – 464Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST55
Domaini465 – 513Laminin EGF-like 4PROSITE-ProRule annotationAdd BLAST49
Domaini514 – 523Laminin EGF-like 5; first partPROSITE-ProRule annotation10
Domaini527 – 719Laminin IV type A 1PROSITE-ProRule annotationAdd BLAST193
Domaini720 – 752Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd BLAST33
Domaini753 – 802Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST50
Domaini803 – 860Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST58
Domaini861 – 913Laminin EGF-like 8PROSITE-ProRule annotationAdd BLAST53
Domaini914 – 962Laminin EGF-like 9PROSITE-ProRule annotationAdd BLAST49
Domaini963 – 1009Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST47
Domaini1010 – 1055Laminin EGF-like 11PROSITE-ProRule annotationAdd BLAST46
Domaini1056 – 1101Laminin EGF-like 12PROSITE-ProRule annotationAdd BLAST46
Domaini1102 – 1161Laminin EGF-like 13PROSITE-ProRule annotationAdd BLAST60
Domaini1162 – 1171Laminin EGF-like 14; first partPROSITE-ProRule annotation10
Domaini1172 – 1375Laminin IV type A 2PROSITE-ProRule annotationAdd BLAST204
Domaini1376 – 1415Laminin EGF-like 14; second partPROSITE-ProRule annotationAdd BLAST40
Domaini1416 – 1464Laminin EGF-like 15PROSITE-ProRule annotationAdd BLAST49
Domaini1465 – 1522Laminin EGF-like 16PROSITE-ProRule annotationAdd BLAST58
Domaini1523 – 1569Laminin EGF-like 17PROSITE-ProRule annotationAdd BLAST47
Domaini2141 – 2324Laminin G-like 1PROSITE-ProRule annotationAdd BLAST184
Domaini2336 – 2517Laminin G-like 2PROSITE-ProRule annotationAdd BLAST182
Domaini2522 – 2706Laminin G-like 3PROSITE-ProRule annotationAdd BLAST185
Domaini2759 – 2930Laminin G-like 4PROSITE-ProRule annotationAdd BLAST172
Domaini2929 – 3115Laminin G-like 5PROSITE-ProRule annotationAdd BLAST187

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1570 – 2140Domain II and IAdd BLAST571

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1662 – 1863Sequence analysisAdd BLAST202
Coiled coili1923 – 2146Sequence analysisAdd BLAST224

Domaini

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.

Sequence similaritiesi

Contains 17 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 5 laminin G-like domains.PROSITE-ProRule annotation
Contains 2 laminin IV type A domains.PROSITE-ProRule annotation
Contains 1 laminin N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Laminin EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410KCXA. Eukaryota.
COG0419. LUCA.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000293201.
HOVERGENiHBG052298.
InParanoidiQ60675.
KOiK05637.
OMAiGYFNFQE.
OrthoDBiEOG091G005L.
TreeFamiTF335359.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR013320. ConA-like_dom.
IPR000742. EGF-like_dom.
IPR009030. Growth_fac_rcpt_.
IPR009254. Laminin_aI.
IPR010307. Laminin_domII.
IPR002049. Laminin_EGF.
IPR001791. Laminin_G.
IPR000034. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. 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]
SMARTiSM00181. EGF. 11 hits.
SM00180. EGF_Lam. 16 hits.
SM00281. LamB. 2 hits.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 5 hits.
SSF57184. SSF57184. 3 hits.
PROSITEiPS00022. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q60675-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAATAGILL LLLLGTLEGS QTQRRQSQAH QQRGLFPAVL NLASNALITT
60 70 80 90 100
NATCGEKGPE MYCKLVEHVP GQPVRNPQCR ICNQNSSNPY QRHPITNAID
110 120 130 140 150
GKNTWWQSPS IKNGVEYHYV TITLDLQQVF QIAYVIVKAA NSPRPGNWIL
160 170 180 190 200
ERSLDDVEYK PWQYHAVTDT ECLTLYNIYP RTGPPSYAKD DEVICTSFYS
210 220 230 240 250
KIHPLENGEI HISLINGRPS ADDPSPELLE FTSARYIRLR FQRIRTLNAD
260 270 280 290 300
LMMFAHKDPR EIDPIVTRRY YYSVKDISVG GMCICYGHAR ACPLDPATNK
310 320 330 340 350
SRCECEHNTC GESCDRCCPG FHQKPWRAGT FLTKSECEAC NCHGKAEECY
360 370 380 390 400
YDETVASRNL SLNIHGKYIG GGVCINCTHN TAGINCETCV DGFFRPKGVS
410 420 430 440 450
PNYPRPCQPC HCDPTGSLSE VCVKDEKYAQ RGLKPGSCHC KTGFGGVNCD
460 470 480 490 500
RCVRGYHGYP DCQPCNCSGL GSTNEDPCVG PCSCKENVEG EDCSRCKSGF
510 520 530 540 550
FNLQEDNQKG CEECFCSGVS NRCQSSYWTY GNIQDMRGWY LTDLSGRIRM
560 570 580 590 600
APQLDNPDSP QQISISNSEA RKSLLDGYYW SAPPPYLGNR LPAVGGQLSF
610 620 630 640 650
TISYDLEEEE DDTEKILQLM IIFEGNDLRI STAYKEVYLE PSEEHIEEVS
660 670 680 690 700
LKEEAFTIHG TNLPVTRKDF MIVLTNLERV LMQITYNLGM DAIFRLSSVN
710 720 730 740 750
LESAVPYPTD RRIATDVEVC QCPPGYSGSS CETCWPRHRR VNGTIFGGIC
760 770 780 790 800
EPCQCFAHAE ACDDITGECL NCKDHTGGPY CNECLPGFYG DPTRGSPEDC
810 820 830 840 850
QPCACPLNIP SNNFSPTCHL DRSLGLICDE CPIGYTGPRC ERCAEGYFGQ
860 870 880 890 900
PSIPGGSCQP CQCNDNLDYS IPGSCDSLSG SCLICKPGTT GRYCELCADG
910 920 930 940 950
YFGDAVNAKN CQPCRCNING SFSEICHTRT GQCECRPNVQ GRHCDECKPE
960 970 980 990 1000
TFGLQLGRGC LPCNCNSFGS KSFDCEASGQ CWCQPGVAGK KCDRCAHGYF
1010 1020 1030 1040 1050
NFQEGGCIAC DCSHLGNNCD PKTGQCICPP NTTGEKCSEC LPNTWGHSIV
1060 1070 1080 1090 1100
TGCKVCNCST VGSLASQCNV NTGQCSCHPK FSGMKCSECS RGHWNYPLCT
1110 1120 1130 1140 1150
LCDCFLPGTD ATTCDLETRK CSCSDQTGQC SCKVNVEGVH CDRCRPGKFG
1160 1170 1180 1190 1200
LDAKNPLGCS SCYCFGVTSQ CSEAKGLIRT WVTLSDEQTI LPLVDEALQH
1210 1220 1230 1240 1250
TTTKGIAFQK PEIVAKMDEV RQELHLEPFY WKLPQQFEGK KLMAYGGKLK
1260 1270 1280 1290 1300
YAIYFEARDE TGFATYKPQV IIRGGTPTHA RIITRHMAAP LIGQLTRHEI
1310 1320 1330 1340 1350
EMTEKEWKYY GDDPRISRTV TREDFLDILY DIHYILIKAT YGNVVRQSRI
1360 1370 1380 1390 1400
SEISMEVAEP GHVLAGSPPA HLIERCDCPP GYSGLSCETC APGFYRLRSE
1410 1420 1430 1440 1450
PGGRTPGPTL GTCVPCQCNG HSSQCDPETS VCQNCQHHTA GDFCERCALG
1460 1470 1480 1490 1500
YYGIVRGLPN DCQPCACPLI SPSNNFSPSC VLEGLEDYRC TACPRGYEGQ
1510 1520 1530 1540 1550
YCERCAPGYT GSPSSPGGSC QECECDPYGS LPVPCDRVTG LCTCRPGATG
1560 1570 1580 1590 1600
RKCDGCEHWH AREGAECVFC GDECTGLLLG DLARLEQMTM NINLTGPLPA
1610 1620 1630 1640 1650
PYKILYGLEN TTQELKHLLS PQRAPERLIQ LAEGNVNTLV METNELLTRA
1660 1670 1680 1690 1700
TKVTADGEQT GQDAERTNSR AESLEEFIKG LVQDAEAINE KAVQLNETLG
1710 1720 1730 1740 1750
NQDKTAERNL EELQKEIDRM LKELRSKDLQ TQKEVAEDEL VAAEGLLKRV
1760 1770 1780 1790 1800
NKLFGEPRAQ NEDMEKDLQQ KLAEYKNKLD DAWDLLREAT DKTRDANRLS
1810 1820 1830 1840 1850
AANQKNMTIL ETKKEAIEGS KRQIENTLKE GNDILDEANR LLGEINSVID
1860 1870 1880 1890 1900
YVDDIKTKLP PMSEELSDKI DDLAQEIKDR RLAEKVFQAE SHAAQLNDSS
1910 1920 1930 1940 1950
AVLDGILDEA KNISFNATAA FRAYSNIKDY IDEAEKVARE AKELAQGATK
1960 1970 1980 1990 2000
LATSPQGLLK EDAKGSLQKS FRILNEAKKL ANDVKGNHND LNDLKTRLET
2010 2020 2030 2040 2050
ADLRNSGLLG ALNDTMDKLS AITNDTAAKL QAVKEKAREA NDTAKAVLAQ
2060 2070 2080 2090 2100
VKDLHQNLDG LKQNYNKLAD SVAKTNAVVK DPSKNKIIAD AGTSVRNLEQ
2110 2120 2130 2140 2150
EADRLIDKLK PIKELEDNLK KNISEIKELI NQARKQANSI KVSVSSGGDC
2160 2170 2180 2190 2200
VRTYRPEIKK GSYNNIVVHV KTAVADNLLF YLGSAKFIDF LAIEMRKGKV
2210 2220 2230 2240 2250
SFLWDVGSGV GRVEYPDLTI DDSYWYRIEA SRTGRNGSIS VRALDGPKAS
2260 2270 2280 2290 2300
MVPSTYHSVS PPGYTILDVD ANAMLFVGGL TGKIKKADAV RVITFTGCMG
2310 2320 2330 2340 2350
ETYFDNKPIG LWNFREKEGD CKGCTVSPQV EDSEGTIQFD GEGYALVSRP
2360 2370 2380 2390 2400
IRWYPNISTV MFKFRTFSSS ALLMYLATRD LKDFMSVELS DGHVKVSYDL
2410 2420 2430 2440 2450
GSGMTSVVSN QNHNDGKWKA FTLSRIQKQA NISIVDIDSN QEENVATSSS
2460 2470 2480 2490 2500
GNNFGLDLKA DDKIYFGGLP TLRNLSMKAR PEVNVKKYSG CLKDIEISRT
2510 2520 2530 2540 2550
PYNILSSPDY VGVTKGCSLE NVYTVSFPKP GFVELAAVSI DVGTEINLSF
2560 2570 2580 2590 2600
STRNESGIIL LGSGGTLTPP RRKRRQTTQA YYAIFLNKGR LEVHLSSGTR
2610 2620 2630 2640 2650
TMRKIVIKPE PNLFHDGREH SVHVERTRGI FTVQIDEDRR HMQNLTEEQP
2660 2670 2680 2690 2700
IEVKKLFVGG APPEFQPSPL RNIPAFQGCV WNLVINSIPM DFAQPIAFKN
2710 2720 2730 2740 2750
ADIGRCTYQK PREDESEAVP AEVIVQPQPV PTPAFPFPAP TMVHGPCVAE
2760 2770 2780 2790 2800
SEPALLTGSK QFGLSRNSHI AIAFDDTKVK NRLTIELEVR TEAESGLLFY
2810 2820 2830 2840 2850
MARINHADFA TVQLRNGFPY FSYDLGSGDT STMIPTKIND GQWHKIKIVR
2860 2870 2880 2890 2900
VKQEGILYVD DASSQTISPK KADILDVVGI LYVGGLPINY TTRRIGPVTY
2910 2920 2930 2940 2950
SLDGCVRNLH MEQAPVDLDQ PTSSFHVGTC FANAESGTYF DGTGFAKAVG
2960 2970 2980 2990 3000
GFKVGLDLLV EFEFRTTRPT GVLLGVSSQK MDGMGIEMID EKLMFHVDNG
3010 3020 3030 3040 3050
AGRFTAIYDA GIPGHMCNGQ WHKVTAKKIK NRLELVVDGN QVDAQSPNSA
3060 3070 3080 3090 3100
STSADTNDPV FVGGFPGGLN QFGLTTNIRF RGCIRSLKLT KGTGKPLEVN
3110
FAKALELRGV QPVSCPTT
Length:3,118
Mass (Da):343,815
Last modified:October 16, 2013 - v2
Checksum:iCCD31C71B1E0DFD4
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti616I → L in AAC52165 (PubMed:7795883).Curated1
Sequence conflicti646I → V in AAC52165 (PubMed:7795883).Curated1
Sequence conflicti678 – 682ERVLM → GEILI in AAC52165 (PubMed:7795883).Curated5
Sequence conflicti704A → P in AAC52165 (PubMed:7795883).Curated1
Sequence conflicti853I → V in AAC52165 (PubMed:7795883).Curated1
Sequence conflicti908A → T in AAC52165 (PubMed:7795883).Curated1
Sequence conflicti917N → D in AAC52165 (PubMed:7795883).Curated1
Sequence conflicti925I → D in AAC52165 (PubMed:7795883).Curated1
Sequence conflicti1694Q → K in AAC52165 (PubMed:7795883).Curated1
Sequence conflicti1840R → Q in AAC52165 (PubMed:7795883).Curated1
Sequence conflicti2205D → I in AAC52165 (PubMed:7795883).Curated1
Sequence conflicti2214 – 2215EY → GF in AAC52165 (PubMed:7795883).Curated2
Sequence conflicti2523Y → N in AAC52165 (PubMed:7795883).Curated1
Sequence conflicti2642M → I in AAC52165 (PubMed:7795883).Curated1
Sequence conflicti2729P → S in AAC52165 (PubMed:7795883).Curated1
Sequence conflicti2739A → V in AAC52165 (PubMed:7795883).Curated1
Sequence conflicti2773A → V in AAC52165 (PubMed:7795883).Curated1
Sequence conflicti2802A → G in AAC52165 (PubMed:7795883).Curated1
Sequence conflicti2810A → G in AAC52165 (PubMed:7795883).Curated1
Sequence conflicti2820Y → F in AAC52165 (PubMed:7795883).Curated1
Sequence conflicti2829 – 2831DTS → STR in AAC52165 (PubMed:7795883).Curated3
Sequence conflicti2878V → G in AAC52165 (PubMed:7795883).Curated1
Sequence conflicti2946A → G in AAC52165 (PubMed:7795883).Curated1
Sequence conflicti2953K → I in AAC52165 (PubMed:7795883).Curated1
Sequence conflicti2976V → I in AAC52165 (PubMed:7795883).Curated1
Sequence conflicti3011G → E in AAC52165 (PubMed:7795883).Curated1
Sequence conflicti3022H → Y in AAC52165 (PubMed:7795883).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS48526.1.
PIRiI49077. S53868.
RefSeqiNP_032507.2. NM_008481.2.
UniGeneiMm.256087.

Genome annotation databases

EnsembliENSMUST00000092639; ENSMUSP00000090304; ENSMUSG00000019899.
GeneIDi16773.
KEGGimmu:16773.
UCSCiuc007esf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS48526.1.
PIRiI49077. S53868.
RefSeqiNP_032507.2. NM_008481.2.
UniGeneiMm.256087.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DYKX-ray2.00A2730-3094[»]
1OKQX-ray2.80A2730-3094[»]
1QU0X-ray2.35A/B/C/D2932-3106[»]
2WJSX-ray2.80A2136-2565[»]
A2579-2746[»]
5IK4X-ray1.27A2730-3118[»]
5IK5X-ray1.39A2730-3118[»]
5IK7X-ray2.00A/B2742-3118[»]
5IK8X-ray2.00A/B2742-3118[»]
ProteinModelPortaliQ60675.
SMRiQ60675.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-225176.
STRINGi10090.ENSMUSP00000090304.

PTM databases

iPTMnetiQ60675.
PhosphoSitePlusiQ60675.

Proteomic databases

MaxQBiQ60675.
PaxDbiQ60675.
PeptideAtlasiQ60675.
PRIDEiQ60675.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000092639; ENSMUSP00000090304; ENSMUSG00000019899.
GeneIDi16773.
KEGGimmu:16773.
UCSCiuc007esf.2. mouse.

Organism-specific databases

CTDi3908.
MGIiMGI:99912. Lama2.

Phylogenomic databases

eggNOGiENOG410KCXA. Eukaryota.
COG0419. LUCA.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000293201.
HOVERGENiHBG052298.
InParanoidiQ60675.
KOiK05637.
OMAiGYFNFQE.
OrthoDBiEOG091G005L.
TreeFamiTF335359.

Enzyme and pathway databases

ReactomeiR-MMU-3000157. Laminin interactions.
R-MMU-3000171. Non-integrin membrane-ECM interactions.
R-MMU-8874081. MET activates PTK2 signaling.

Miscellaneous databases

EvolutionaryTraceiQ60675.
PROiQ60675.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000019899.
CleanExiMM_LAMA2.
ExpressionAtlasiQ60675. baseline and differential.
GenevisibleiQ60675. MM.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR013320. ConA-like_dom.
IPR000742. EGF-like_dom.
IPR009030. Growth_fac_rcpt_.
IPR009254. Laminin_aI.
IPR010307. Laminin_domII.
IPR002049. Laminin_EGF.
IPR001791. Laminin_G.
IPR000034. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. 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]
SMARTiSM00181. EGF. 11 hits.
SM00180. EGF_Lam. 16 hits.
SM00281. LamB. 2 hits.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 5 hits.
SSF57184. SSF57184. 3 hits.
PROSITEiPS00022. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiLAMA2_MOUSE
AccessioniPrimary (citable) accession number: Q60675
Secondary accession number(s): F8VQ43, Q05003, Q64061
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 16, 2013
Last modified: November 30, 2016
This is version 164 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.