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Q61001 (LAMA5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Laminin subunit alpha-5
Alternative name(s):
Laminin-10 subunit alpha
Laminin-11 subunit alpha
Laminin-15 subunit alpha
Gene names
Name:Lama5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length3718 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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).

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane. Note: Major component.

Tissue specificity

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.

Domain

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 similarities

Contains 22 laminin EGF-like domains.

Contains 5 laminin G-like domains.

Contains 1 laminin IV type A domain.

Contains 1 laminin N-terminal domain.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentBasement membrane
Extracellular matrix
Secreted
   DomainCoiled coil
Laminin EGF-like domain
Repeat
Signal
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbranching involved in salivary gland morphogenesis

Inferred from mutant phenotype PubMed 14568553. Source: MGI

branching involved in ureteric bud morphogenesis

Inferred from mutant phenotype PubMed 14568553. Source: MGI

branching morphogenesis of an epithelial tube

Inferred from mutant phenotype PubMed 14568553. Source: MGI

cilium assembly

Inferred from mutant phenotype PubMed 16365040. Source: MGI

establishment of protein localization to plasma membrane

Inferred from mutant phenotype PubMed 11507772. Source: MGI

hair follicle development

Inferred from mutant phenotype PubMed 18676816. Source: MGI

integrin-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

lung development

Inferred from mutant phenotype PubMed 12051813. Source: MGI

morphogenesis of a polarized epithelium

Inferred from mutant phenotype PubMed 16365040. Source: MGI

morphogenesis of embryonic epithelium

Inferred from mutant phenotype PubMed 16365040. Source: MGI

muscle organ development

Inferred from mutant phenotype PubMed 12921739. Source: MGI

neural crest cell migration

Inferred from mutant phenotype PubMed 16316641. Source: MGI

odontogenesis of dentin-containing tooth

Inferred from mutant phenotype PubMed 16365040. Source: MGI

organ morphogenesis

Inferred from mutant phenotype PubMed 12743034. Source: MGI

regulation of cell adhesion

Inferred from electronic annotation. Source: InterPro

regulation of cell migration

Inferred from electronic annotation. Source: InterPro

regulation of cell proliferation

Inferred from mutant phenotype PubMed 16365040. Source: MGI

regulation of embryonic development

Inferred from electronic annotation. Source: InterPro

substrate adhesion-dependent cell spreading

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbasal lamina

Inferred from direct assay PubMed 16886065PubMed 9396756. Source: MGI

basement membrane

Inferred from direct assay PubMed 11507772PubMed 12051813PubMed 12743034PubMed 12921739PubMed 14568553PubMed 15895400PubMed 18757743PubMed 19651211PubMed 8707838PubMed 9299121PubMed 9735344. Source: MGI

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from electronic annotation. Source: Ensembl

laminin-1 complex

Inferred from electronic annotation. Source: InterPro

laminin-10 complex

Inferred from physical interaction PubMed 9299121. Source: MGI

laminin-5 complex

Inferred from electronic annotation. Source: Ensembl

proteinaceous extracellular matrix

Inferred from direct assay PubMed 16554364. Source: MGI

   Molecular_functionintegrin binding

Inferred from direct assay PubMed 11741585. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4040 Ref.2
Chain41 – 37183678Laminin subunit alpha-5
PRO_0000017063

Regions

Domain46 – 304259Laminin N-terminal
Domain305 – 36359Laminin EGF-like 1
Domain364 – 43370Laminin EGF-like 2
Domain434 – 47946Laminin EGF-like 3
Domain500 – 54647Laminin EGF-like 4
Domain547 – 59246Laminin EGF-like 5
Domain593 – 63745Laminin EGF-like 6
Domain638 – 68245Laminin EGF-like 7
Domain683 – 72846Laminin EGF-like 8
Domain729 – 78153Laminin EGF-like 9
Domain782 – 83352Laminin EGF-like 10
Domain834 – 85522Laminin EGF-like 11; truncated
Domain1443 – 148846Laminin EGF-like 12
Domain1489 – 153244Laminin EGF-like 13
Domain1533 – 158149Laminin EGF-like 14
Domain1582 – 163251Laminin EGF-like 15
Domain1633 – 164210Laminin EGF-like 16; first part
Domain1646 – 1831186Laminin IV type A
Domain1832 – 186433Laminin EGF-like 16; second part
Domain1865 – 191450Laminin EGF-like 17
Domain1915 – 197056Laminin EGF-like 18
Domain1971 – 202454Laminin EGF-like 19
Domain2025 – 207147Laminin EGF-like 20
Domain2072 – 211847Laminin EGF-like 21
Domain2119 – 216850Laminin EGF-like 22
Domain2736 – 2933198Laminin G-like 1
Domain2947 – 3119173Laminin G-like 2
Domain3128 – 3296169Laminin G-like 3
Domain3337 – 3511175Laminin G-like 4
Domain3518 – 3689172Laminin G-like 5
Region856 – 1442587Domain IV 1 (domain IV B)
Region2169 – 2735567Domain II and I
Coiled coil2205 – 225753 Potential
Coiled coil2330 – 2464135 Potential
Coiled coil2604 – 262118 Potential
Coiled coil2639 – 270567 Potential
Motif1723 – 17253Cell attachment site Potential
Motif1839 – 18413Cell attachment site Potential

Amino acid modifications

Glycosylation1001N-linked (GlcNAc...) Potential
Glycosylation1481N-linked (GlcNAc...) Potential
Glycosylation2481N-linked (GlcNAc...) Ref.5
Glycosylation3831N-linked (GlcNAc...) Potential
Glycosylation4571N-linked (GlcNAc...) Potential
Glycosylation4851N-linked (GlcNAc...) Potential
Glycosylation9051N-linked (GlcNAc...) Potential
Glycosylation9261N-linked (GlcNAc...) Ref.5
Glycosylation9641N-linked (GlcNAc...) Potential
Glycosylation13351N-linked (GlcNAc...) Potential
Glycosylation15341N-linked (GlcNAc...) Potential
Glycosylation20211N-linked (GlcNAc...) Potential
Glycosylation21981N-linked (GlcNAc...) Ref.5
Glycosylation22111N-linked (GlcNAc...) Ref.5
Glycosylation23651N-linked (GlcNAc...) Potential
Glycosylation23951N-linked (GlcNAc...) Ref.5
Glycosylation24251N-linked (GlcNAc...) Ref.5
Glycosylation25031N-linked (GlcNAc...) Potential
Glycosylation25701N-linked (GlcNAc...) Potential
Glycosylation27091N-linked (GlcNAc...) Potential
Glycosylation31111N-linked (GlcNAc...) Potential
Glycosylation32131N-linked (GlcNAc...) Potential
Glycosylation32611N-linked (GlcNAc...) Potential
Glycosylation32911N-linked (GlcNAc...) Potential
Glycosylation36231N-linked (GlcNAc...) Ref.5
Glycosylation36731N-linked (GlcNAc...) Potential
Disulfide bond305 ↔ 314 By similarity
Disulfide bond307 ↔ 327 By similarity
Disulfide bond329 ↔ 338 By similarity
Disulfide bond341 ↔ 361 By similarity
Disulfide bond364 ↔ 373 By similarity
Disulfide bond366 ↔ 398 By similarity
Disulfide bond401 ↔ 410 By similarity
Disulfide bond413 ↔ 431 By similarity
Disulfide bond434 ↔ 445 By similarity
Disulfide bond436 ↔ 452 By similarity
Disulfide bond454 ↔ 463 By similarity
Disulfide bond466 ↔ 476 By similarity
Disulfide bond500 ↔ 512 By similarity
Disulfide bond502 ↔ 521 By similarity
Disulfide bond523 ↔ 532 By similarity
Disulfide bond535 ↔ 544 By similarity
Disulfide bond547 ↔ 559 By similarity
Disulfide bond549 ↔ 566 By similarity
Disulfide bond568 ↔ 577 By similarity
Disulfide bond580 ↔ 590 By similarity
Disulfide bond593 ↔ 605 By similarity
Disulfide bond595 ↔ 611 By similarity
Disulfide bond613 ↔ 622 By similarity
Disulfide bond625 ↔ 635 By similarity
Disulfide bond638 ↔ 650 By similarity
Disulfide bond640 ↔ 656 By similarity
Disulfide bond658 ↔ 667 By similarity
Disulfide bond670 ↔ 680 By similarity
Disulfide bond683 ↔ 695 By similarity
Disulfide bond685 ↔ 702 By similarity
Disulfide bond704 ↔ 713 By similarity
Disulfide bond716 ↔ 731 By similarity
Disulfide bond752 ↔ 761 By similarity
Disulfide bond764 ↔ 779 By similarity
Disulfide bond782 ↔ 796 By similarity
Disulfide bond784 ↔ 802 By similarity
Disulfide bond804 ↔ 813 By similarity
Disulfide bond816 ↔ 831 By similarity
Disulfide bond834 ↔ 846 By similarity
Disulfide bond836 ↔ 853 By similarity
Disulfide bond855 ↔ 864 By similarity
Disulfide bond1443 ↔ 1455 By similarity
Disulfide bond1445 ↔ 1462 By similarity
Disulfide bond1464 ↔ 1473 By similarity
Disulfide bond1476 ↔ 1486 By similarity
Disulfide bond1489 ↔ 1496 By similarity
Disulfide bond1491 ↔ 1503 By similarity
Disulfide bond1505 ↔ 1514 By similarity
Disulfide bond1517 ↔ 1530 By similarity
Disulfide bond1533 ↔ 1548 By similarity
Disulfide bond1535 ↔ 1555 By similarity
Disulfide bond1557 ↔ 1566 By similarity
Disulfide bond1569 ↔ 1579 By similarity
Disulfide bond1582 ↔ 1594 By similarity
Disulfide bond1584 ↔ 1601 By similarity
Disulfide bond1603 ↔ 1612 By similarity
Disulfide bond1615 ↔ 1630 By similarity
Disulfide bond1865 ↔ 1874 By similarity
Disulfide bond1867 ↔ 1881 By similarity
Disulfide bond1884 ↔ 1893 By similarity
Disulfide bond1896 ↔ 1912 By similarity
Disulfide bond1915 ↔ 1930 By similarity
Disulfide bond1917 ↔ 1939 By similarity
Disulfide bond1941 ↔ 1950 By similarity
Disulfide bond1953 ↔ 1968 By similarity
Disulfide bond1971 ↔ 1986 By similarity
Disulfide bond1973 ↔ 1993 By similarity
Disulfide bond1996 ↔ 2005 By similarity
Disulfide bond2008 ↔ 2022 By similarity
Disulfide bond2025 ↔ 2035 By similarity
Disulfide bond2027 ↔ 2042 By similarity
Disulfide bond2044 ↔ 2053 By similarity
Disulfide bond2056 ↔ 2069 By similarity
Disulfide bond2072 ↔ 2083 By similarity
Disulfide bond2074 ↔ 2090 By similarity
Disulfide bond2092 ↔ 2101 By similarity
Disulfide bond2104 ↔ 2116 By similarity
Disulfide bond2119 ↔ 2126 By similarity
Disulfide bond2121 ↔ 2133 By similarity
Disulfide bond2135 ↔ 2144 By similarity
Disulfide bond2147 ↔ 2166 By similarity
Disulfide bond2169Interchain Probable
Disulfide bond2172Interchain Probable
Disulfide bond2903 ↔ 2933 By similarity
Disulfide bond3094 ↔ 3119 By similarity
Disulfide bond3265 ↔ 3296 By similarity
Disulfide bond3488 ↔ 3511 By similarity
Disulfide bond3661 ↔ 3689 By similarity

Experimental info

Sequence conflict6621Y → N in AAC53430. Ref.3
Sequence conflict11711Y → H in AAC53430. Ref.3
Sequence conflict22231S → R in AAC53430. Ref.3
Sequence conflict24111L → V in AAC53430. Ref.3
Sequence conflict27511T → P in AAC53430. Ref.3
Sequence conflict34971R → Q in AAC53430. Ref.3
Sequence conflict37071Q → H in AAC53430. Ref.3

Secondary structure

.................................................. 3718
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q61001 [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: 18542A9661BA82E9

FASTA3,718404,054
        10         20         30         40         50         60 
MAKRGGQLCA GSAPGALGPR SPAPRPLLLL LAGLALVGEA RTPGGDGFSL HPPYFNLAEG 

        70         80         90        100        110        120 
ARITASATCG EEAPTRSVSR PTEDLYCKLV GGPVAGGDPN QTIQGQYCDI CTAANSNKAH 

       130        140        150        160        170        180 
PVSNAIDGTE RWWQSPPLSR GLEYNEVNVT LDLGQVFHVA YVLIKFANSP RPDLWVLERS 

       190        200        210        220        230        240 
TDFGHTYQPW QFFASSKRDC LERFGPRTLE RITQDDDVIC TTEYSRIVPL ENGEIVVSLV 

       250        260        270        280        290        300 
NGRPGALNFS YSPLLRDFTK ATNIRLRFLR TNTLLGHLMG KALRDPTVTR RYYYSIKDIS 

       310        320        330        340        350        360 
IGGRCVCHGH ADVCDAKDPL DPFRLQCACQ HNTCGGSCDR CCPGFNQQPW KPATTDSANE 

       370        380        390        400        410        420 
CQSCNCHGHA YDCYYDPEVD RRNASQNQDN VYQGGGVCLD CQHHTTGINC ERCLPGFFRA 

       430        440        450        460        470        480 
PDQPLDSPHV CRPCDCESDF TDGTCEDLTG RCYCRPNFTG ELCAACAEGY TDFPHCYPLP 

       490        500        510        520        530        540 
SFPHNDTREQ VLPAGQIVNC DCNAAGTQGN ACRKDPRLGR CVCKPNFRGA HCELCAPGFH 

       550        560        570        580        590        600 
GPSCHPCQCS SPGVANSLCD PESGQCMCRT GFEGDRCDHC ALGYFHFPLC QLCGCSPAGT 

       610        620        630        640        650        660 
LPEGCDEAGR CQCRPGFDGP HCDRCLPGYH GYPDCHACAC DPRGALDQQC GVGGLCHCRP 

       670        680        690        700        710        720 
GYTGATCQEC SPGFYGFPSC IPCHCSADGS LHTTCDPTTG QCRCRPRVTG LHCDMCVPGA 

       730        740        750        760        770        780 
YNFPYCEAGS CHPAGLAPAN PALPETQAPC MCRAHVEGPS CDRCKPGYWG LSASNPEGCT 

       790        800        810        820        830        840 
RCSCDPRGTL GGVTECQGNG QCFCKAHVCG KTCAACKDGF FGLDYADYFG CRSCRCDVGG 

       850        860        870        880        890        900 
ALGQGCEPKT GACRCRPNTQ GPTCSEPAKD HYLPDLHHMR LELEEAATPE GHAVRFGFNP 

       910        920        930        940        950        960 
LEFENFSWRG YAHMMAIQPR IVARLNVTSP DLFRLVFRYV NRGSTSVNGQ ISVREEGKLS 

       970        980        990       1000       1010       1020 
SCTNCTEQSQ PVAFPPSTEP AFVTVPQRGF GEPFVLNPGI WALLVEAEGV LLDYVVLLPS 

      1030       1040       1050       1060       1070       1080 
TYYEAALLQH RVTEACTYRP SALHSTENCL VYAHLPLDGF PSAAGTEALC RHDNSLPRPC 

      1090       1100       1110       1120       1130       1140 
PTEQLSPSHP PLATCFGSDV DIQLEMAVPQ PGQYVLVVEY VGEDSHQEMG VAVHTPQRAP 

      1150       1160       1170       1180       1190       1200 
QQGVLNLHPC PYSSLCRSPA RDTQHHLAIF YLDSEASIRL TAEQAHFFLH SVTLVPVEEF 

      1210       1220       1230       1240       1250       1260 
STEFVEPRVF CVSSHGTFNP SSAACLASRF PKPPQPIILK DCQVLPLPPD LPLTQSQELS 

      1270       1280       1290       1300       1310       1320 
PGAPPEGPQP RPPTAVDPNA EPTLLRHPQG TVVFTTQVPT LGRYAFLLHG YQPVHPSFPV 

      1330       1340       1350       1360       1370       1380 
EVLINGGRIW QGHANASFCP HGYGCRTLVL CEGQTMLDVT DNELTVTVRV PEGRWLWLDY 

      1390       1400       1410       1420       1430       1440 
VLIVPEDAYS SSYLQEEPLD KSYDFISHCA TQGYHISPSS SSPFCRNAAT SLSLFYNNGA 

      1450       1460       1470       1480       1490       1500 
LPCGCHEVGA VSPTCEPFGG QCPCRGHVIG RDCSRCATGY WGFPNCRPCD CGARLCDELT 

      1510       1520       1530       1540       1550       1560 
GQCICPPRTV PPDCLVCQPQ SFGCHPLVGC EECNCSGPGV QELTDPTCDM DSGQCRCRPN 

      1570       1580       1590       1600       1610       1620 
VAGRRCDTCA PGFYGYPSCR PCDCHEAGTM ASVCDPLTGQ CHCKENVQGS RCDQCRVGTF 

      1630       1640       1650       1660       1670       1680 
SLDAANPKGC TRCFCFGATE RCGNSNLARH EFVDMEGWVL LSSDRQVVPH EHRPEIELLH 

      1690       1700       1710       1720       1730       1740 
ADLRSVADTF SELYWQAPPS YLGDRVSSYG GTLHYELHSE TQRGDIFIPY ESRPDVVLQG 

      1750       1760       1770       1780       1790       1800 
NQMSIAFLEL AYPPPGQVHR GQLQLVEGNF RHLETHNPVS REELMMVLAG LEQLQIRALF 

      1810       1820       1830       1840       1850       1860 
SQTSSSVSLR RVVLEVASEA GRGPPASNVE LCMCPANYRG DSCQECAPGY YRDTKGLFLG 

      1870       1880       1890       1900       1910       1920 
RCVPCQCHGH SDRCLPGSGI CVGCQHNTEG DQCERCRPGF VSSDPSNPAS PCVSCPCPLA 

      1930       1940       1950       1960       1970       1980 
VPSNNFADGC VLRNGRTQCL CRPGYAGASC ERCAPGFFGN PLVLGSSCQP CDCSGNGDPN 

      1990       2000       2010       2020       2030       2040 
MIFSDCDPLT GACRGCLRHT TGPHCERCAP GFYGNALLPG NCTRCDCSPC GTETCDPQSG 

      2050       2060       2070       2080       2090       2100 
RCLCKAGVTG QRCDRCLEGY FGFEQCQGCR PCACGPAAKG SECHPQSGQC HCQPGTTGPQ 

      2110       2120       2130       2140       2150       2160 
CLECAPGYWG LPEKGCRRCQ CPRGHCDPHT GHCTCPPGLS GERCDTCSQQ HQVPVPGKPG 

      2170       2180       2190       2200       2210       2220 
GHGIHCEVCD HCVVLLLDDL ERAGALLPAI REQLQGINAS SAAWARLHRL NASIADLQSK 

      2230       2240       2250       2260       2270       2280 
LRSPPGPRYQ AAQQLQTLEQ QSISLQQDTE RLGSQATGVQ GQAGQLLDTT ESTLGRAQKL 

      2290       2300       2310       2320       2330       2340 
LESVRAVGRA LNELASRMGQ GSPGDALVPS GEQLRWALAE VERLLWDMRT RDLGAQGAVA 

      2350       2360       2370       2380       2390       2400 
EAELAEAQRL MARVQEQLTS FWEENQSLAT HIRDQLAQYE SGLMDLREAL NQAVNTTREA 

      2410       2420       2430       2440       2450       2460 
EELNSRNQER LKEALQWKQE LSQDNATLKA TLQAASLILG HVSELLQGID QAKEDLEHLA 

      2470       2480       2490       2500       2510       2520 
ASLDGAWTPL LKRMQAFSPA SSKVDLVEAA EAHAQKLNQL AINLSGIILG INQDRFIQRA 

      2530       2540       2550       2560       2570       2580 
VEASNAYSSI LQAVQAAEDA AGQALRQASR TWEMVVQRGL AAGARQLLAN SSALEETILG 

      2590       2600       2610       2620       2630       2640 
HQGRLGLAQG RLQAAGIQLH NVWARKNQLA AQIQEAQAML AMDTSETSEK IAHAKAVAAE 

      2650       2660       2670       2680       2690       2700 
ALSTATHVQS QLQGMQKNVE RWQSQLGGLQ GQDLSQVERD ASSSVSTLEK TLPQLLAKLS 

      2710       2720       2730       2740       2750       2760 
RLENRGVHNA SLALSANIGR VRKLIAQARS AASKVKVSMK FNGRSGVRLR TPRDLADLAA 

      2770       2780       2790       2800       2810       2820 
YTALKFHIQS PVPAPEPGKN TGDHFVLYMG SRQATGDYMG VSLRNQKVHW VYRLGKAGPT 

      2830       2840       2850       2860       2870       2880 
TLSIDENIGE QFAAVSIDRT LQFGHMSVTV EKQMVHEIKG DTVAPGSEGL LNLHPDDFVF 

      2890       2900       2910       2920       2930       2940 
YVGGYPSNFT PPEPLRFPGY LGCIEMETLN EEVVSLYNFE QTFMLDTAVD KPCARSKATG 

      2950       2960       2970       2980       2990       3000 
DPWLTDGSYL DGSGFARISF EKQFSNTKRF DQELRLVSYN GIIFFLKQES QFLCLAVQEG 

      3010       3020       3030       3040       3050       3060 
TLVLFYDFGS GLKKADPLQP PQALTAASKA IQVFLLAGNR KRVLVRVERA TVFSVDQDNM 

      3070       3080       3090       3100       3110       3120 
LEMADAYYLG GVPPEQLPLS LRQLFPSGGS VRGCIKGIKA LGKYVDLKRL NTTGISFGCT 

      3130       3140       3150       3160       3170       3180 
ADLLVGRTMT FHGHGFLPLA LPDVAPITEV VYSGFGFRGT QDNNLLYYRT SPDGPYQVSL 

      3190       3200       3210       3220       3230       3240 
REGHVTLRFM NQEVETQRVF ADGAPHYVAF YSNVTGVWLY VDDQLQLVKS HERTTPMLQL 

      3250       3260       3270       3280       3290       3300 
QPEEPSRLLL GGLPVSGTFH NFSGCISNVF VQRLRGPQRV FDLHQNMGSV NVSVGCTPAQ 

      3310       3320       3330       3340       3350       3360 
LIETSRATAQ KVSRRSRQPS QDLACTTPWL PGTIQDAYQF GGPLPSYLQF VGISPSHRNR 

      3370       3380       3390       3400       3410       3420 
LHLSMLVRPH AASQGLLLST APMSGRSPSL VLFLNHGHFV AQTEGPGPRL QVQSRQHSRA 

      3430       3440       3450       3460       3470       3480 
GQWHRVSVRW GMQQIQLVVD GSQTWSQKAL HHRVPRAERP QPYTLSVGGL PASSYSSKLP 

      3490       3500       3510       3520       3530       3540 
VSVGFSGCLK KLQLDKRPLR TPTQMVGVTP CVSGPLEDGL FFPGSEGVVT LELPKAKMPY 

      3550       3560       3570       3580       3590       3600 
VSLELEMRPL AAAGLIFHLG QALATPYMQL KVLTEQVLLQ ANDGAGEFST WVTYPKLCDG 

      3610       3620       3630       3640       3650       3660 
RWHRVAVIMG RDTLRLEVDT QSNHTTGRLP ESLAGSPALL HLGSLPKSST ARPELPAYRG 

      3670       3680       3690       3700       3710 
CLRKLLINGA PVNVTASVQI QGAVGMRGCP SGTLALSKQG KALTQRQAKP SVSPLLWH 

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"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: NUCLEOTIDE SEQUENCE [MRNA] OF 1-92, PROTEIN SEQUENCE OF 41-46.
[3]"Molecular cloning of a novel laminin chain, alpha 5, and widespread expression in adult mouse tissues."
Miner J.H., Lewis R.M., Sanes J.R.
J. Biol. Chem. 270:28523-28526(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 84-3718.
Strain: C57BL/6 X CBA.
Tissue: Lung.
[4]Miner J.H., Lewis R.M., Sanes J.R.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[5]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-248; ASN-926; ASN-2198; ASN-2211; ASN-2395; ASN-2425 AND ASN-3623.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL663027 Genomic DNA. Translation: CAM16215.1.
AJ293593 mRNA. Translation: CAB99255.1.
U37501 mRNA. Translation: AAC53430.1.
PIRT10053.
RefSeqNP_001074640.1. NM_001081171.2.
UniGeneMm.4339.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y38X-ray2.90A44-433[»]
ProteinModelPortalQ61001.
SMRQ61001. Positions 47-433.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ61001. 4 interactions.
MINTMINT-4997223.

PTM databases

PhosphoSiteQ61001.

Proteomic databases

PaxDbQ61001.
PRIDEQ61001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000015791; ENSMUSP00000015791; ENSMUSG00000015647.
GeneID16776.
KEGGmmu:16776.
UCSCuc008oip.1. mouse.

Organism-specific databases

CTD3911.
MGIMGI:105382. Lama5.

Phylogenomic databases

eggNOGNOG292643.
GeneTreeENSGT00750000117549.
HOGENOMHOG000231235.
HOVERGENHBG052300.
InParanoidA2ABW7.
KOK06240.
OMAHTTGPRC.
OrthoDBEOG7DFXB9.
TreeFamTF335359.

Gene expression databases

ArrayExpressQ61001.
BgeeQ61001.
CleanExMM_LAMA5.
GenevestigatorQ61001.

Family and domain databases

Gene3D2.60.120.200. 5 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
IPR010307. Laminin_II.
IPR008211. Laminin_N.
[Graphical view]
PfamPF00052. 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]
SMARTSM00180. EGF_Lam. 20 hits.
SM00281. LamB. 1 hit.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 5 hits.
PROSITEPS00022. 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]
ProtoNetSearch...

Other

ChiTaRSLAMA5. mouse.
EvolutionaryTraceQ61001.
NextBio290620.
PROQ61001.
SOURCESearch...

Entry information

Entry nameLAMA5_MOUSE
AccessionPrimary (citable) accession number: Q61001
Secondary accession number(s): A2ABW7, Q9JHQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 141 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot