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Q60675

- LAMA2_MOUSE

UniProt

Q60675 - LAMA2_MOUSE

Protein

Laminin subunit alpha-2

Gene

Lama2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (16 Oct 2013)
      Previous versions | rss
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    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

    1. axon guidance Source: MGI
    2. cell adhesion Source: UniProtKB-KW
    3. positive regulation of synaptic transmission, cholinergic Source: MGI
    4. regulation of cell adhesion Source: InterPro
    5. regulation of cell migration Source: InterPro
    6. regulation of embryonic development Source: InterPro

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_196606. ECM proteoglycans.
    REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_202342. Laminin interactions.

    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
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:99912. Lama2.

    Subcellular locationi

    GO - Cellular componenti

    1. basal lamina Source: MGI
    2. basement membrane Source: MGI
    3. extracellular region Source: Reactome
    4. laminin-1 complex Source: InterPro
    5. sarcolemma Source: MGI

    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)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19191 PublicationAdd
    BLAST
    Chaini20 – 31183099Laminin subunit alpha-2PRO_0000017057Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi51 – 511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi85 – 851N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi283 ↔ 292By similarity
    Disulfide bondi285 ↔ 303By similarity
    Glycosylationi299 – 2991N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi305 ↔ 314By similarity
    Disulfide bondi317 ↔ 337By similarity
    Disulfide bondi340 ↔ 349By similarity
    Disulfide bondi342 ↔ 374By similarity
    Glycosylationi359 – 3591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi376 – 3761N-linked (GlcNAc...)Sequence Analysis
    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
    Glycosylationi466 – 4661N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi467 ↔ 482By similarity
    Disulfide bondi484 ↔ 493By similarity
    Disulfide bondi496 ↔ 511By similarity
    Glycosylationi742 – 7421N-linked (GlcNAc...)Sequence Analysis
    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
    Glycosylationi919 – 9191N-linked (GlcNAc...)Sequence Analysis
    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
    Glycosylationi1031 – 10311N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1040 ↔ 1053By similarity
    Disulfide bondi1056 ↔ 1068By similarity
    Glycosylationi1057 – 10571N-linked (GlcNAc...)Sequence Analysis
    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 bondi1570 – 1570InterchainCurated
    Disulfide bondi1574 – 1574InterchainCurated
    Glycosylationi1593 – 15931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1610 – 16101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1696 – 16961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1806 – 18061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1897 – 18971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1912 – 19121N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1916 – 19161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2013 – 20131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2024 – 20241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2041 – 20411N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2122 – 21221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2236 – 22361N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2298 ↔ 2324By similarity
    Glycosylationi2356 – 23561N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2431 – 24311N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2474 – 24741N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2491 ↔ 2517By similarity
    Glycosylationi2547 – 25471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2554 – 25541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2644 – 26441N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2679 ↔ 2706By similarity
    Glycosylationi2889 – 28891N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2905 ↔ 2930By similarity
    Disulfide bondi3083 ↔ 3115By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ60675.
    PaxDbiQ60675.
    PRIDEiQ60675.

    PTM databases

    PhosphoSiteiQ60675.

    Expressioni

    Gene expression databases

    CleanExiMM_LAMA2.
    GenevestigatoriQ60675.

    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.

    Structurei

    Secondary structure

    1
    3118
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2151 – 21544
    Beta strandi2163 – 217311
    Beta strandi2177 – 21837
    Beta strandi2190 – 21967
    Beta strandi2199 – 220810
    Beta strandi2210 – 22145
    Beta strandi2226 – 22338
    Beta strandi2236 – 224611
    Turni2247 – 22504
    Beta strandi2256 – 22594
    Beta strandi2274 – 22796
    Beta strandi2297 – 22993
    Beta strandi2303 – 23086
    Beta strandi2316 – 23194
    Beta strandi2337 – 234812
    Beta strandi2357 – 236711
    Beta strandi2369 – 23779
    Beta strandi2381 – 239010
    Beta strandi2393 – 23997
    Beta strandi2404 – 24085
    Beta strandi2415 – 24173
    Beta strandi2419 – 24268
    Beta strandi2429 – 24368
    Turni2437 – 24393
    Beta strandi2442 – 24487
    Beta strandi2463 – 24675
    Beta strandi2489 – 24979
    Beta strandi2500 – 25023
    Helixi2504 – 25063
    Beta strandi2511 – 25166
    Beta strandi2524 – 25263
    Beta strandi2528 – 25303
    Beta strandi2532 – 25354
    Beta strandi2544 – 255310
    Beta strandi2555 – 25628
    Beta strandi2581 – 25877
    Beta strandi2590 – 25967
    Beta strandi2603 – 26075
    Beta strandi2614 – 26185
    Beta strandi2620 – 26267
    Beta strandi2628 – 263811
    Beta strandi2641 – 26444
    Beta strandi2656 – 26594
    Beta strandi2678 – 26858
    Beta strandi2696 – 27005
    Beta strandi2760 – 27623
    Beta strandi2769 – 27735
    Helixi2776 – 27794
    Beta strandi2780 – 279112
    Beta strandi2796 – 28027
    Beta strandi2806 – 281510
    Beta strandi2818 – 282710
    Beta strandi2829 – 28335
    Beta strandi2840 – 28423
    Beta strandi2844 – 28518
    Beta strandi2854 – 28596
    Beta strandi2862 – 28676
    Beta strandi2869 – 28713
    Beta strandi2879 – 28857
    Beta strandi2903 – 291412
    Beta strandi2922 – 29265
    Beta strandi2931 – 294717
    Beta strandi2950 – 29523
    Beta strandi2955 – 296713
    Beta strandi2971 – 29777
    Beta strandi2979 – 29813
    Beta strandi2983 – 29897
    Beta strandi2992 – 300110
    Beta strandi3004 – 30085
    Helixi3015 – 30173
    Beta strandi3018 – 30203
    Beta strandi3022 – 30298
    Beta strandi3032 – 30376
    Beta strandi3040 – 30456
    Beta strandi3061 – 30633
    Beta strandi3081 – 309010
    Helixi3101 – 31033

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DYKX-ray2.00A2730-3094[»]
    1OKQX-ray2.80A2730-3094[»]
    1QU0X-ray2.35A/B/C/D2932-3106[»]
    2WJSX-ray2.80A2136-2565[»]
    A2579-2746[»]
    ProteinModelPortaliQ60675.
    SMRiQ60675. Positions 2142-2707, 2744-3117.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ60675.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 282252Laminin N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini283 – 33957Laminin EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini340 – 40970Laminin EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini410 – 46455Laminin EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini465 – 51349Laminin EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini514 – 52310Laminin EGF-like 5; first partPROSITE-ProRule annotation
    Domaini527 – 719193Laminin IV type A 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini720 – 75233Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd
    BLAST
    Domaini753 – 80250Laminin EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini803 – 86058Laminin EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini861 – 91353Laminin EGF-like 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini914 – 96249Laminin EGF-like 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini963 – 100947Laminin EGF-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1010 – 105546Laminin EGF-like 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini1056 – 110146Laminin EGF-like 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini1102 – 116160Laminin EGF-like 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini1162 – 117110Laminin EGF-like 14; first partPROSITE-ProRule annotation
    Domaini1172 – 1375204Laminin IV type A 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1376 – 141540Laminin EGF-like 14; second partPROSITE-ProRule annotationAdd
    BLAST
    Domaini1416 – 146449Laminin EGF-like 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini1465 – 152258Laminin EGF-like 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini1523 – 156947Laminin EGF-like 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini2141 – 2324184Laminin G-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini2336 – 2517182Laminin G-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2522 – 2706185Laminin G-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini2759 – 2930172Laminin G-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini2929 – 3115187Laminin G-like 5PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1570 – 2140571Domain II and IAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1662 – 1863202Sequence AnalysisAdd
    BLAST
    Coiled coili1923 – 2146224Sequence AnalysisAdd
    BLAST

    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

    eggNOGiCOG0419.
    GeneTreeiENSGT00750000117374.
    HOGENOMiHOG000293201.
    HOVERGENiHBG052298.
    KOiK05637.
    OMAiHTTTKGI.
    OrthoDBiEOG7SR4KJ.
    TreeFamiTF335359.

    Family and domain databases

    Gene3Di2.60.120.200. 5 hits.
    InterProiIPR008985. 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]
    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]
    SMARTiSM00180. EGF_Lam. 15 hits.
    SM00281. LamB. 2 hits.
    SM00282. LamG. 5 hits.
    SM00136. LamNT. 1 hit.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.
    SSF49899. 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

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    MPAATAGILL LLLLGTLEGS QTQRRQSQAH QQRGLFPAVL NLASNALITT     50
    NATCGEKGPE MYCKLVEHVP GQPVRNPQCR ICNQNSSNPY QRHPITNAID 100
    GKNTWWQSPS IKNGVEYHYV TITLDLQQVF QIAYVIVKAA NSPRPGNWIL 150
    ERSLDDVEYK PWQYHAVTDT ECLTLYNIYP RTGPPSYAKD DEVICTSFYS 200
    KIHPLENGEI HISLINGRPS ADDPSPELLE FTSARYIRLR FQRIRTLNAD 250
    LMMFAHKDPR EIDPIVTRRY YYSVKDISVG GMCICYGHAR ACPLDPATNK 300
    SRCECEHNTC GESCDRCCPG FHQKPWRAGT FLTKSECEAC NCHGKAEECY 350
    YDETVASRNL SLNIHGKYIG GGVCINCTHN TAGINCETCV DGFFRPKGVS 400
    PNYPRPCQPC HCDPTGSLSE VCVKDEKYAQ RGLKPGSCHC KTGFGGVNCD 450
    RCVRGYHGYP DCQPCNCSGL GSTNEDPCVG PCSCKENVEG EDCSRCKSGF 500
    FNLQEDNQKG CEECFCSGVS NRCQSSYWTY GNIQDMRGWY LTDLSGRIRM 550
    APQLDNPDSP QQISISNSEA RKSLLDGYYW SAPPPYLGNR LPAVGGQLSF 600
    TISYDLEEEE DDTEKILQLM IIFEGNDLRI STAYKEVYLE PSEEHIEEVS 650
    LKEEAFTIHG TNLPVTRKDF MIVLTNLERV LMQITYNLGM DAIFRLSSVN 700
    LESAVPYPTD RRIATDVEVC QCPPGYSGSS CETCWPRHRR VNGTIFGGIC 750
    EPCQCFAHAE ACDDITGECL NCKDHTGGPY CNECLPGFYG DPTRGSPEDC 800
    QPCACPLNIP SNNFSPTCHL DRSLGLICDE CPIGYTGPRC ERCAEGYFGQ 850
    PSIPGGSCQP CQCNDNLDYS IPGSCDSLSG SCLICKPGTT GRYCELCADG 900
    YFGDAVNAKN CQPCRCNING SFSEICHTRT GQCECRPNVQ GRHCDECKPE 950
    TFGLQLGRGC LPCNCNSFGS KSFDCEASGQ CWCQPGVAGK KCDRCAHGYF 1000
    NFQEGGCIAC DCSHLGNNCD PKTGQCICPP NTTGEKCSEC LPNTWGHSIV 1050
    TGCKVCNCST VGSLASQCNV NTGQCSCHPK FSGMKCSECS RGHWNYPLCT 1100
    LCDCFLPGTD ATTCDLETRK CSCSDQTGQC SCKVNVEGVH CDRCRPGKFG 1150
    LDAKNPLGCS SCYCFGVTSQ CSEAKGLIRT WVTLSDEQTI LPLVDEALQH 1200
    TTTKGIAFQK PEIVAKMDEV RQELHLEPFY WKLPQQFEGK KLMAYGGKLK 1250
    YAIYFEARDE TGFATYKPQV IIRGGTPTHA RIITRHMAAP LIGQLTRHEI 1300
    EMTEKEWKYY GDDPRISRTV TREDFLDILY DIHYILIKAT YGNVVRQSRI 1350
    SEISMEVAEP GHVLAGSPPA HLIERCDCPP GYSGLSCETC APGFYRLRSE 1400
    PGGRTPGPTL GTCVPCQCNG HSSQCDPETS VCQNCQHHTA GDFCERCALG 1450
    YYGIVRGLPN DCQPCACPLI SPSNNFSPSC VLEGLEDYRC TACPRGYEGQ 1500
    YCERCAPGYT GSPSSPGGSC QECECDPYGS LPVPCDRVTG LCTCRPGATG 1550
    RKCDGCEHWH AREGAECVFC GDECTGLLLG DLARLEQMTM NINLTGPLPA 1600
    PYKILYGLEN TTQELKHLLS PQRAPERLIQ LAEGNVNTLV METNELLTRA 1650
    TKVTADGEQT GQDAERTNSR AESLEEFIKG LVQDAEAINE KAVQLNETLG 1700
    NQDKTAERNL EELQKEIDRM LKELRSKDLQ TQKEVAEDEL VAAEGLLKRV 1750
    NKLFGEPRAQ NEDMEKDLQQ KLAEYKNKLD DAWDLLREAT DKTRDANRLS 1800
    AANQKNMTIL ETKKEAIEGS KRQIENTLKE GNDILDEANR LLGEINSVID 1850
    YVDDIKTKLP PMSEELSDKI DDLAQEIKDR RLAEKVFQAE SHAAQLNDSS 1900
    AVLDGILDEA KNISFNATAA FRAYSNIKDY IDEAEKVARE AKELAQGATK 1950
    LATSPQGLLK EDAKGSLQKS FRILNEAKKL ANDVKGNHND LNDLKTRLET 2000
    ADLRNSGLLG ALNDTMDKLS AITNDTAAKL QAVKEKAREA NDTAKAVLAQ 2050
    VKDLHQNLDG LKQNYNKLAD SVAKTNAVVK DPSKNKIIAD AGTSVRNLEQ 2100
    EADRLIDKLK PIKELEDNLK KNISEIKELI NQARKQANSI KVSVSSGGDC 2150
    VRTYRPEIKK GSYNNIVVHV KTAVADNLLF YLGSAKFIDF LAIEMRKGKV 2200
    SFLWDVGSGV GRVEYPDLTI DDSYWYRIEA SRTGRNGSIS VRALDGPKAS 2250
    MVPSTYHSVS PPGYTILDVD ANAMLFVGGL TGKIKKADAV RVITFTGCMG 2300
    ETYFDNKPIG LWNFREKEGD CKGCTVSPQV EDSEGTIQFD GEGYALVSRP 2350
    IRWYPNISTV MFKFRTFSSS ALLMYLATRD LKDFMSVELS DGHVKVSYDL 2400
    GSGMTSVVSN QNHNDGKWKA FTLSRIQKQA NISIVDIDSN QEENVATSSS 2450
    GNNFGLDLKA DDKIYFGGLP TLRNLSMKAR PEVNVKKYSG CLKDIEISRT 2500
    PYNILSSPDY VGVTKGCSLE NVYTVSFPKP GFVELAAVSI DVGTEINLSF 2550
    STRNESGIIL LGSGGTLTPP RRKRRQTTQA YYAIFLNKGR LEVHLSSGTR 2600
    TMRKIVIKPE PNLFHDGREH SVHVERTRGI FTVQIDEDRR HMQNLTEEQP 2650
    IEVKKLFVGG APPEFQPSPL RNIPAFQGCV WNLVINSIPM DFAQPIAFKN 2700
    ADIGRCTYQK PREDESEAVP AEVIVQPQPV PTPAFPFPAP TMVHGPCVAE 2750
    SEPALLTGSK QFGLSRNSHI AIAFDDTKVK NRLTIELEVR TEAESGLLFY 2800
    MARINHADFA TVQLRNGFPY FSYDLGSGDT STMIPTKIND GQWHKIKIVR 2850
    VKQEGILYVD DASSQTISPK KADILDVVGI LYVGGLPINY TTRRIGPVTY 2900
    SLDGCVRNLH MEQAPVDLDQ PTSSFHVGTC FANAESGTYF DGTGFAKAVG 2950
    GFKVGLDLLV EFEFRTTRPT GVLLGVSSQK MDGMGIEMID EKLMFHVDNG 3000
    AGRFTAIYDA GIPGHMCNGQ WHKVTAKKIK NRLELVVDGN QVDAQSPNSA 3050
    STSADTNDPV FVGGFPGGLN QFGLTTNIRF RGCIRSLKLT KGTGKPLEVN 3100
    FAKALELRGV QPVSCPTT 3118
    Length:3,118
    Mass (Da):343,815
    Last modified:October 16, 2013 - v2
    Checksum:iCCD31C71B1E0DFD4
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti616 – 6161I → L in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti646 – 6461I → V in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti678 – 6825ERVLM → GEILI in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti704 – 7041A → P in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti853 – 8531I → V in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti908 – 9081A → T in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti917 – 9171N → D in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti925 – 9251I → D in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti1694 – 16941Q → K in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti1840 – 18401R → Q in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti2205 – 22051D → I in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti2214 – 22152EY → GF in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti2523 – 25231Y → N in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti2642 – 26421M → I in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti2729 – 27291P → S in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti2739 – 27391A → V in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti2773 – 27731A → V in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti2802 – 28021A → G in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti2810 – 28101A → G in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti2820 – 28201Y → F in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti2829 – 28313DTS → STR in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti2878 – 28781V → G in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti2946 – 29461A → G in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti2953 – 29531K → I in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti2976 – 29761V → I in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti3011 – 30111G → E in AAC52165. (PubMed:7795883)Curated
    Sequence conflicti3022 – 30221H → Y in AAC52165. (PubMed:7795883)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS48526.1.
    PIRi I49077. S53868.
    RefSeqi NP_032507.2. NM_008481.2.
    UniGenei Mm.256087.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DYK X-ray 2.00 A 2730-3094 [» ]
    1OKQ X-ray 2.80 A 2730-3094 [» ]
    1QU0 X-ray 2.35 A/B/C/D 2932-3106 [» ]
    2WJS X-ray 2.80 A 2136-2565 [» ]
    A 2579-2746 [» ]
    ProteinModelPortali Q60675.
    SMRi Q60675. Positions 2142-2707, 2744-3117.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-225176.

    PTM databases

    PhosphoSitei Q60675.

    Proteomic databases

    MaxQBi Q60675.
    PaxDbi Q60675.
    PRIDEi Q60675.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000092639 ; ENSMUSP00000090304 ; ENSMUSG00000019899 .
    GeneIDi 16773.
    KEGGi mmu:16773.

    Organism-specific databases

    CTDi 3908.
    MGIi MGI:99912. Lama2.

    Phylogenomic databases

    eggNOGi COG0419.
    GeneTreei ENSGT00750000117374.
    HOGENOMi HOG000293201.
    HOVERGENi HBG052298.
    KOi K05637.
    OMAi HTTTKGI.
    OrthoDBi EOG7SR4KJ.
    TreeFami TF335359.

    Enzyme and pathway databases

    Reactomei REACT_196606. ECM proteoglycans.
    REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_202342. Laminin interactions.

    Miscellaneous databases

    ChiTaRSi LAMA2. mouse.
    EvolutionaryTracei Q60675.
    NextBioi 290606.
    PROi Q60675.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_LAMA2.
    Genevestigatori Q60675.

    Family and domain databases

    Gene3Di 2.60.120.200. 5 hits.
    InterProi IPR008985. 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 ]
    Pfami PF00052. 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 ]
    SMARTi SM00180. EGF_Lam. 15 hits.
    SM00281. LamB. 2 hits.
    SM00282. LamG. 5 hits.
    SM00136. LamNT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49785. SSF49785. 1 hit.
    SSF49899. SSF49899. 5 hits.
    SSF57184. SSF57184. 3 hits.
    PROSITEi PS00022. 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 ]
    ProtoNeti Search...

    Publicationsi

    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. 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.

    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: October 1, 2014
    This is version 143 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

    External Data

    Dasty 3