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Protein

Laminin subunit alpha-5

Gene

Lama5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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. Alpha-5 may be the major laminin alpha chain of adult epithelial and/or endothelial basal laminae.

GO - Molecular functioni

  • integrin binding Source: MGI

GO - Biological processi

  • animal organ morphogenesis Source: MGI
  • 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 migration Source: MGI
  • cilium assembly Source: MGI
  • establishment of protein localization to plasma membrane Source: MGI
  • extracellular matrix organization Source: Reactome
  • hair follicle development Source: MGI
  • integrin-mediated signaling pathway 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
  • regulation of cell adhesion Source: InterPro
  • regulation of cell migration Source: InterPro
  • regulation of cell proliferation Source: MGI
  • regulation of embryonic development Source: InterPro
  • substrate adhesion-dependent cell spreading Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-MMU-3000157. Laminin interactions.
R-MMU-3000171. Non-integrin membrane-ECM interactions.
R-MMU-8874081. MET activates PTK2 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit alpha-5
Alternative name(s):
Laminin-10 subunit alpha
Laminin-11 subunit alpha
Laminin-15 subunit alpha
Gene namesi
Name:Lama5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:105382. Lama5.

Subcellular locationi

GO - Cellular componenti

  • basal lamina Source: MGI
  • basement membrane Source: MGI
  • extracellular exosome Source: MGI
  • extracellular matrix Source: MGI
  • extracellular region Source: Reactome
  • extracellular space Source: MGI
  • laminin-10 complex Source: MGI
  • laminin-5 complex Source: Ensembl
  • nucleus Source: MGI
  • proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 401 PublicationAdd BLAST40
ChainiPRO_000001706341 – 3718Laminin subunit alpha-5Add BLAST3678

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi100N-linked (GlcNAc...)Sequence analysis1
Glycosylationi148N-linked (GlcNAc...)Sequence analysis1
Glycosylationi248N-linked (GlcNAc...)1 Publication1
Disulfide bondi305 ↔ 314By similarity
Disulfide bondi307 ↔ 327By similarity
Disulfide bondi329 ↔ 338By similarity
Disulfide bondi341 ↔ 361By similarity
Disulfide bondi364 ↔ 373By similarity
Disulfide bondi366 ↔ 398By similarity
Glycosylationi383N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi401 ↔ 410By similarity
Disulfide bondi413 ↔ 431By similarity
Disulfide bondi434 ↔ 445By similarity
Disulfide bondi436 ↔ 452By similarity
Disulfide bondi454 ↔ 463By similarity
Glycosylationi457N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi466 ↔ 476By similarity
Glycosylationi485N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi500 ↔ 512By similarity
Disulfide bondi502 ↔ 521By similarity
Disulfide bondi523 ↔ 532By similarity
Disulfide bondi535 ↔ 544By similarity
Disulfide bondi547 ↔ 559By similarity
Disulfide bondi549 ↔ 566By similarity
Disulfide bondi568 ↔ 577By similarity
Disulfide bondi580 ↔ 590By similarity
Disulfide bondi593 ↔ 605By similarity
Disulfide bondi595 ↔ 611By similarity
Disulfide bondi613 ↔ 622By similarity
Disulfide bondi625 ↔ 635By similarity
Disulfide bondi638 ↔ 650By similarity
Disulfide bondi640 ↔ 656By similarity
Disulfide bondi658 ↔ 667By similarity
Disulfide bondi670 ↔ 680By similarity
Disulfide bondi683 ↔ 695By similarity
Disulfide bondi685 ↔ 702By similarity
Disulfide bondi704 ↔ 713By similarity
Disulfide bondi716 ↔ 731By similarity
Disulfide bondi752 ↔ 761By similarity
Disulfide bondi764 ↔ 779By similarity
Disulfide bondi782 ↔ 796By similarity
Disulfide bondi784 ↔ 802By similarity
Disulfide bondi804 ↔ 813By similarity
Disulfide bondi816 ↔ 831By similarity
Disulfide bondi834 ↔ 846By similarity
Disulfide bondi836 ↔ 853By similarity
Disulfide bondi855 ↔ 864By similarity
Glycosylationi905N-linked (GlcNAc...)Sequence analysis1
Glycosylationi926N-linked (GlcNAc...)1 Publication1
Glycosylationi964N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1335N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1443 ↔ 1455By similarity
Disulfide bondi1445 ↔ 1462By similarity
Disulfide bondi1464 ↔ 1473By similarity
Disulfide bondi1476 ↔ 1486By similarity
Disulfide bondi1489 ↔ 1496By similarity
Disulfide bondi1491 ↔ 1503By similarity
Disulfide bondi1505 ↔ 1514By similarity
Disulfide bondi1517 ↔ 1530By similarity
Disulfide bondi1533 ↔ 1548By similarity
Glycosylationi1534N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1535 ↔ 1555By similarity
Disulfide bondi1557 ↔ 1566By similarity
Disulfide bondi1569 ↔ 1579By similarity
Disulfide bondi1582 ↔ 1594By similarity
Disulfide bondi1584 ↔ 1601By similarity
Disulfide bondi1603 ↔ 1612By similarity
Disulfide bondi1615 ↔ 1630By similarity
Disulfide bondi1865 ↔ 1874By similarity
Disulfide bondi1867 ↔ 1881By similarity
Disulfide bondi1884 ↔ 1893By similarity
Disulfide bondi1896 ↔ 1912By similarity
Disulfide bondi1915 ↔ 1930By similarity
Disulfide bondi1917 ↔ 1939By similarity
Disulfide bondi1941 ↔ 1950By similarity
Disulfide bondi1953 ↔ 1968By similarity
Disulfide bondi1971 ↔ 1986By similarity
Disulfide bondi1973 ↔ 1993By similarity
Disulfide bondi1996 ↔ 2005By similarity
Disulfide bondi2008 ↔ 2022By similarity
Glycosylationi2021N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2025 ↔ 2035By similarity
Disulfide bondi2027 ↔ 2042By similarity
Disulfide bondi2044 ↔ 2053By similarity
Disulfide bondi2056 ↔ 2069By similarity
Disulfide bondi2072 ↔ 2083By similarity
Disulfide bondi2074 ↔ 2090By similarity
Disulfide bondi2092 ↔ 2101By similarity
Disulfide bondi2104 ↔ 2116By similarity
Disulfide bondi2119 ↔ 2126By similarity
Disulfide bondi2121 ↔ 2133By similarity
Disulfide bondi2135 ↔ 2144By similarity
Disulfide bondi2147 ↔ 2166By similarity
Disulfide bondi2169InterchainCurated
Disulfide bondi2172InterchainCurated
Glycosylationi2198N-linked (GlcNAc...)1 Publication1
Glycosylationi2211N-linked (GlcNAc...)1 Publication1
Glycosylationi2365N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2395N-linked (GlcNAc...)1 Publication1
Glycosylationi2425N-linked (GlcNAc...)1 Publication1
Glycosylationi2503N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2570N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2709N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2903 ↔ 2933By similarity
Disulfide bondi3094 ↔ 3119By similarity
Glycosylationi3111N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3213N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3261N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3265 ↔ 3296By similarity
Glycosylationi3291N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3488 ↔ 3511By similarity
Glycosylationi3623N-linked (GlcNAc...)1 Publication1
Disulfide bondi3661 ↔ 3689By similarity
Glycosylationi3673N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ61001.
PaxDbiQ61001.
PeptideAtlasiQ61001.
PRIDEiQ61001.

PTM databases

iPTMnetiQ61001.
PhosphoSitePlusiQ61001.

Expressioni

Tissue specificityi

In adult, high levels in heart, lung, and kidney; lower in brain, muscle and testis; very low in liver, gut and skin. Expressed in many tissues in embryonic day 11.

Gene expression databases

BgeeiENSMUSG00000015647.
CleanExiMM_LAMA5.
GenevisibleiQ61001. 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

BioGridi201100. 1 interactor.
IntActiQ61001. 4 interactors.
MINTiMINT-4997223.
STRINGi10090.ENSMUSP00000015791.

Structurei

Secondary structure

13718
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni57 – 60Combined sources4
Beta strandi62 – 67Combined sources6
Helixi122 – 124Combined sources3
Beta strandi127 – 130Combined sources4
Beta strandi148 – 166Combined sources19
Beta strandi173 – 193Combined sources21
Helixi197 – 203Combined sources7
Turni206 – 209Combined sources4
Beta strandi227 – 229Combined sources3
Beta strandi234 – 243Combined sources10
Helixi244 – 246Combined sources3
Helixi249 – 251Combined sources3
Helixi253 – 259Combined sources7
Beta strandi260 – 270Combined sources11
Helixi278 – 283Combined sources6
Turni286 – 288Combined sources3
Helixi289 – 291Combined sources3
Beta strandi295 – 304Combined sources10
Beta strandi314 – 317Combined sources4
Beta strandi325 – 327Combined sources3
Beta strandi333 – 337Combined sources5
Beta strandi373 – 375Combined sources3
Helixi377 – 381Combined sources5
Beta strandi396 – 400Combined sources5
Beta strandi403 – 407Combined sources5
Beta strandi430 – 432Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Y38X-ray2.90A44-433[»]
ProteinModelPortaliQ61001.
SMRiQ61001.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ61001.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini46 – 304Laminin N-terminalPROSITE-ProRule annotationAdd BLAST259
Domaini305 – 363Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST59
Domaini364 – 433Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST70
Domaini434 – 479Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST46
Domaini500 – 546Laminin EGF-like 4PROSITE-ProRule annotationAdd BLAST47
Domaini547 – 592Laminin EGF-like 5PROSITE-ProRule annotationAdd BLAST46
Domaini593 – 637Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST45
Domaini638 – 682Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST45
Domaini683 – 728Laminin EGF-like 8PROSITE-ProRule annotationAdd BLAST46
Domaini729 – 781Laminin EGF-like 9PROSITE-ProRule annotationAdd BLAST53
Domaini782 – 833Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST52
Domaini834 – 855Laminin EGF-like 11; truncatedPROSITE-ProRule annotationAdd BLAST22
Domaini1443 – 1488Laminin EGF-like 12PROSITE-ProRule annotationAdd BLAST46
Domaini1489 – 1532Laminin EGF-like 13PROSITE-ProRule annotationAdd BLAST44
Domaini1533 – 1581Laminin EGF-like 14PROSITE-ProRule annotationAdd BLAST49
Domaini1582 – 1632Laminin EGF-like 15PROSITE-ProRule annotationAdd BLAST51
Domaini1633 – 1642Laminin EGF-like 16; first partPROSITE-ProRule annotation10
Domaini1646 – 1831Laminin IV type APROSITE-ProRule annotationAdd BLAST186
Domaini1832 – 1864Laminin EGF-like 16; second partPROSITE-ProRule annotationAdd BLAST33
Domaini1865 – 1914Laminin EGF-like 17PROSITE-ProRule annotationAdd BLAST50
Domaini1915 – 1970Laminin EGF-like 18PROSITE-ProRule annotationAdd BLAST56
Domaini1971 – 2024Laminin EGF-like 19PROSITE-ProRule annotationAdd BLAST54
Domaini2025 – 2071Laminin EGF-like 20PROSITE-ProRule annotationAdd BLAST47
Domaini2072 – 2118Laminin EGF-like 21PROSITE-ProRule annotationAdd BLAST47
Domaini2119 – 2168Laminin EGF-like 22PROSITE-ProRule annotationAdd BLAST50
Domaini2736 – 2933Laminin G-like 1PROSITE-ProRule annotationAdd BLAST198
Domaini2947 – 3119Laminin G-like 2PROSITE-ProRule annotationAdd BLAST173
Domaini3128 – 3296Laminin G-like 3PROSITE-ProRule annotationAdd BLAST169
Domaini3337 – 3511Laminin G-like 4PROSITE-ProRule annotationAdd BLAST175
Domaini3518 – 3689Laminin G-like 5PROSITE-ProRule annotationAdd BLAST172

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni856 – 1442Domain IV 1 (domain IV B)Add BLAST587
Regioni2169 – 2735Domain II and IAdd BLAST567

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili2205 – 2257Sequence analysisAdd BLAST53
Coiled coili2330 – 2464Sequence analysisAdd BLAST135
Coiled coili2604 – 2621Sequence analysisAdd BLAST18
Coiled coili2639 – 2705Sequence analysisAdd BLAST67

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1723 – 1725Cell attachment siteSequence analysis3
Motifi1839 – 1841Cell attachment siteSequence analysis3

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 22 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 5 laminin G-like domains.PROSITE-ProRule annotation
Contains 1 laminin IV type A domain.PROSITE-ProRule annotation
Contains 1 laminin N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Laminin EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiKOG1836. Eukaryota.
ENOG410XRDC. LUCA.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000231235.
HOVERGENiHBG052300.
InParanoidiQ61001.
KOiK06240.
OMAiHTTGPRC.
OrthoDBiEOG091G005L.
TreeFamiTF335359.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR013320. ConA-like_dom.
IPR000742. EGF-like_dom.
IPR009254. Laminin_aI.
IPR010307. Laminin_domII.
IPR002049. Laminin_EGF.
IPR001791. Laminin_G.
IPR000034. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. 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.
[Graphical view]
SMARTiSM00181. EGF. 15 hits.
SM00180. EGF_Lam. 22 hits.
SM00281. LamB. 1 hit.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 5 hits.
PROSITEiPS00022. 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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q61001-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:3,718
Mass (Da):404,054
Last modified:July 27, 2011 - v4
Checksum:i18542A9661BA82E9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti662Y → N in AAC53430 (PubMed:7499364).Curated1
Sequence conflicti1171Y → H in AAC53430 (PubMed:7499364).Curated1
Sequence conflicti2223S → R in AAC53430 (PubMed:7499364).Curated1
Sequence conflicti2411L → V in AAC53430 (PubMed:7499364).Curated1
Sequence conflicti2751T → P in AAC53430 (PubMed:7499364).Curated1
Sequence conflicti3497R → Q in AAC53430 (PubMed:7499364).Curated1
Sequence conflicti3707Q → H in AAC53430 (PubMed:7499364).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL663027 Genomic DNA. Translation: CAM16215.1.
AJ293593 mRNA. Translation: CAB99255.1.
U37501 mRNA. Translation: AAC53430.1.
CCDSiCCDS38375.1.
PIRiT10053.
RefSeqiNP_001074640.1. NM_001081171.2.
UniGeneiMm.4339.

Genome annotation databases

EnsembliENSMUST00000015791; ENSMUSP00000015791; ENSMUSG00000015647.
GeneIDi16776.
KEGGimmu:16776.
UCSCiuc008oip.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL663027 Genomic DNA. Translation: CAM16215.1.
AJ293593 mRNA. Translation: CAB99255.1.
U37501 mRNA. Translation: AAC53430.1.
CCDSiCCDS38375.1.
PIRiT10053.
RefSeqiNP_001074640.1. NM_001081171.2.
UniGeneiMm.4339.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Y38X-ray2.90A44-433[»]
ProteinModelPortaliQ61001.
SMRiQ61001.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201100. 1 interactor.
IntActiQ61001. 4 interactors.
MINTiMINT-4997223.
STRINGi10090.ENSMUSP00000015791.

PTM databases

iPTMnetiQ61001.
PhosphoSitePlusiQ61001.

Proteomic databases

MaxQBiQ61001.
PaxDbiQ61001.
PeptideAtlasiQ61001.
PRIDEiQ61001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000015791; ENSMUSP00000015791; ENSMUSG00000015647.
GeneIDi16776.
KEGGimmu:16776.
UCSCiuc008oip.1. mouse.

Organism-specific databases

CTDi3911.
MGIiMGI:105382. Lama5.

Phylogenomic databases

eggNOGiKOG1836. Eukaryota.
ENOG410XRDC. LUCA.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000231235.
HOVERGENiHBG052300.
InParanoidiQ61001.
KOiK06240.
OMAiHTTGPRC.
OrthoDBiEOG091G005L.
TreeFamiTF335359.

Enzyme and pathway databases

ReactomeiR-MMU-3000157. Laminin interactions.
R-MMU-3000171. Non-integrin membrane-ECM interactions.
R-MMU-8874081. MET activates PTK2 signaling.

Miscellaneous databases

ChiTaRSiLama5. mouse.
EvolutionaryTraceiQ61001.
PROiQ61001.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000015647.
CleanExiMM_LAMA5.
GenevisibleiQ61001. MM.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR013320. ConA-like_dom.
IPR000742. EGF-like_dom.
IPR009254. Laminin_aI.
IPR010307. Laminin_domII.
IPR002049. Laminin_EGF.
IPR001791. Laminin_G.
IPR000034. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. 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.
[Graphical view]
SMARTiSM00181. EGF. 15 hits.
SM00180. EGF_Lam. 22 hits.
SM00281. LamB. 1 hit.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 5 hits.
PROSITEiPS00022. 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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLAMA5_MOUSE
AccessioniPrimary (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: November 30, 2016
This is version 165 of the entry and version 4 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.