UniProtKB - Q61001 (LAMA5_MOUSE)
Laminin subunit alpha-5
Lama5
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. Alpha-5 may be the major laminin alpha chain of adult epithelial and/or endothelial basal laminae.
GO - Molecular functioni
- extracellular matrix structural constituent Source: GO_Central
- integrin binding Source: MGI
GO - Biological processi
- animal organ morphogenesis Source: MGI
- axon guidance Source: GO_Central
- branching involved in salivary gland morphogenesis Source: MGI
- branching involved in ureteric bud morphogenesis Source: MGI
- branching morphogenesis of an epithelial tube Source: MGI
- cell-cell adhesion Source: GO_Central
- cell migration Source: MGI
- cilium assembly Source: MGI
- hair follicle development Source: MGI
- integrin-mediated signaling pathway Source: MGI
- kidney development Source: MGI
- lung development Source: MGI
- morphogenesis of a polarized epithelium Source: MGI
- morphogenesis of embryonic epithelium Source: MGI
- muscle organ development Source: MGI
- neural crest cell migration Source: MGI
- odontogenesis of dentin-containing tooth Source: MGI
- protein localization to plasma membrane Source: MGI
- regulation of cell adhesion Source: InterPro
- regulation of cell migration Source: InterPro
- regulation of cell population proliferation Source: MGI
- regulation of embryonic development Source: InterPro
- substrate adhesion-dependent cell spreading Source: MGI
- tissue development Source: GO_Central
Keywordsi
Biological process | Cell adhesion |
Enzyme and pathway databases
Reactomei | R-MMU-3000157, Laminin interactions R-MMU-8874081, MET activates PTK2 signaling |
Names & Taxonomyi
Protein namesi | Recommended name: Laminin subunit alpha-5Alternative name(s): Laminin-10 subunit alpha Laminin-11 subunit alpha Laminin-15 subunit alpha |
Gene namesi | Name:Lama5 |
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:105382, Lama5 |
VEuPathDBi | HostDB:ENSMUSG00000015647 |
Subcellular locationi
Extracellular region or secreted
Note: Major component.
Extracellular region or secreted
- extracellular region Source: Reactome
- extracellular space Source: MGI
- synaptic cleft Source: SynGO
Other locations
- basement membrane Source: MGI
- collagen-containing extracellular matrix Source: BHF-UCL
- extracellular matrix Source: MGI
- laminin-10 complex Source: MGI
- laminin-5 complex Source: MGI
- neuromuscular junction Source: SynGO
Keywords - Cellular componenti
Basement membrane, Extracellular matrix, SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 40 | 1 PublicationAdd BLAST | 40 | |
ChainiPRO_0000017063 | 41 – 3718 | Laminin subunit alpha-5Add BLAST | 3678 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 100 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 148 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 248 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 305 ↔ 314 | By similarity | ||
Disulfide bondi | 307 ↔ 327 | By similarity | ||
Disulfide bondi | 329 ↔ 338 | By similarity | ||
Disulfide bondi | 341 ↔ 361 | By similarity | ||
Disulfide bondi | 364 ↔ 373 | By similarity | ||
Disulfide bondi | 366 ↔ 398 | By similarity | ||
Glycosylationi | 383 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 401 ↔ 410 | By similarity | ||
Disulfide bondi | 413 ↔ 431 | By similarity | ||
Disulfide bondi | 434 ↔ 445 | By similarity | ||
Disulfide bondi | 436 ↔ 452 | By similarity | ||
Disulfide bondi | 454 ↔ 463 | By similarity | ||
Glycosylationi | 457 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 466 ↔ 476 | By similarity | ||
Glycosylationi | 485 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 500 ↔ 512 | By similarity | ||
Disulfide bondi | 502 ↔ 521 | By similarity | ||
Disulfide bondi | 523 ↔ 532 | By similarity | ||
Disulfide bondi | 535 ↔ 544 | By similarity | ||
Disulfide bondi | 547 ↔ 559 | By similarity | ||
Disulfide bondi | 549 ↔ 566 | By similarity | ||
Disulfide bondi | 568 ↔ 577 | By similarity | ||
Disulfide bondi | 580 ↔ 590 | By similarity | ||
Disulfide bondi | 593 ↔ 605 | By similarity | ||
Disulfide bondi | 595 ↔ 611 | By similarity | ||
Disulfide bondi | 613 ↔ 622 | By similarity | ||
Disulfide bondi | 625 ↔ 635 | By similarity | ||
Disulfide bondi | 638 ↔ 650 | By similarity | ||
Disulfide bondi | 640 ↔ 656 | By similarity | ||
Disulfide bondi | 658 ↔ 667 | By similarity | ||
Disulfide bondi | 670 ↔ 680 | By similarity | ||
Disulfide bondi | 683 ↔ 695 | By similarity | ||
Disulfide bondi | 685 ↔ 702 | By similarity | ||
Disulfide bondi | 704 ↔ 713 | By similarity | ||
Disulfide bondi | 716 ↔ 731 | By similarity | ||
Disulfide bondi | 752 ↔ 761 | By similarity | ||
Disulfide bondi | 764 ↔ 779 | By similarity | ||
Disulfide bondi | 782 ↔ 796 | By similarity | ||
Disulfide bondi | 784 ↔ 802 | By similarity | ||
Disulfide bondi | 804 ↔ 813 | By similarity | ||
Disulfide bondi | 816 ↔ 831 | By similarity | ||
Disulfide bondi | 834 ↔ 846 | By similarity | ||
Disulfide bondi | 836 ↔ 853 | By similarity | ||
Disulfide bondi | 855 ↔ 864 | By similarity | ||
Glycosylationi | 905 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 926 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 964 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1335 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1443 ↔ 1455 | By similarity | ||
Disulfide bondi | 1445 ↔ 1462 | By similarity | ||
Disulfide bondi | 1464 ↔ 1473 | By similarity | ||
Disulfide bondi | 1476 ↔ 1486 | By similarity | ||
Disulfide bondi | 1489 ↔ 1496 | By similarity | ||
Disulfide bondi | 1491 ↔ 1503 | By similarity | ||
Disulfide bondi | 1505 ↔ 1514 | By similarity | ||
Disulfide bondi | 1517 ↔ 1530 | By similarity | ||
Disulfide bondi | 1533 ↔ 1548 | By similarity | ||
Glycosylationi | 1534 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1535 ↔ 1555 | By similarity | ||
Disulfide bondi | 1557 ↔ 1566 | By similarity | ||
Disulfide bondi | 1569 ↔ 1579 | By similarity | ||
Disulfide bondi | 1582 ↔ 1594 | By similarity | ||
Disulfide bondi | 1584 ↔ 1601 | By similarity | ||
Disulfide bondi | 1603 ↔ 1612 | By similarity | ||
Disulfide bondi | 1615 ↔ 1630 | By similarity | ||
Disulfide bondi | 1865 ↔ 1874 | By similarity | ||
Disulfide bondi | 1867 ↔ 1881 | By similarity | ||
Disulfide bondi | 1884 ↔ 1893 | By similarity | ||
Disulfide bondi | 1896 ↔ 1912 | By similarity | ||
Disulfide bondi | 1915 ↔ 1930 | By similarity | ||
Disulfide bondi | 1917 ↔ 1939 | By similarity | ||
Disulfide bondi | 1941 ↔ 1950 | By similarity | ||
Disulfide bondi | 1953 ↔ 1968 | By similarity | ||
Disulfide bondi | 1971 ↔ 1986 | By similarity | ||
Disulfide bondi | 1973 ↔ 1993 | By similarity | ||
Disulfide bondi | 1996 ↔ 2005 | By similarity | ||
Disulfide bondi | 2008 ↔ 2022 | By similarity | ||
Glycosylationi | 2021 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2025 ↔ 2035 | By similarity | ||
Disulfide bondi | 2027 ↔ 2042 | By similarity | ||
Disulfide bondi | 2044 ↔ 2053 | By similarity | ||
Disulfide bondi | 2056 ↔ 2069 | By similarity | ||
Disulfide bondi | 2072 ↔ 2083 | By similarity | ||
Disulfide bondi | 2074 ↔ 2090 | By similarity | ||
Disulfide bondi | 2092 ↔ 2101 | By similarity | ||
Disulfide bondi | 2104 ↔ 2116 | By similarity | ||
Disulfide bondi | 2119 ↔ 2126 | By similarity | ||
Disulfide bondi | 2121 ↔ 2133 | By similarity | ||
Disulfide bondi | 2135 ↔ 2144 | By similarity | ||
Disulfide bondi | 2147 ↔ 2166 | By similarity | ||
Disulfide bondi | 2169 | InterchainCurated | ||
Disulfide bondi | 2172 | InterchainCurated | ||
Glycosylationi | 2198 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 2211 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 2365 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2395 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 2425 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 2503 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2570 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2709 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2903 ↔ 2933 | By similarity | ||
Disulfide bondi | 3094 ↔ 3119 | By similarity | ||
Glycosylationi | 3111 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 3213 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 3261 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 3265 ↔ 3296 | By similarity | ||
Glycosylationi | 3291 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 3488 ↔ 3511 | By similarity | ||
Glycosylationi | 3623 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 3661 ↔ 3689 | By similarity | ||
Glycosylationi | 3673 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
Keywords - PTMi
Disulfide bond, GlycoproteinProteomic databases
EPDi | Q61001 |
jPOSTi | Q61001 |
MaxQBi | Q61001 |
PaxDbi | Q61001 |
PeptideAtlasi | Q61001 |
PRIDEi | Q61001 |
ProteomicsDBi | 264910 |
PTM databases
GlyConnecti | 2458, 7 N-Linked glycans (8 sites) |
GlyGeni | Q61001, 26 sites, 7 N-linked glycans (8 sites) |
iPTMneti | Q61001 |
PhosphoSitePlusi | Q61001 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSMUSG00000015647, Expressed in decidua and 268 other tissues |
Genevisiblei | Q61001, 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-5 is a subunit of laminin-10 (laminin-511), laminin-11 (laminin-521) and laminin-15 (laminin-523).
GO - Molecular functioni
- integrin binding Source: MGI
Protein-protein interaction databases
BioGRIDi | 201100, 15 interactors |
ComplexPortali | CPX-3016, Laminin-511 complex CPX-3017, Laminin-521 complex CPX-3020, Laminin-522 complex CPX-3021, Laminin-523 complex |
IntActi | Q61001, 3 interactors |
MINTi | Q61001 |
STRINGi | 10090.ENSMUSP00000015791 |
Miscellaneous databases
RNActi | Q61001, protein |
Structurei
Secondary structure
3D structure databases
SMRi | Q61001 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q61001 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 46 – 304 | Laminin N-terminalPROSITE-ProRule annotationAdd BLAST | 259 | |
Domaini | 305 – 363 | Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST | 59 | |
Domaini | 364 – 433 | Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST | 70 | |
Domaini | 434 – 479 | Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST | 46 | |
Domaini | 500 – 546 | Laminin EGF-like 4PROSITE-ProRule annotationAdd BLAST | 47 | |
Domaini | 547 – 592 | Laminin EGF-like 5PROSITE-ProRule annotationAdd BLAST | 46 | |
Domaini | 593 – 637 | Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST | 45 | |
Domaini | 638 – 682 | Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST | 45 | |
Domaini | 683 – 728 | Laminin EGF-like 8PROSITE-ProRule annotationAdd BLAST | 46 | |
Domaini | 729 – 781 | Laminin EGF-like 9PROSITE-ProRule annotationAdd BLAST | 53 | |
Domaini | 782 – 833 | Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST | 52 | |
Domaini | 834 – 855 | Laminin EGF-like 11; truncatedPROSITE-ProRule annotationAdd BLAST | 22 | |
Domaini | 1443 – 1488 | Laminin EGF-like 12PROSITE-ProRule annotationAdd BLAST | 46 | |
Domaini | 1489 – 1532 | Laminin EGF-like 13PROSITE-ProRule annotationAdd BLAST | 44 | |
Domaini | 1533 – 1581 | Laminin EGF-like 14PROSITE-ProRule annotationAdd BLAST | 49 | |
Domaini | 1582 – 1632 | Laminin EGF-like 15PROSITE-ProRule annotationAdd BLAST | 51 | |
Domaini | 1633 – 1642 | Laminin EGF-like 16; first partPROSITE-ProRule annotation | 10 | |
Domaini | 1646 – 1831 | Laminin IV type APROSITE-ProRule annotationAdd BLAST | 186 | |
Domaini | 1832 – 1864 | Laminin EGF-like 16; second partPROSITE-ProRule annotationAdd BLAST | 33 | |
Domaini | 1865 – 1914 | Laminin EGF-like 17PROSITE-ProRule annotationAdd BLAST | 50 | |
Domaini | 1915 – 1970 | Laminin EGF-like 18PROSITE-ProRule annotationAdd BLAST | 56 | |
Domaini | 1971 – 2024 | Laminin EGF-like 19PROSITE-ProRule annotationAdd BLAST | 54 | |
Domaini | 2025 – 2071 | Laminin EGF-like 20PROSITE-ProRule annotationAdd BLAST | 47 | |
Domaini | 2072 – 2118 | Laminin EGF-like 21PROSITE-ProRule annotationAdd BLAST | 47 | |
Domaini | 2119 – 2168 | Laminin EGF-like 22PROSITE-ProRule annotationAdd BLAST | 50 | |
Domaini | 2736 – 2933 | Laminin G-like 1PROSITE-ProRule annotationAdd BLAST | 198 | |
Domaini | 2947 – 3119 | Laminin G-like 2PROSITE-ProRule annotationAdd BLAST | 173 | |
Domaini | 3128 – 3296 | Laminin G-like 3PROSITE-ProRule annotationAdd BLAST | 169 | |
Domaini | 3337 – 3511 | Laminin G-like 4PROSITE-ProRule annotationAdd BLAST | 175 | |
Domaini | 3518 – 3689 | Laminin G-like 5PROSITE-ProRule annotationAdd BLAST | 172 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 856 – 1442 | Domain IV 1 (domain IV B)Add BLAST | 587 | |
Regioni | 1253 – 1284 | DisorderedSequence analysisAdd BLAST | 32 | |
Regioni | 2169 – 2735 | Domain II and IAdd BLAST | 567 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 2205 – 2257 | Sequence analysisAdd BLAST | 53 | |
Coiled coili | 2330 – 2464 | Sequence analysisAdd BLAST | 135 | |
Coiled coili | 2604 – 2621 | Sequence analysisAdd BLAST | 18 | |
Coiled coili | 2639 – 2705 | Sequence analysisAdd BLAST | 67 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 1723 – 1725 | Cell attachment siteSequence analysis | 3 | |
Motifi | 1839 – 1841 | Cell attachment siteSequence analysis | 3 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 1263 – 1277 | Pro residuesSequence analysisAdd BLAST | 15 |
Domaini
Keywords - Domaini
Coiled coil, Laminin EGF-like domain, Repeat, SignalPhylogenomic databases
eggNOGi | KOG1836, Eukaryota |
GeneTreei | ENSGT00940000156537 |
HOGENOMi | CLU_000301_1_0_1 |
InParanoidi | Q61001 |
OMAi | RDTYQFG |
OrthoDBi | 2342at2759 |
PhylomeDBi | Q61001 |
TreeFami | TF335359 |
Family and domain databases
CDDi | cd00055, EGF_Lam, 19 hits cd00110, LamG, 5 hits |
InterProi | View protein in InterPro IPR013320, ConA-like_dom_sf IPR000742, EGF-like_dom IPR009254, Laminin_aI IPR010307, Laminin_dom_II IPR001791, Laminin_G IPR000034, Laminin_IV IPR008211, Laminin_N IPR002049, LE_dom |
Pfami | View protein in Pfam PF00052, Laminin_B, 1 hit PF00053, Laminin_EGF, 19 hits PF02210, Laminin_G_2, 5 hits PF06008, Laminin_I, 1 hit PF06009, Laminin_II, 1 hit PF00055, Laminin_N, 1 hit |
SMARTi | View protein in SMART SM00181, EGF, 15 hits SM00180, EGF_Lam, 22 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, 19 hits PS01186, EGF_2, 4 hits PS01248, EGF_LAM_1, 19 hits PS50027, EGF_LAM_2, 21 hits PS50025, LAM_G_DOMAIN, 5 hits PS51115, LAMININ_IVA, 1 hit PS51117, LAMININ_NTER, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MAKRGGQLCA GSAPGALGPR SPAPRPLLLL LAGLALVGEA RTPGGDGFSL
60 70 80 90 100
HPPYFNLAEG ARITASATCG EEAPTRSVSR PTEDLYCKLV GGPVAGGDPN
110 120 130 140 150
QTIQGQYCDI CTAANSNKAH PVSNAIDGTE RWWQSPPLSR GLEYNEVNVT
160 170 180 190 200
LDLGQVFHVA YVLIKFANSP RPDLWVLERS TDFGHTYQPW QFFASSKRDC
210 220 230 240 250
LERFGPRTLE RITQDDDVIC TTEYSRIVPL ENGEIVVSLV NGRPGALNFS
260 270 280 290 300
YSPLLRDFTK ATNIRLRFLR TNTLLGHLMG KALRDPTVTR RYYYSIKDIS
310 320 330 340 350
IGGRCVCHGH ADVCDAKDPL DPFRLQCACQ HNTCGGSCDR CCPGFNQQPW
360 370 380 390 400
KPATTDSANE CQSCNCHGHA YDCYYDPEVD RRNASQNQDN VYQGGGVCLD
410 420 430 440 450
CQHHTTGINC ERCLPGFFRA PDQPLDSPHV CRPCDCESDF TDGTCEDLTG
460 470 480 490 500
RCYCRPNFTG ELCAACAEGY TDFPHCYPLP SFPHNDTREQ VLPAGQIVNC
510 520 530 540 550
DCNAAGTQGN ACRKDPRLGR CVCKPNFRGA HCELCAPGFH GPSCHPCQCS
560 570 580 590 600
SPGVANSLCD PESGQCMCRT GFEGDRCDHC ALGYFHFPLC QLCGCSPAGT
610 620 630 640 650
LPEGCDEAGR CQCRPGFDGP HCDRCLPGYH GYPDCHACAC DPRGALDQQC
660 670 680 690 700
GVGGLCHCRP GYTGATCQEC SPGFYGFPSC IPCHCSADGS LHTTCDPTTG
710 720 730 740 750
QCRCRPRVTG LHCDMCVPGA YNFPYCEAGS CHPAGLAPAN PALPETQAPC
760 770 780 790 800
MCRAHVEGPS CDRCKPGYWG LSASNPEGCT RCSCDPRGTL GGVTECQGNG
810 820 830 840 850
QCFCKAHVCG KTCAACKDGF FGLDYADYFG CRSCRCDVGG ALGQGCEPKT
860 870 880 890 900
GACRCRPNTQ GPTCSEPAKD HYLPDLHHMR LELEEAATPE GHAVRFGFNP
910 920 930 940 950
LEFENFSWRG YAHMMAIQPR IVARLNVTSP DLFRLVFRYV NRGSTSVNGQ
960 970 980 990 1000
ISVREEGKLS SCTNCTEQSQ PVAFPPSTEP AFVTVPQRGF GEPFVLNPGI
1010 1020 1030 1040 1050
WALLVEAEGV LLDYVVLLPS TYYEAALLQH RVTEACTYRP SALHSTENCL
1060 1070 1080 1090 1100
VYAHLPLDGF PSAAGTEALC RHDNSLPRPC PTEQLSPSHP PLATCFGSDV
1110 1120 1130 1140 1150
DIQLEMAVPQ PGQYVLVVEY VGEDSHQEMG VAVHTPQRAP QQGVLNLHPC
1160 1170 1180 1190 1200
PYSSLCRSPA RDTQHHLAIF YLDSEASIRL TAEQAHFFLH SVTLVPVEEF
1210 1220 1230 1240 1250
STEFVEPRVF CVSSHGTFNP SSAACLASRF PKPPQPIILK DCQVLPLPPD
1260 1270 1280 1290 1300
LPLTQSQELS PGAPPEGPQP RPPTAVDPNA EPTLLRHPQG TVVFTTQVPT
1310 1320 1330 1340 1350
LGRYAFLLHG YQPVHPSFPV EVLINGGRIW QGHANASFCP HGYGCRTLVL
1360 1370 1380 1390 1400
CEGQTMLDVT DNELTVTVRV PEGRWLWLDY VLIVPEDAYS SSYLQEEPLD
1410 1420 1430 1440 1450
KSYDFISHCA TQGYHISPSS SSPFCRNAAT SLSLFYNNGA LPCGCHEVGA
1460 1470 1480 1490 1500
VSPTCEPFGG QCPCRGHVIG RDCSRCATGY WGFPNCRPCD CGARLCDELT
1510 1520 1530 1540 1550
GQCICPPRTV PPDCLVCQPQ SFGCHPLVGC EECNCSGPGV QELTDPTCDM
1560 1570 1580 1590 1600
DSGQCRCRPN VAGRRCDTCA PGFYGYPSCR PCDCHEAGTM ASVCDPLTGQ
1610 1620 1630 1640 1650
CHCKENVQGS RCDQCRVGTF SLDAANPKGC TRCFCFGATE RCGNSNLARH
1660 1670 1680 1690 1700
EFVDMEGWVL LSSDRQVVPH EHRPEIELLH ADLRSVADTF SELYWQAPPS
1710 1720 1730 1740 1750
YLGDRVSSYG GTLHYELHSE TQRGDIFIPY ESRPDVVLQG NQMSIAFLEL
1760 1770 1780 1790 1800
AYPPPGQVHR GQLQLVEGNF RHLETHNPVS REELMMVLAG LEQLQIRALF
1810 1820 1830 1840 1850
SQTSSSVSLR RVVLEVASEA GRGPPASNVE LCMCPANYRG DSCQECAPGY
1860 1870 1880 1890 1900
YRDTKGLFLG RCVPCQCHGH SDRCLPGSGI CVGCQHNTEG DQCERCRPGF
1910 1920 1930 1940 1950
VSSDPSNPAS PCVSCPCPLA VPSNNFADGC VLRNGRTQCL CRPGYAGASC
1960 1970 1980 1990 2000
ERCAPGFFGN PLVLGSSCQP CDCSGNGDPN MIFSDCDPLT GACRGCLRHT
2010 2020 2030 2040 2050
TGPHCERCAP GFYGNALLPG NCTRCDCSPC GTETCDPQSG RCLCKAGVTG
2060 2070 2080 2090 2100
QRCDRCLEGY FGFEQCQGCR PCACGPAAKG SECHPQSGQC HCQPGTTGPQ
2110 2120 2130 2140 2150
CLECAPGYWG LPEKGCRRCQ CPRGHCDPHT GHCTCPPGLS GERCDTCSQQ
2160 2170 2180 2190 2200
HQVPVPGKPG GHGIHCEVCD HCVVLLLDDL ERAGALLPAI REQLQGINAS
2210 2220 2230 2240 2250
SAAWARLHRL NASIADLQSK LRSPPGPRYQ AAQQLQTLEQ QSISLQQDTE
2260 2270 2280 2290 2300
RLGSQATGVQ GQAGQLLDTT ESTLGRAQKL LESVRAVGRA LNELASRMGQ
2310 2320 2330 2340 2350
GSPGDALVPS GEQLRWALAE VERLLWDMRT RDLGAQGAVA EAELAEAQRL
2360 2370 2380 2390 2400
MARVQEQLTS FWEENQSLAT HIRDQLAQYE SGLMDLREAL NQAVNTTREA
2410 2420 2430 2440 2450
EELNSRNQER LKEALQWKQE LSQDNATLKA TLQAASLILG HVSELLQGID
2460 2470 2480 2490 2500
QAKEDLEHLA ASLDGAWTPL LKRMQAFSPA SSKVDLVEAA EAHAQKLNQL
2510 2520 2530 2540 2550
AINLSGIILG INQDRFIQRA VEASNAYSSI LQAVQAAEDA AGQALRQASR
2560 2570 2580 2590 2600
TWEMVVQRGL AAGARQLLAN SSALEETILG HQGRLGLAQG RLQAAGIQLH
2610 2620 2630 2640 2650
NVWARKNQLA AQIQEAQAML AMDTSETSEK IAHAKAVAAE ALSTATHVQS
2660 2670 2680 2690 2700
QLQGMQKNVE RWQSQLGGLQ GQDLSQVERD ASSSVSTLEK TLPQLLAKLS
2710 2720 2730 2740 2750
RLENRGVHNA SLALSANIGR VRKLIAQARS AASKVKVSMK FNGRSGVRLR
2760 2770 2780 2790 2800
TPRDLADLAA YTALKFHIQS PVPAPEPGKN TGDHFVLYMG SRQATGDYMG
2810 2820 2830 2840 2850
VSLRNQKVHW VYRLGKAGPT TLSIDENIGE QFAAVSIDRT LQFGHMSVTV
2860 2870 2880 2890 2900
EKQMVHEIKG DTVAPGSEGL LNLHPDDFVF YVGGYPSNFT PPEPLRFPGY
2910 2920 2930 2940 2950
LGCIEMETLN EEVVSLYNFE QTFMLDTAVD KPCARSKATG DPWLTDGSYL
2960 2970 2980 2990 3000
DGSGFARISF EKQFSNTKRF DQELRLVSYN GIIFFLKQES QFLCLAVQEG
3010 3020 3030 3040 3050
TLVLFYDFGS GLKKADPLQP PQALTAASKA IQVFLLAGNR KRVLVRVERA
3060 3070 3080 3090 3100
TVFSVDQDNM LEMADAYYLG GVPPEQLPLS LRQLFPSGGS VRGCIKGIKA
3110 3120 3130 3140 3150
LGKYVDLKRL NTTGISFGCT ADLLVGRTMT FHGHGFLPLA LPDVAPITEV
3160 3170 3180 3190 3200
VYSGFGFRGT QDNNLLYYRT SPDGPYQVSL REGHVTLRFM NQEVETQRVF
3210 3220 3230 3240 3250
ADGAPHYVAF YSNVTGVWLY VDDQLQLVKS HERTTPMLQL QPEEPSRLLL
3260 3270 3280 3290 3300
GGLPVSGTFH NFSGCISNVF VQRLRGPQRV FDLHQNMGSV NVSVGCTPAQ
3310 3320 3330 3340 3350
LIETSRATAQ KVSRRSRQPS QDLACTTPWL PGTIQDAYQF GGPLPSYLQF
3360 3370 3380 3390 3400
VGISPSHRNR LHLSMLVRPH AASQGLLLST APMSGRSPSL VLFLNHGHFV
3410 3420 3430 3440 3450
AQTEGPGPRL QVQSRQHSRA GQWHRVSVRW GMQQIQLVVD GSQTWSQKAL
3460 3470 3480 3490 3500
HHRVPRAERP QPYTLSVGGL PASSYSSKLP VSVGFSGCLK KLQLDKRPLR
3510 3520 3530 3540 3550
TPTQMVGVTP CVSGPLEDGL FFPGSEGVVT LELPKAKMPY VSLELEMRPL
3560 3570 3580 3590 3600
AAAGLIFHLG QALATPYMQL KVLTEQVLLQ ANDGAGEFST WVTYPKLCDG
3610 3620 3630 3640 3650
RWHRVAVIMG RDTLRLEVDT QSNHTTGRLP ESLAGSPALL HLGSLPKSST
3660 3670 3680 3690 3700
ARPELPAYRG CLRKLLINGA PVNVTASVQI QGAVGMRGCP SGTLALSKQG
3710
KALTQRQAKP SVSPLLWH
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 662 | Y → N in AAC53430 (PubMed:7499364).Curated | 1 | |
Sequence conflicti | 1171 | Y → H in AAC53430 (PubMed:7499364).Curated | 1 | |
Sequence conflicti | 2223 | S → R in AAC53430 (PubMed:7499364).Curated | 1 | |
Sequence conflicti | 2411 | L → V in AAC53430 (PubMed:7499364).Curated | 1 | |
Sequence conflicti | 2751 | T → P in AAC53430 (PubMed:7499364).Curated | 1 | |
Sequence conflicti | 3497 | R → Q in AAC53430 (PubMed:7499364).Curated | 1 | |
Sequence conflicti | 3707 | Q → H in AAC53430 (PubMed:7499364).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL663027 Genomic DNA No translation available. AJ293593 mRNA Translation: CAB99255.1 U37501 mRNA Translation: AAC53430.1 |
CCDSi | CCDS38375.1 |
PIRi | T10053 |
RefSeqi | NP_001074640.1, NM_001081171.2 |
Genome annotation databases
Ensembli | ENSMUST00000015791; ENSMUSP00000015791; ENSMUSG00000015647 |
GeneIDi | 16776 |
KEGGi | mmu:16776 |
UCSCi | uc008oip.1, mouse |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL663027 Genomic DNA No translation available. AJ293593 mRNA Translation: CAB99255.1 U37501 mRNA Translation: AAC53430.1 |
CCDSi | CCDS38375.1 |
PIRi | T10053 |
RefSeqi | NP_001074640.1, NM_001081171.2 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2Y38 | X-ray | 2.90 | A | 44-433 | [»] | |
SMRi | Q61001 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 201100, 15 interactors |
ComplexPortali | CPX-3016, Laminin-511 complex CPX-3017, Laminin-521 complex CPX-3020, Laminin-522 complex CPX-3021, Laminin-523 complex |
IntActi | Q61001, 3 interactors |
MINTi | Q61001 |
STRINGi | 10090.ENSMUSP00000015791 |
PTM databases
GlyConnecti | 2458, 7 N-Linked glycans (8 sites) |
GlyGeni | Q61001, 26 sites, 7 N-linked glycans (8 sites) |
iPTMneti | Q61001 |
PhosphoSitePlusi | Q61001 |
Proteomic databases
EPDi | Q61001 |
jPOSTi | Q61001 |
MaxQBi | Q61001 |
PaxDbi | Q61001 |
PeptideAtlasi | Q61001 |
PRIDEi | Q61001 |
ProteomicsDBi | 264910 |
Protocols and materials databases
Antibodypediai | 14779, 300 antibodies from 32 providers |
Genome annotation databases
Ensembli | ENSMUST00000015791; ENSMUSP00000015791; ENSMUSG00000015647 |
GeneIDi | 16776 |
KEGGi | mmu:16776 |
UCSCi | uc008oip.1, mouse |
Organism-specific databases
CTDi | 3911 |
MGIi | MGI:105382, Lama5 |
VEuPathDBi | HostDB:ENSMUSG00000015647 |
Phylogenomic databases
eggNOGi | KOG1836, Eukaryota |
GeneTreei | ENSGT00940000156537 |
HOGENOMi | CLU_000301_1_0_1 |
InParanoidi | Q61001 |
OMAi | RDTYQFG |
OrthoDBi | 2342at2759 |
PhylomeDBi | Q61001 |
TreeFami | TF335359 |
Enzyme and pathway databases
Reactomei | R-MMU-3000157, Laminin interactions R-MMU-8874081, MET activates PTK2 signaling |
Miscellaneous databases
BioGRID-ORCSi | 16776, 3 hits in 73 CRISPR screens |
ChiTaRSi | Lama5, mouse |
EvolutionaryTracei | Q61001 |
PROi | PR:Q61001 |
RNActi | Q61001, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000015647, Expressed in decidua and 268 other tissues |
Genevisiblei | Q61001, MM |
Family and domain databases
CDDi | cd00055, EGF_Lam, 19 hits cd00110, LamG, 5 hits |
InterProi | View protein in InterPro IPR013320, ConA-like_dom_sf IPR000742, EGF-like_dom IPR009254, Laminin_aI IPR010307, Laminin_dom_II IPR001791, Laminin_G IPR000034, Laminin_IV IPR008211, Laminin_N IPR002049, LE_dom |
Pfami | View protein in Pfam PF00052, Laminin_B, 1 hit PF00053, Laminin_EGF, 19 hits PF02210, Laminin_G_2, 5 hits PF06008, Laminin_I, 1 hit PF06009, Laminin_II, 1 hit PF00055, Laminin_N, 1 hit |
SMARTi | View protein in SMART SM00181, EGF, 15 hits SM00180, EGF_Lam, 22 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, 19 hits PS01186, EGF_2, 4 hits PS01248, EGF_LAM_1, 19 hits PS50027, EGF_LAM_2, 21 hits PS50025, LAM_G_DOMAIN, 5 hits PS51115, LAMININ_IVA, 1 hit PS51117, LAMININ_NTER, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | LAMA5_MOUSE | |
Accessioni | Q61001Primary (citable) accession number: Q61001 Secondary accession number(s): A2ABW7, Q9JHQ6 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
Last sequence update: | July 27, 2011 | |
Last modified: | May 25, 2022 | |
This is version 201 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
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references