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Q60675

- LAMA2_MOUSE

UniProt

Q60675 - LAMA2_MOUSE

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Protein
Laminin subunit alpha-2
Gene
Lama2
Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  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
Complete GO annotation...

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi51 – 511N-linked (GlcNAc...) Reviewed prediction
Glycosylationi85 – 851N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi283 ↔ 292 By similarity
Disulfide bondi285 ↔ 303 By similarity
Glycosylationi299 – 2991N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi305 ↔ 314 By similarity
Disulfide bondi317 ↔ 337 By similarity
Disulfide bondi340 ↔ 349 By similarity
Disulfide bondi342 ↔ 374 By similarity
Glycosylationi359 – 3591N-linked (GlcNAc...) Reviewed prediction
Glycosylationi376 – 3761N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi377 ↔ 386 By similarity
Disulfide bondi389 ↔ 407 By similarity
Disulfide bondi410 ↔ 422 By similarity
Disulfide bondi412 ↔ 438 By similarity
Disulfide bondi440 ↔ 449 By similarity
Disulfide bondi452 ↔ 462 By similarity
Disulfide bondi465 ↔ 478 By similarity
Glycosylationi466 – 4661N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi467 ↔ 482 By similarity
Disulfide bondi484 ↔ 493 By similarity
Disulfide bondi496 ↔ 511 By similarity
Glycosylationi742 – 7421N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi753 ↔ 762 By similarity
Disulfide bondi755 ↔ 769 By similarity
Disulfide bondi772 ↔ 781 By similarity
Disulfide bondi784 ↔ 800 By similarity
Disulfide bondi803 ↔ 818 By similarity
Disulfide bondi805 ↔ 828 By similarity
Disulfide bondi831 ↔ 840 By similarity
Disulfide bondi843 ↔ 858 By similarity
Disulfide bondi861 ↔ 875 By similarity
Disulfide bondi863 ↔ 882 By similarity
Disulfide bondi885 ↔ 894 By similarity
Disulfide bondi897 ↔ 911 By similarity
Disulfide bondi914 ↔ 926 By similarity
Disulfide bondi916 ↔ 933 By similarity
Glycosylationi919 – 9191N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi935 ↔ 944 By similarity
Disulfide bondi947 ↔ 960 By similarity
Disulfide bondi963 ↔ 975 By similarity
Disulfide bondi965 ↔ 981 By similarity
Disulfide bondi983 ↔ 992 By similarity
Disulfide bondi995 ↔ 1007 By similarity
Disulfide bondi1010 ↔ 1019 By similarity
Disulfide bondi1012 ↔ 1026 By similarity
Disulfide bondi1028 ↔ 1037 By similarity
Glycosylationi1031 – 10311N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1040 ↔ 1053 By similarity
Disulfide bondi1056 ↔ 1068 By similarity
Glycosylationi1057 – 10571N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1058 ↔ 1075 By similarity
Disulfide bondi1077 ↔ 1086 By similarity
Disulfide bondi1089 ↔ 1099 By similarity
Disulfide bondi1102 ↔ 1114 By similarity
Disulfide bondi1104 ↔ 1130 By similarity
Disulfide bondi1132 ↔ 1141 By similarity
Disulfide bondi1144 ↔ 1159 By similarity
Disulfide bondi1378 ↔ 1387 By similarity
Disulfide bondi1416 ↔ 1425 By similarity
Disulfide bondi1418 ↔ 1432 By similarity
Disulfide bondi1435 ↔ 1444 By similarity
Disulfide bondi1447 ↔ 1462 By similarity
Disulfide bondi1465 ↔ 1480 By similarity
Disulfide bondi1467 ↔ 1490 By similarity
Disulfide bondi1493 ↔ 1502 By similarity
Disulfide bondi1505 ↔ 1520 By similarity
Disulfide bondi1523 ↔ 1535 By similarity
Disulfide bondi1525 ↔ 1542 By similarity
Disulfide bondi1544 ↔ 1553 By similarity
Disulfide bondi1556 ↔ 1567 By similarity
Disulfide bondi1570 – 1570Interchain Inferred
Disulfide bondi1574 – 1574Interchain Inferred
Glycosylationi1593 – 15931N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1610 – 16101N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1696 – 16961N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1806 – 18061N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1897 – 18971N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1912 – 19121N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1916 – 19161N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2013 – 20131N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2024 – 20241N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2041 – 20411N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2122 – 21221N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2236 – 22361N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2298 ↔ 2324 By similarity
Glycosylationi2356 – 23561N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2431 – 24311N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2474 – 24741N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2491 ↔ 2517 By similarity
Glycosylationi2547 – 25471N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2554 – 25541N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2644 – 26441N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2679 ↔ 2706 By similarity
Glycosylationi2889 – 28891N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2905 ↔ 2930 By similarity
Disulfide bondi3083 ↔ 3115 By 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

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.

Miscellaneous databases

EvolutionaryTraceiQ60675.

Family & Domainsi

Domains and Repeats

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

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1662 – 1863202 Reviewed prediction
Add
BLAST
Coiled coili1923 – 2146224 Reviewed prediction
Add
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

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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti616 – 6161I → L in AAC52165. 1 Publication
Sequence conflicti646 – 6461I → V in AAC52165. 1 Publication
Sequence conflicti678 – 6825ERVLM → GEILI in AAC52165. 1 Publication
Sequence conflicti704 – 7041A → P in AAC52165. 1 Publication
Sequence conflicti853 – 8531I → V in AAC52165. 1 Publication
Sequence conflicti908 – 9081A → T in AAC52165. 1 Publication
Sequence conflicti917 – 9171N → D in AAC52165. 1 Publication
Sequence conflicti925 – 9251I → D in AAC52165. 1 Publication
Sequence conflicti1694 – 16941Q → K in AAC52165. 1 Publication
Sequence conflicti1840 – 18401R → Q in AAC52165. 1 Publication
Sequence conflicti2205 – 22051D → I in AAC52165. 1 Publication
Sequence conflicti2214 – 22152EY → GF in AAC52165. 1 Publication
Sequence conflicti2523 – 25231Y → N in AAC52165. 1 Publication
Sequence conflicti2642 – 26421M → I in AAC52165. 1 Publication
Sequence conflicti2729 – 27291P → S in AAC52165. 1 Publication
Sequence conflicti2739 – 27391A → V in AAC52165. 1 Publication
Sequence conflicti2773 – 27731A → V in AAC52165. 1 Publication
Sequence conflicti2802 – 28021A → G in AAC52165. 1 Publication
Sequence conflicti2810 – 28101A → G in AAC52165. 1 Publication
Sequence conflicti2820 – 28201Y → F in AAC52165. 1 Publication
Sequence conflicti2829 – 28313DTS → STR in AAC52165. 1 Publication
Sequence conflicti2878 – 28781V → G in AAC52165. 1 Publication
Sequence conflicti2946 – 29461A → G in AAC52165. 1 Publication
Sequence conflicti2953 – 29531K → I in AAC52165. 1 Publication
Sequence conflicti2976 – 29761V → I in AAC52165. 1 Publication
Sequence conflicti3011 – 30111G → E in AAC52165. 1 Publication
Sequence conflicti3022 – 30221H → Y in AAC52165. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 142 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

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