UniProtKB - Q61789 (LAMA3_MOUSE)
Laminin subunit alpha-3
Lama3
Functioni
GO - Molecular functioni
- extracellular matrix structural constituent Source: GO_Central
- integrin binding Source: GO_Central
GO - Biological processi
- animal organ morphogenesis Source: GO_Central
- axon guidance Source: GO_Central
- cell-cell adhesion Source: MGI
- cell migration Source: GO_Central
- endodermal cell differentiation Source: Ensembl
- hemidesmosome assembly Source: MGI
- integrin-mediated signaling pathway Source: GO_Central
- morphogenesis of a polarized epithelium Source: GO_Central
- regulation of cell adhesion Source: InterPro
- regulation of cell migration Source: InterPro
- regulation of embryonic development Source: InterPro
- tissue development Source: GO_Central
Keywordsi
Biological process | Cell adhesion |
Enzyme and pathway databases
Reactomei | R-MMU-1474228, Degradation of the extracellular matrix R-MMU-2022090, Assembly of collagen fibrils and other multimeric structures R-MMU-2214320, Anchoring fibril formation R-MMU-3000157, Laminin interactions R-MMU-446107, Type I hemidesmosome assembly R-MMU-8874081, MET activates PTK2 signaling |
Names & Taxonomyi
Protein namesi | Recommended name: Laminin subunit alpha-3Alternative name(s): Epiligrin subunit alpha Kalinin subunit alpha Laminin-5 subunit alpha Laminin-6 subunit alpha Laminin-7 subunit alpha Nicein subunit alpha |
Gene namesi | Name:Lama3 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:99909, Lama3 |
Subcellular locationi
Extracellular region or secreted
Note: Major component.
Endoplasmic reticulum
- endoplasmic reticulum Source: MGI
Extracellular region or secreted
- extracellular region Source: Reactome
Other locations
- adherens junction Source: MGI
- basement membrane Source: MGI
- collagen-containing extracellular matrix Source: BHF-UCL
- hemidesmosome Source: MGI
- laminin-3 complex Source: MGI
- laminin-5 complex Source: MGI
Keywords - Cellular componenti
Basement membrane, Extracellular matrix, SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 31 | 1 PublicationAdd BLAST | 31 | |
ChainiPRO_0000017059 | 32 – 3330 | Laminin subunit alpha-3Add BLAST | 3299 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 139 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 296 ↔ 305 | By similarity | ||
Disulfide bondi | 298 ↔ 316 | By similarity | ||
Disulfide bondi | 318 ↔ 327 | By similarity | ||
Disulfide bondi | 330 ↔ 350 | By similarity | ||
Disulfide bondi | 353 ↔ 362 | By similarity | ||
Disulfide bondi | 355 ↔ 387 | By similarity | ||
Disulfide bondi | 390 ↔ 399 | By similarity | ||
Disulfide bondi | 402 ↔ 420 | By similarity | ||
Disulfide bondi | 423 ↔ 433 | By similarity | ||
Disulfide bondi | 425 ↔ 440 | By similarity | ||
Disulfide bondi | 442 ↔ 451 | By similarity | ||
Glycosylationi | 445 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 454 ↔ 464 | By similarity | ||
Disulfide bondi | 488 ↔ 500 | By similarity | ||
Disulfide bondi | 490 ↔ 506 | By similarity | ||
Disulfide bondi | 508 ↔ 517 | By similarity | ||
Disulfide bondi | 520 ↔ 530 | By similarity | ||
Disulfide bondi | 533 ↔ 545 | By similarity | ||
Disulfide bondi | 535 ↔ 552 | By similarity | ||
Disulfide bondi | 554 ↔ 563 | By similarity | ||
Disulfide bondi | 566 ↔ 583 | By similarity | ||
Disulfide bondi | 628 ↔ 642 | By similarity | ||
Disulfide bondi | 630 ↔ 649 | By similarity | ||
Disulfide bondi | 651 ↔ 660 | By similarity | ||
Disulfide bondi | 663 ↔ 678 | By similarity | ||
Disulfide bondi | 681 ↔ 693 | By similarity | ||
Disulfide bondi | 683 ↔ 700 | By similarity | ||
Disulfide bondi | 702 ↔ 711 | By similarity | ||
Disulfide bondi | 1309 ↔ 1316 | By similarity | ||
Disulfide bondi | 1311 ↔ 1323 | By similarity | ||
Disulfide bondi | 1325 ↔ 1334 | By similarity | ||
Disulfide bondi | 1337 ↔ 1350 | By similarity | ||
Disulfide bondi | 1353 ↔ 1368 | By similarity | ||
Glycosylationi | 1354 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1355 ↔ 1375 | By similarity | ||
Disulfide bondi | 1377 ↔ 1386 | By similarity | ||
Disulfide bondi | 1389 ↔ 1399 | By similarity | ||
Disulfide bondi | 1402 ↔ 1414 | By similarity | ||
Disulfide bondi | 1404 ↔ 1421 | By similarity | ||
Disulfide bondi | 1423 ↔ 1432 | By similarity | ||
Disulfide bondi | 1435 ↔ 1450 | By similarity | ||
Glycosylationi | 1673 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1684 ↔ 1693 | By similarity | ||
Disulfide bondi | 1686 ↔ 1700 | By similarity | ||
Disulfide bondi | 1703 ↔ 1712 | By similarity | ||
Disulfide bondi | 1715 ↔ 1728 | By similarity | ||
Disulfide bondi | 1731 ↔ 1743 | By similarity | ||
Disulfide bondi | 1733 ↔ 1752 | By similarity | ||
Disulfide bondi | 1754 ↔ 1763 | By similarity | ||
Disulfide bondi | 1766 ↔ 1781 | By similarity | ||
Disulfide bondi | 1819 | InterchainCurated | ||
Disulfide bondi | 1822 | InterchainCurated | ||
Glycosylationi | 2159 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2261 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2332 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2361 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2498 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2557 ↔ 2587 | By similarity | ||
Glycosylationi | 2580 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2733 ↔ 2756 | By similarity | ||
Glycosylationi | 2747 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2891 ↔ 2923 | By similarity | ||
Glycosylationi | 3094 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 3124 ↔ 3147 | By similarity | ||
Glycosylationi | 3270 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 3299 ↔ 3327 | By similarity |
Keywords - PTMi
Disulfide bond, GlycoproteinProteomic databases
PaxDbi | Q61789 |
PeptideAtlasi | Q61789 |
PRIDEi | Q61789 |
ProteomicsDBi | 264908 [Q61789-1] 264909 [Q61789-2] |
PTM databases
GlyGeni | Q61789, 13 sites |
iPTMneti | Q61789 |
PhosphoSitePlusi | Q61789 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSMUSG00000024421, Expressed in molar tooth and 143 other tissues |
Genevisiblei | Q61789, 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-3 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein), laminin-6 (laminin-311 or K-laminin) and laminin-7 (laminin-321 or KS-laminin).
GO - Molecular functioni
- integrin binding Source: GO_Central
Protein-protein interaction databases
BioGRIDi | 201098, 8 interactors |
ComplexPortali | CPX-3012, Laminin-332 complex variant A [Q61789-2] CPX-3013, Laminin-311 complex variant A [Q61789-2] CPX-3014, Laminin-321 complex [Q61789-2] CPX-3164, Laminin-332 complex variant B [Q61789-1] CPX-3167, Laminin-311 complex variant B [Q61789-1] |
IntActi | Q61789, 1 interactor |
STRINGi | 10090.ENSMUSP00000089703 |
Miscellaneous databases
RNActi | Q61789, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 40 – 295 | Laminin N-terminalPROSITE-ProRule annotationAdd BLAST | 256 | |
Domaini | 296 – 350 | Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST | 55 | |
Domaini | 353 – 420 | Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST | 68 | |
Domaini | 423 – 464 | Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST | 42 | |
Domaini | 488 – 530 | Laminin EGF-like 4PROSITE-ProRule annotationAdd BLAST | 43 | |
Domaini | 533 – 576 | Laminin EGF-like 5PROSITE-ProRule annotationAdd BLAST | 44 | |
Domaini | 582 – 625 | Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST | 44 | |
Domaini | 628 – 678 | Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST | 51 | |
Domaini | 681 – 725 | Laminin EGF-like 8PROSITE-ProRule annotationAdd BLAST | 45 | |
Domaini | 1309 – 1352 | Laminin EGF-like 9PROSITE-ProRule annotationAdd BLAST | 44 | |
Domaini | 1353 – 1401 | Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST | 49 | |
Domaini | 1402 – 1452 | Laminin EGF-like 11PROSITE-ProRule annotationAdd BLAST | 51 | |
Domaini | 1453 – 1462 | Laminin EGF-like 12; first partPROSITE-ProRule annotation | 10 | |
Domaini | 1466 – 1650 | Laminin IV type APROSITE-ProRule annotationAdd BLAST | 185 | |
Domaini | 1651 – 1683 | Laminin EGF-like 12; second partPROSITE-ProRule annotationAdd BLAST | 33 | |
Domaini | 1684 – 1730 | Laminin EGF-like 13PROSITE-ProRule annotationAdd BLAST | 47 | |
Domaini | 1731 – 1783 | Laminin EGF-like 14PROSITE-ProRule annotationAdd BLAST | 53 | |
Domaini | 1784 – 1818 | Laminin EGF-like 15; truncatedPROSITE-ProRule annotationAdd BLAST | 35 | |
Domaini | 2386 – 2587 | Laminin G-like 1PROSITE-ProRule annotationAdd BLAST | 202 | |
Domaini | 2594 – 2756 | Laminin G-like 2PROSITE-ProRule annotationAdd BLAST | 163 | |
Domaini | 2763 – 2923 | Laminin G-like 3PROSITE-ProRule annotationAdd BLAST | 161 | |
Domaini | 2983 – 3147 | Laminin G-like 4PROSITE-ProRule annotationAdd BLAST | 165 | |
Domaini | 3154 – 3327 | Laminin G-like 5PROSITE-ProRule annotationAdd BLAST | 174 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 295 – 725 | Domain VAdd BLAST | 431 | |
Regioni | 793 – 1262 | Domain IV 1 (domain IV B)Add BLAST | 470 | |
Regioni | 1263 – 1462 | Domain III BAdd BLAST | 200 | |
Regioni | 1651 – 1818 | Domain III AAdd BLAST | 168 | |
Regioni | 1819 – 2385 | Domain II and IAdd BLAST | 567 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 1851 – 1980 | Sequence analysisAdd BLAST | 130 | |
Coiled coili | 2012 – 2057 | Sequence analysisAdd BLAST | 46 | |
Coiled coili | 2088 – 2165 | Sequence analysisAdd BLAST | 78 | |
Coiled coili | 2211 – 2238 | Sequence analysisAdd BLAST | 28 | |
Coiled coili | 2318 – 2383 | Sequence analysisAdd BLAST | 66 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 2274 – 2276 | Cell attachment siteSequence analysis | 3 |
Domaini
Keywords - Domaini
Coiled coil, Laminin EGF-like domain, Repeat, SignalPhylogenomic databases
eggNOGi | KOG1836, Eukaryota |
GeneTreei | ENSGT00940000155638 |
HOGENOMi | CLU_000301_1_0_1 |
InParanoidi | Q61789 |
OMAi | IRANYWE |
OrthoDBi | 2342at2759 |
TreeFami | TF335359 |
Family and domain databases
Gene3Di | 2.60.120.1490, 1 hit |
InterProi | View protein in InterPro IPR013320, ConA-like_dom_sf IPR000742, EGF-like_dom IPR009254, Laminin_aI IPR010307, Laminin_dom_II IPR002049, Laminin_EGF IPR001791, Laminin_G IPR000034, Laminin_IV IPR008211, Laminin_N IPR038684, Laminin_N_sf |
Pfami | View protein in Pfam PF00052, Laminin_B, 1 hit PF00053, Laminin_EGF, 12 hits PF00054, Laminin_G_1, 1 hit PF02210, Laminin_G_2, 4 hits PF06008, Laminin_I, 1 hit PF06009, Laminin_II, 1 hit PF00055, Laminin_N, 1 hit |
SMARTi | View protein in SMART SM00181, EGF, 8 hits SM00180, EGF_Lam, 14 hits SM00281, LamB, 1 hit SM00282, LamG, 5 hits SM00136, LamNT, 1 hit |
SUPFAMi | SSF49899, SSF49899, 5 hits |
PROSITEi | View protein in PROSITE PS00022, EGF_1, 11 hits PS01186, EGF_2, 1 hit PS01248, EGF_LAM_1, 12 hits PS50027, EGF_LAM_2, 13 hits PS50025, LAM_G_DOMAIN, 5 hits PS51115, LAMININ_IVA, 1 hit PS51117, LAMININ_NTER, 1 hit |
s (2)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MAVALGRAPR SLPLLLTLLL LLLLRMSPSW SVVGQDHPMS SRSLHPPYFN
60 70 80 90 100
LAQAARIWAT ATCGERDPEV SRPRPELFCK LVGGPAAQGS GHTIQGQFCD
110 120 130 140 150
YCNSEDSRKA HPASHAIDGS ERWWQSPPLS SGTQYNQVNL TLDLGQLFHV
160 170 180 190 200
AYILIKFANS PRPDLWILER SVDFGSTYSP WQYFAHSRRD CVEQFGQEAN
210 220 230 240 250
MAITQDDQML CVTEYSRIVP LENGEIVVSL INGRPGAKKF AFSDTLREFT
260 270 280 290 300
KATNIRLRFL RTNTLLGHLI SKAERDPTVT RRYYYSIKDI SVGGRCVCNG
310 320 330 340 350
HAEACSADNP EKQFRCECQH HTCGDTCNRC CAGYNQRRWQ PAGQEQHNEC
360 370 380 390 400
EACNCHGHAV DCYYDPDVEH QQASLNSKGV YAGGGVCINC QHNTAGVNCE
410 420 430 440 450
KCAKGYFRPH GVPVDALHGC IPCSCDPERA DDCDQGSGHC HCKPNFSGDY
460 470 480 490 500
CETCADGYYN FPFCLRIPVF PNYTPSPEDP VAGNIKGCDC NLEGVLPEIC
510 520 530 540 550
DDRGRCLCRP GVEGPQCDSC RSGSYSFPIC QACQCSTIGS YPVPCDPGNG
560 570 580 590 600
QCDCLPGITG RQCDRCLSGA YDFPYCQGSG SVCHPAGTLD SSLGYCQCKQ
610 620 630 640 650
HVASPTCSVC KPLYWNLAKE NPRGCSECQC HEAGTLSGIG ECGQEDGDCS
660 670 680 690 700
CKAHVTGDAC DTCEDGFFSL EKSNYFGCQG CQCDIGGALT TMCSGPSGVC
710 720 730 740 750
QCREHVEGKQ CQRPENNYYF PDLHHMKYEV EDGTGPNGRN LRFGFDPLVF
760 770 780 790 800
PEFSWRGYAP MTSVQNEVRV RLSVRQSSLS LFRIVLRYIS PGTEAISGRI
810 820 830 840 850
TLYSSQGDSD ALQSRKITFP PSKEPAFVTV PGNGFAGPFS ITPGTWIACI
860 870 880 890 900
QVEGVLLDYL VLLPRDYYEA FTLQVPVTEP CAHTGSPQDN CLLYQHLPLT
910 920 930 940 950
AFSCTLACEA RHFLLDGELR PLAMRQPTPT HPAMVDLSGR EVELQLRLRV
960 970 980 990 1000
PQVGHYVVLL EYATEVEQLF VVDVNLKSSG SALAGQVNIY SCKYSIPCRS
1010 1020 1030 1040 1050
VVIDSLSRTA VHELLADADI QLKAHMAHFL LYHICIIPAE EFSTEYLRPQ
1060 1070 1080 1090 1100
VHCIASYRQH ANPSASCVSL AHETPPTASI LDATSRGLFS ALPHEPSSPA
1110 1120 1130 1140 1150
DGVTLKAPQS QVTLKGLIPH LGRHVFVIHF YQAEHPGFPT EVIVNGGRQW
1160 1170 1180 1190 1200
SGSFLASFCP HLLGCRDQVI SDGQVEFDIS EAEVAVTVKI PDGKSLTLVR
1210 1220 1230 1240 1250
VLVVPAENYD YQILHKTTVD KSSEFISSCG GDSFYIDPQA ASGFCKNSAR
1260 1270 1280 1290 1300
SLVAFYHNGA IPCECDPAGT AGHHCSPEGG QCPCRPNVIG RQCSRCATGY
1310 1320 1330 1340 1350
YGFPYCKPCN CGRRLCEEVT GKCLCPPHTV RPQCEVCEMN SFNFHPVAGC
1360 1370 1380 1390 1400
DVCNCSRKGT IEAAVSECDR DSGQCRCKPR VTGQQCDKCA PGFYQFPECV
1410 1420 1430 1440 1450
PCSCNRDGTE PSVCDPETGA CMCKENVEGP QCQLCREGSF YLDPTNPKGC
1460 1470 1480 1490 1500
TKCFCFGVNT DCQSSHKQRA KFVDMMGWRL ETADGVDVPV SFNPGSNSMV
1510 1520 1530 1540 1550
ADLQELPPSV HSASWVAPPS YLGDKVSSYG GYLTYHAKSF GLPGDMVLLG
1560 1570 1580 1590 1600
KQPDVQLTGQ HMSLIHKEPS DPRPDRLHHG RVQVIEGNFR HEGSSAPVSR
1610 1620 1630 1640 1650
EELMTVLSRL ERLHIRGLHF TETQRLTLGE VGLEEASDTG SGPRAHLVEM
1660 1670 1680 1690 1700
CACPPDYTGD SCQGCRPGYY WDNKSLPVGR CVPCNCNGHS NRCQDGSGIC
1710 1720 1730 1740 1750
INCQHNTAGE HCERCQAGHY GNAIHGSCRV CPCPHTNSFA TGCAVDGGAV
1760 1770 1780 1790 1800
RCACKPGYTG TQCERCAPGY FGNPQKFGGS CQPCNCNSNG QLGPCDPLTG
1810 1820 1830 1840 1850
DCVNQEPKDG SPAEECDDCD SCVMTLLNDL ASMGEELRLV KSKLQGLSVS
1860 1870 1880 1890 1900
TGALEQIRHM ETQAKDLRNQ LLGFRSATSS HGSKMDDLEK ELSHLNREFE
1910 1920 1930 1940 1950
TLQEKAQVNS RKAQTLYNNI DQTIQSAKEL DMKIKNIVQN VHILLKQMAR
1960 1970 1980 1990 2000
PGGEGTDLPV GDWSRELAEA QRMMRDLRSR DFKKHLQEAE AEKMEAQLLL
2010 2020 2030 2040 2050
HRIRTWLESH QVENNGLLKN IRDSLNDYED KLQDLRSILQ EAAAQAKQAT
2060 2070 2080 2090 2100
GINHENEGVL GAIQRQMKEM DSLKNDFTKY LATADSSLLQ TNNLLQQMDK
2110 2120 2130 2140 2150
SQKEYESLAA ALNGARQELS DRVRELSRSG GKAPLVVEAE KHAQSLQELA
2160 2170 2180 2190 2200
KQLEEIKRNT SGDELVRCAV DAATAYENIL NAIRAAEDAA SKATSASKSA
2210 2220 2230 2240 2250
FQTVIKEDLP KRAKTLSSDS EELLNEAKMT QKRLQQVSPA LNSLQQTLKT
2260 2270 2280 2290 2300
VSVQKDLLDA NLTVARDDLH GIQRGDIDSV VIGAKSMVRE ANGITSEVLD
2310 2320 2330 2340 2350
GLNPIQTDLG RIKDSYESAR REDFSKALVD ANNSVKKLTR KLPDLFIKIE
2360 2370 2380 2390 2400
SINQQLLPLG NISDNVDRIR ELIQQARDAA NKVAIPMRFN GKSGVEVRLP
2410 2420 2430 2440 2450
NDLEDLKGYT SLSLFLQRPD LRENGGTEDM FVMYLGNKDA SKDYIGMAVV
2460 2470 2480 2490 2500
DGQLTCVYNL GDREAEVQID QVLTESESQE AVMDRVKFQR IYQFAKLNYT
2510 2520 2530 2540 2550
KEATSTKPKA PGVYDMESAS SNTLLNLDPE NAVFYVGGYP PGFELPRRLR
2560 2570 2580 2590 2600
FPPYKGCIEL DDLNENVLSL YNFKTTFNLN TTEVEPCRRR KEESDKNYFE
2610 2620 2630 2640 2650
GTGYARIPTQ PNAPFPNFMQ TIQTTVDRGL LFFAENQDNF ISLNIEDGNL
2660 2670 2680 2690 2700
MVKYKLNSEP PKEKGIRDTI NNGRDHMILI SIGKSQKRML INMNKHSIII
2710 2720 2730 2740 2750
EGEIFDFSTY YLGGIPIAIR ERFNISTPAF QGCMKNLKKT SGVVRLNDTV
2760 2770 2780 2790 2800
GVTKKCSEDW KLVRTASFSR GGQMSFTNLD VPSLDRFQLS FGFQTFQPSG
2810 2820 2830 2840 2850
TLLNHQTRTS SLLVTLEDGH IALSTRDSSS PIFKSPGTYM DGLLHHVSVI
2860 2870 2880 2890 2900
SDTSGLRLLI DDQVLRRNQR LASFSNAQQS LSMGGGYFEG CISNVFVQRM
2910 2920 2930 2940 2950
SQSPEVLDMA SKSTKRDAFL GGCSLNKPPF LMLFKSPKGF NKARSFNVNQ
2960 2970 2980 2990 3000
LLQDAPQAAR SIEAWQDGKS CLPPLNTKAT HRALQFGDSP TSHLLFKLPQ
3010 3020 3030 3040 3050
ELLKPRLQFS LDIQTTSSRG LVFHTGTRDS FVALYLSEGH VIFALGAGGK
3060 3070 3080 3090 3100
KLRLRSKERY HDGKWHSVVF GLSGRKVHLV VDGLRAQEGS LPGNSTISPR
3110 3120 3130 3140 3150
EQVYLGLSPS RKSKSLPQHS FVGCLRNFQL DSKPLDSPSA RSGVSPCLGG
3160 3170 3180 3190 3200
SLEKGIYFSQ GGGHVVLANS VSLEPALTLT LSIRPRSLTG VLIHIASQSG
3210 3220 3230 3240 3250
EHLSVYMEAG KVTTSMNSEA GGTVTSITPK RSLCDGQWHS VTVSIKQHTL
3260 3270 3280 3290 3300
HLELDTDNSY TAGQLSFPPN STRGSLHIGG VPDKLKMLTL PVWNSFFGCL
3310 3320 3330
KNIQVNHIPV PITEATDVQG SVSLNGCPDH
Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 982 | A → R in CAA58837 (PubMed:7665604).Curated | 1 | |
Sequence conflicti | 1150 | W → R in CAA58837 (PubMed:7665604).Curated | 1 | |
Sequence conflicti | 1224 | E → K in CAA58837 (PubMed:7665604).Curated | 1 | |
Sequence conflicti | 1272 | G → GH in CAA58837 (PubMed:7665604).Curated | 1 | |
Sequence conflicti | 1291 | R → S in CAA58837 (PubMed:7665604).Curated | 1 | |
Sequence conflicti | 1398 | E → K in CAA58837 (PubMed:7665604).Curated | 1 | |
Sequence conflicti | 1466 | H → R in CAA58837 (PubMed:7665604).Curated | 1 | |
Sequence conflicti | 1479 | R → V in CAA58837 (PubMed:7665604).Curated | 1 | |
Sequence conflicti | 1488 | V → F in CAA58837 (PubMed:7665604).Curated | 1 | |
Sequence conflicti | 1527 – 1528 | SS → II in CAA58837 (PubMed:7665604).Curated | 2 | |
Sequence conflicti | 1608 | S → P in CAA58837 (PubMed:7665604).Curated | 1 | |
Sequence conflicti | 1983 – 1984 | KK → QN in CAA58836 (PubMed:7665604).Curated | 2 | |
Sequence conflicti | 1983 – 1984 | KK → QN in CAA58837 (PubMed:7665604).Curated | 2 | |
Sequence conflicti | 1983 – 1984 | KK → QN in AAA68091 (PubMed:8012114).Curated | 2 | |
Sequence conflicti | 1987 | Q → G in CAA58836 (PubMed:7665604).Curated | 1 | |
Sequence conflicti | 1987 | Q → G in CAA58837 (PubMed:7665604).Curated | 1 | |
Sequence conflicti | 1987 | Q → G in AAA68091 (PubMed:8012114).Curated | 1 | |
Sequence conflicti | 2463 | R → G in CAA58836 (PubMed:7665604).Curated | 1 | |
Sequence conflicti | 2463 | R → G in CAA58837 (PubMed:7665604).Curated | 1 | |
Sequence conflicti | 2463 | R → G in AAA68091 (PubMed:8012114).Curated | 1 | |
Sequence conflicti | 2488 | F → S in CAA58836 (PubMed:7665604).Curated | 1 | |
Sequence conflicti | 2488 | F → S in CAA58837 (PubMed:7665604).Curated | 1 | |
Sequence conflicti | 2488 | F → S in AAA68091 (PubMed:8012114).Curated | 1 | |
Sequence conflicti | 2617 – 2620 | NFMQ → KLSW in CAA58836 (PubMed:7665604).Curated | 4 | |
Sequence conflicti | 2617 – 2620 | NFMQ → KLSW in CAA58837 (PubMed:7665604).Curated | 4 | |
Sequence conflicti | 2724 – 2725 | NI → PL in CAA58836 (PubMed:7665604).Curated | 2 | |
Sequence conflicti | 2724 – 2725 | NI → PL in CAA58837 (PubMed:7665604).Curated | 2 | |
Sequence conflicti | 3257 | D → Y in CAA58836 (PubMed:7665604).Curated | 1 | |
Sequence conflicti | 3257 | D → Y in CAA58837 (PubMed:7665604).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_003038 | 1 – 1619 | Missing in isoform A. 1 PublicationAdd BLAST | 1619 | |
Alternative sequenceiVSP_003039 | 1620 – 1662 | FTETQ…TGDSC → MLPAVRWSAWSTGWLWIFGA ALGQCLGYGSEQQRVAFLQR PSQNHLQASYMELRPS in isoform A. 1 PublicationAdd BLAST | 43 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X84013 mRNA Translation: CAA58836.1 X84014 mRNA Translation: CAA58837.1 Frameshift. AC102131 Genomic DNA No translation available. AC102248 Genomic DNA No translation available. AC139027 Genomic DNA No translation available. AC157909 Genomic DNA No translation available. AJ293592 mRNA Translation: CAB99254.2 U88353 mRNA Translation: AAC53179.1 L20478 mRNA Translation: AAA68091.1 |
CCDSi | CCDS50222.1 [Q61789-1] CCDS84360.1 [Q61789-2] |
RefSeqi | NP_001334390.1, NM_001347461.1 [Q61789-2] NP_034810.1, NM_010680.1 [Q61789-1] |
Genome annotation databases
Ensembli | ENSMUST00000092070; ENSMUSP00000089703; ENSMUSG00000024421 [Q61789-1] ENSMUST00000188815; ENSMUSP00000140104; ENSMUSG00000024421 [Q61789-2] |
GeneIDi | 16774 |
KEGGi | mmu:16774 |
UCSCi | uc008ecf.2, mouse [Q61789-1] uc008ech.1, mouse [Q61789-2] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X84013 mRNA Translation: CAA58836.1 X84014 mRNA Translation: CAA58837.1 Frameshift. AC102131 Genomic DNA No translation available. AC102248 Genomic DNA No translation available. AC139027 Genomic DNA No translation available. AC157909 Genomic DNA No translation available. AJ293592 mRNA Translation: CAB99254.2 U88353 mRNA Translation: AAC53179.1 L20478 mRNA Translation: AAA68091.1 |
CCDSi | CCDS50222.1 [Q61789-1] CCDS84360.1 [Q61789-2] |
RefSeqi | NP_001334390.1, NM_001347461.1 [Q61789-2] NP_034810.1, NM_010680.1 [Q61789-1] |
3D structure databases
SMRi | Q61789 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 201098, 8 interactors |
ComplexPortali | CPX-3012, Laminin-332 complex variant A [Q61789-2] CPX-3013, Laminin-311 complex variant A [Q61789-2] CPX-3014, Laminin-321 complex [Q61789-2] CPX-3164, Laminin-332 complex variant B [Q61789-1] CPX-3167, Laminin-311 complex variant B [Q61789-1] |
IntActi | Q61789, 1 interactor |
STRINGi | 10090.ENSMUSP00000089703 |
PTM databases
GlyGeni | Q61789, 13 sites |
iPTMneti | Q61789 |
PhosphoSitePlusi | Q61789 |
Proteomic databases
PaxDbi | Q61789 |
PeptideAtlasi | Q61789 |
PRIDEi | Q61789 |
ProteomicsDBi | 264908 [Q61789-1] 264909 [Q61789-2] |
Protocols and materials databases
Antibodypediai | 1948, 192 antibodies |
Genome annotation databases
Ensembli | ENSMUST00000092070; ENSMUSP00000089703; ENSMUSG00000024421 [Q61789-1] ENSMUST00000188815; ENSMUSP00000140104; ENSMUSG00000024421 [Q61789-2] |
GeneIDi | 16774 |
KEGGi | mmu:16774 |
UCSCi | uc008ecf.2, mouse [Q61789-1] uc008ech.1, mouse [Q61789-2] |
Organism-specific databases
CTDi | 3909 |
MGIi | MGI:99909, Lama3 |
Phylogenomic databases
eggNOGi | KOG1836, Eukaryota |
GeneTreei | ENSGT00940000155638 |
HOGENOMi | CLU_000301_1_0_1 |
InParanoidi | Q61789 |
OMAi | IRANYWE |
OrthoDBi | 2342at2759 |
TreeFami | TF335359 |
Enzyme and pathway databases
Reactomei | R-MMU-1474228, Degradation of the extracellular matrix R-MMU-2022090, Assembly of collagen fibrils and other multimeric structures R-MMU-2214320, Anchoring fibril formation R-MMU-3000157, Laminin interactions R-MMU-446107, Type I hemidesmosome assembly R-MMU-8874081, MET activates PTK2 signaling |
Miscellaneous databases
BioGRID-ORCSi | 16774, 1 hit in 53 CRISPR screens |
ChiTaRSi | Lama3, mouse |
PROi | PR:Q61789 |
RNActi | Q61789, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000024421, Expressed in molar tooth and 143 other tissues |
Genevisiblei | Q61789, MM |
Family and domain databases
Gene3Di | 2.60.120.1490, 1 hit |
InterProi | View protein in InterPro IPR013320, ConA-like_dom_sf IPR000742, EGF-like_dom IPR009254, Laminin_aI IPR010307, Laminin_dom_II IPR002049, Laminin_EGF IPR001791, Laminin_G IPR000034, Laminin_IV IPR008211, Laminin_N IPR038684, Laminin_N_sf |
Pfami | View protein in Pfam PF00052, Laminin_B, 1 hit PF00053, Laminin_EGF, 12 hits PF00054, Laminin_G_1, 1 hit PF02210, Laminin_G_2, 4 hits PF06008, Laminin_I, 1 hit PF06009, Laminin_II, 1 hit PF00055, Laminin_N, 1 hit |
SMARTi | View protein in SMART SM00181, EGF, 8 hits SM00180, EGF_Lam, 14 hits SM00281, LamB, 1 hit SM00282, LamG, 5 hits SM00136, LamNT, 1 hit |
SUPFAMi | SSF49899, SSF49899, 5 hits |
PROSITEi | View protein in PROSITE PS00022, EGF_1, 11 hits PS01186, EGF_2, 1 hit PS01248, EGF_LAM_1, 12 hits PS50027, EGF_LAM_2, 13 hits PS50025, LAM_G_DOMAIN, 5 hits PS51115, LAMININ_IVA, 1 hit PS51117, LAMININ_NTER, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | LAMA3_MOUSE | |
Accessioni | Q61789Primary (citable) accession number: Q61789 Secondary accession number(s): E9PUR4 Q9JHQ7 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
Last sequence update: | October 16, 2013 | |
Last modified: | April 7, 2021 | |
This is version 190 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot