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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. extracellular matrix organization Source: Ensembl
  4. myelination in peripheral nervous system Source: Ensembl
  5. positive regulation of synaptic transmission, cholinergic Source: MGI
  6. regulation of cell adhesion Source: InterPro
  7. regulation of cell migration Source: InterPro
  8. 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. dendritic spine Source: Ensembl
  4. extracellular region Source: Reactome
  5. extracellular vesicular exosome Source: Ensembl
  6. laminin-1 complex Source: InterPro
  7. 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 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.
ExpressionAtlasiQ60675. baseline and differential.
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.
GeneTreeiENSGT00760000119121.
HOGENOMiHOG000293201.
HOVERGENiHBG052298.
InParanoidiQ60675.
KOiK05637.
OMAiHTTTKGI.
OrthoDBiEOG7SR4KJ.
TreeFamiTF335359.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR013320. ConA-like_dom.
IPR002049. EGF_laminin.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_N_dom.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR010307. Laminin_domII.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
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 [UniParc]FASTAAdd to Basket

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        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 AAC52165.1 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 ENSGT00760000119121.
HOGENOMi HOG000293201.
HOVERGENi HBG052298.
InParanoidi Q60675.
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.
ExpressionAtlasi Q60675. baseline and differential.
Genevestigatori Q60675.

Family and domain databases

Gene3Di 2.60.120.200. 5 hits.
InterProi IPR013320. ConA-like_dom.
IPR002049. EGF_laminin.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_N_dom.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR010307. Laminin_domII.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
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: October 29, 2014
This is version 144 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