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Q61001

- LAMA5_MOUSE

UniProt

Q61001 - LAMA5_MOUSE

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Protein
Laminin subunit alpha-5
Gene
Lama5
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Alpha-5 may be the major laminin alpha chain of adult epithelial and/or endothelial basal laminae.

GO - Molecular functioni

  1. integrin binding Source: MGI
  2. protein binding Source: MGI
Complete GO annotation...

GO - Biological processi

  1. branching involved in salivary gland morphogenesis Source: MGI
  2. branching involved in ureteric bud morphogenesis Source: MGI
  3. branching morphogenesis of an epithelial tube Source: MGI
  4. cilium assembly Source: MGI
  5. establishment of protein localization to plasma membrane Source: MGI
  6. hair follicle development Source: MGI
  7. integrin-mediated signaling pathway Source: Ensembl
  8. lung development Source: MGI
  9. morphogenesis of a polarized epithelium Source: MGI
  10. morphogenesis of embryonic epithelium Source: MGI
  11. muscle organ development Source: MGI
  12. neural crest cell migration Source: MGI
  13. odontogenesis of dentin-containing tooth Source: MGI
  14. organ morphogenesis Source: MGI
  15. regulation of cell adhesion Source: InterPro
  16. regulation of cell migration Source: InterPro
  17. regulation of cell proliferation Source: MGI
  18. regulation of embryonic development Source: InterPro
  19. substrate adhesion-dependent cell spreading Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_199052. Degradation of the extracellular matrix.
REACT_202342. Laminin interactions.

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
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:105382. Lama5.

Subcellular locationi

GO - Cellular componenti

  1. basal lamina Source: MGI
  2. basement membrane Source: MGI
  3. extracellular region Source: Reactome
  4. extracellular space Source: Ensembl
  5. laminin-1 complex Source: InterPro
  6. laminin-10 complex Source: MGI
  7. laminin-5 complex Source: Ensembl
  8. proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 40401 Publication
Add
BLAST
Chaini41 – 37183678Laminin subunit alpha-5
PRO_0000017063Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi100 – 1001N-linked (GlcNAc...) Reviewed prediction
Glycosylationi148 – 1481N-linked (GlcNAc...) Reviewed prediction
Glycosylationi248 – 2481N-linked (GlcNAc...)1 Publication
Disulfide bondi305 ↔ 314 By similarity
Disulfide bondi307 ↔ 327 By similarity
Disulfide bondi329 ↔ 338 By similarity
Disulfide bondi341 ↔ 361 By similarity
Disulfide bondi364 ↔ 373 By similarity
Disulfide bondi366 ↔ 398 By similarity
Glycosylationi383 – 3831N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi401 ↔ 410 By similarity
Disulfide bondi413 ↔ 431 By similarity
Disulfide bondi434 ↔ 445 By similarity
Disulfide bondi436 ↔ 452 By similarity
Disulfide bondi454 ↔ 463 By similarity
Glycosylationi457 – 4571N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi466 ↔ 476 By similarity
Glycosylationi485 – 4851N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi500 ↔ 512 By similarity
Disulfide bondi502 ↔ 521 By similarity
Disulfide bondi523 ↔ 532 By similarity
Disulfide bondi535 ↔ 544 By similarity
Disulfide bondi547 ↔ 559 By similarity
Disulfide bondi549 ↔ 566 By similarity
Disulfide bondi568 ↔ 577 By similarity
Disulfide bondi580 ↔ 590 By similarity
Disulfide bondi593 ↔ 605 By similarity
Disulfide bondi595 ↔ 611 By similarity
Disulfide bondi613 ↔ 622 By similarity
Disulfide bondi625 ↔ 635 By similarity
Disulfide bondi638 ↔ 650 By similarity
Disulfide bondi640 ↔ 656 By similarity
Disulfide bondi658 ↔ 667 By similarity
Disulfide bondi670 ↔ 680 By similarity
Disulfide bondi683 ↔ 695 By similarity
Disulfide bondi685 ↔ 702 By similarity
Disulfide bondi704 ↔ 713 By similarity
Disulfide bondi716 ↔ 731 By similarity
Disulfide bondi752 ↔ 761 By similarity
Disulfide bondi764 ↔ 779 By similarity
Disulfide bondi782 ↔ 796 By similarity
Disulfide bondi784 ↔ 802 By similarity
Disulfide bondi804 ↔ 813 By similarity
Disulfide bondi816 ↔ 831 By similarity
Disulfide bondi834 ↔ 846 By similarity
Disulfide bondi836 ↔ 853 By similarity
Disulfide bondi855 ↔ 864 By similarity
Glycosylationi905 – 9051N-linked (GlcNAc...) Reviewed prediction
Glycosylationi926 – 9261N-linked (GlcNAc...)1 Publication
Glycosylationi964 – 9641N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1335 – 13351N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1443 ↔ 1455 By similarity
Disulfide bondi1445 ↔ 1462 By similarity
Disulfide bondi1464 ↔ 1473 By similarity
Disulfide bondi1476 ↔ 1486 By similarity
Disulfide bondi1489 ↔ 1496 By similarity
Disulfide bondi1491 ↔ 1503 By similarity
Disulfide bondi1505 ↔ 1514 By similarity
Disulfide bondi1517 ↔ 1530 By similarity
Disulfide bondi1533 ↔ 1548 By similarity
Glycosylationi1534 – 15341N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1535 ↔ 1555 By similarity
Disulfide bondi1557 ↔ 1566 By similarity
Disulfide bondi1569 ↔ 1579 By similarity
Disulfide bondi1582 ↔ 1594 By similarity
Disulfide bondi1584 ↔ 1601 By similarity
Disulfide bondi1603 ↔ 1612 By similarity
Disulfide bondi1615 ↔ 1630 By similarity
Disulfide bondi1865 ↔ 1874 By similarity
Disulfide bondi1867 ↔ 1881 By similarity
Disulfide bondi1884 ↔ 1893 By similarity
Disulfide bondi1896 ↔ 1912 By similarity
Disulfide bondi1915 ↔ 1930 By similarity
Disulfide bondi1917 ↔ 1939 By similarity
Disulfide bondi1941 ↔ 1950 By similarity
Disulfide bondi1953 ↔ 1968 By similarity
Disulfide bondi1971 ↔ 1986 By similarity
Disulfide bondi1973 ↔ 1993 By similarity
Disulfide bondi1996 ↔ 2005 By similarity
Disulfide bondi2008 ↔ 2022 By similarity
Glycosylationi2021 – 20211N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2025 ↔ 2035 By similarity
Disulfide bondi2027 ↔ 2042 By similarity
Disulfide bondi2044 ↔ 2053 By similarity
Disulfide bondi2056 ↔ 2069 By similarity
Disulfide bondi2072 ↔ 2083 By similarity
Disulfide bondi2074 ↔ 2090 By similarity
Disulfide bondi2092 ↔ 2101 By similarity
Disulfide bondi2104 ↔ 2116 By similarity
Disulfide bondi2119 ↔ 2126 By similarity
Disulfide bondi2121 ↔ 2133 By similarity
Disulfide bondi2135 ↔ 2144 By similarity
Disulfide bondi2147 ↔ 2166 By similarity
Disulfide bondi2169 – 2169Interchain Inferred
Disulfide bondi2172 – 2172Interchain Inferred
Glycosylationi2198 – 21981N-linked (GlcNAc...)1 Publication
Glycosylationi2211 – 22111N-linked (GlcNAc...)1 Publication
Glycosylationi2365 – 23651N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2395 – 23951N-linked (GlcNAc...)1 Publication
Glycosylationi2425 – 24251N-linked (GlcNAc...)1 Publication
Glycosylationi2503 – 25031N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2570 – 25701N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2709 – 27091N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2903 ↔ 2933 By similarity
Disulfide bondi3094 ↔ 3119 By similarity
Glycosylationi3111 – 31111N-linked (GlcNAc...) Reviewed prediction
Glycosylationi3213 – 32131N-linked (GlcNAc...) Reviewed prediction
Glycosylationi3261 – 32611N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3265 ↔ 3296 By similarity
Glycosylationi3291 – 32911N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3488 ↔ 3511 By similarity
Glycosylationi3623 – 36231N-linked (GlcNAc...)1 Publication
Disulfide bondi3661 ↔ 3689 By similarity
Glycosylationi3673 – 36731N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ61001.
PaxDbiQ61001.
PRIDEiQ61001.

PTM databases

PhosphoSiteiQ61001.

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

ArrayExpressiQ61001.
BgeeiQ61001.
CleanExiMM_LAMA5.
GenevestigatoriQ61001.

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).

Protein-protein interaction databases

BioGridi201100. 1 interaction.
IntActiQ61001. 4 interactions.
MINTiMINT-4997223.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni57 – 604
Beta strandi62 – 676
Helixi122 – 1243
Beta strandi127 – 1304
Beta strandi148 – 16619
Beta strandi173 – 19321
Helixi197 – 2037
Turni206 – 2094
Beta strandi227 – 2293
Beta strandi234 – 24310
Helixi244 – 2463
Helixi249 – 2513
Helixi253 – 2597
Beta strandi260 – 27011
Helixi278 – 2836
Turni286 – 2883
Helixi289 – 2913
Beta strandi295 – 30410
Beta strandi314 – 3174
Beta strandi325 – 3273
Beta strandi333 – 3375
Beta strandi373 – 3753
Helixi377 – 3815
Beta strandi396 – 4005
Beta strandi403 – 4075
Beta strandi430 – 4323

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y38X-ray2.90A44-433[»]
ProteinModelPortaliQ61001.
SMRiQ61001. Positions 47-433.

Miscellaneous databases

EvolutionaryTraceiQ61001.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 304259Laminin N-terminal
Add
BLAST
Domaini305 – 36359Laminin EGF-like 1
Add
BLAST
Domaini364 – 43370Laminin EGF-like 2
Add
BLAST
Domaini434 – 47946Laminin EGF-like 3
Add
BLAST
Domaini500 – 54647Laminin EGF-like 4
Add
BLAST
Domaini547 – 59246Laminin EGF-like 5
Add
BLAST
Domaini593 – 63745Laminin EGF-like 6
Add
BLAST
Domaini638 – 68245Laminin EGF-like 7
Add
BLAST
Domaini683 – 72846Laminin EGF-like 8
Add
BLAST
Domaini729 – 78153Laminin EGF-like 9
Add
BLAST
Domaini782 – 83352Laminin EGF-like 10
Add
BLAST
Domaini834 – 85522Laminin EGF-like 11; truncated
Add
BLAST
Domaini1443 – 148846Laminin EGF-like 12
Add
BLAST
Domaini1489 – 153244Laminin EGF-like 13
Add
BLAST
Domaini1533 – 158149Laminin EGF-like 14
Add
BLAST
Domaini1582 – 163251Laminin EGF-like 15
Add
BLAST
Domaini1633 – 164210Laminin EGF-like 16; first part
Domaini1646 – 1831186Laminin IV type A
Add
BLAST
Domaini1832 – 186433Laminin EGF-like 16; second part
Add
BLAST
Domaini1865 – 191450Laminin EGF-like 17
Add
BLAST
Domaini1915 – 197056Laminin EGF-like 18
Add
BLAST
Domaini1971 – 202454Laminin EGF-like 19
Add
BLAST
Domaini2025 – 207147Laminin EGF-like 20
Add
BLAST
Domaini2072 – 211847Laminin EGF-like 21
Add
BLAST
Domaini2119 – 216850Laminin EGF-like 22
Add
BLAST
Domaini2736 – 2933198Laminin G-like 1
Add
BLAST
Domaini2947 – 3119173Laminin G-like 2
Add
BLAST
Domaini3128 – 3296169Laminin G-like 3
Add
BLAST
Domaini3337 – 3511175Laminin G-like 4
Add
BLAST
Domaini3518 – 3689172Laminin G-like 5
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni856 – 1442587Domain IV 1 (domain IV B)
Add
BLAST
Regioni2169 – 2735567Domain II and I
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili2205 – 225753 Reviewed prediction
Add
BLAST
Coiled coili2330 – 2464135 Reviewed prediction
Add
BLAST
Coiled coili2604 – 262118 Reviewed prediction
Add
BLAST
Coiled coili2639 – 270567 Reviewed prediction
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1723 – 17253Cell attachment site Reviewed prediction
Motifi1839 – 18413Cell attachment site Reviewed prediction

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

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG292643.
GeneTreeiENSGT00750000117549.
HOGENOMiHOG000231235.
HOVERGENiHBG052300.
InParanoidiA2ABW7.
KOiK06240.
OMAiHTTGPRC.
OrthoDBiEOG7DFXB9.
TreeFamiTF335359.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR008985. 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]
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]
SMARTiSM00180. EGF_Lam. 20 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

MAKRGGQLCA GSAPGALGPR SPAPRPLLLL LAGLALVGEA RTPGGDGFSL     50
HPPYFNLAEG ARITASATCG EEAPTRSVSR PTEDLYCKLV GGPVAGGDPN 100
QTIQGQYCDI CTAANSNKAH PVSNAIDGTE RWWQSPPLSR GLEYNEVNVT 150
LDLGQVFHVA YVLIKFANSP RPDLWVLERS TDFGHTYQPW QFFASSKRDC 200
LERFGPRTLE RITQDDDVIC TTEYSRIVPL ENGEIVVSLV NGRPGALNFS 250
YSPLLRDFTK ATNIRLRFLR TNTLLGHLMG KALRDPTVTR RYYYSIKDIS 300
IGGRCVCHGH ADVCDAKDPL DPFRLQCACQ HNTCGGSCDR CCPGFNQQPW 350
KPATTDSANE CQSCNCHGHA YDCYYDPEVD RRNASQNQDN VYQGGGVCLD 400
CQHHTTGINC ERCLPGFFRA PDQPLDSPHV CRPCDCESDF TDGTCEDLTG 450
RCYCRPNFTG ELCAACAEGY TDFPHCYPLP SFPHNDTREQ VLPAGQIVNC 500
DCNAAGTQGN ACRKDPRLGR CVCKPNFRGA HCELCAPGFH GPSCHPCQCS 550
SPGVANSLCD PESGQCMCRT GFEGDRCDHC ALGYFHFPLC QLCGCSPAGT 600
LPEGCDEAGR CQCRPGFDGP HCDRCLPGYH GYPDCHACAC DPRGALDQQC 650
GVGGLCHCRP GYTGATCQEC SPGFYGFPSC IPCHCSADGS LHTTCDPTTG 700
QCRCRPRVTG LHCDMCVPGA YNFPYCEAGS CHPAGLAPAN PALPETQAPC 750
MCRAHVEGPS CDRCKPGYWG LSASNPEGCT RCSCDPRGTL GGVTECQGNG 800
QCFCKAHVCG KTCAACKDGF FGLDYADYFG CRSCRCDVGG ALGQGCEPKT 850
GACRCRPNTQ GPTCSEPAKD HYLPDLHHMR LELEEAATPE GHAVRFGFNP 900
LEFENFSWRG YAHMMAIQPR IVARLNVTSP DLFRLVFRYV NRGSTSVNGQ 950
ISVREEGKLS SCTNCTEQSQ PVAFPPSTEP AFVTVPQRGF GEPFVLNPGI 1000
WALLVEAEGV LLDYVVLLPS TYYEAALLQH RVTEACTYRP SALHSTENCL 1050
VYAHLPLDGF PSAAGTEALC RHDNSLPRPC PTEQLSPSHP PLATCFGSDV 1100
DIQLEMAVPQ PGQYVLVVEY VGEDSHQEMG VAVHTPQRAP QQGVLNLHPC 1150
PYSSLCRSPA RDTQHHLAIF YLDSEASIRL TAEQAHFFLH SVTLVPVEEF 1200
STEFVEPRVF CVSSHGTFNP SSAACLASRF PKPPQPIILK DCQVLPLPPD 1250
LPLTQSQELS PGAPPEGPQP RPPTAVDPNA EPTLLRHPQG TVVFTTQVPT 1300
LGRYAFLLHG YQPVHPSFPV EVLINGGRIW QGHANASFCP HGYGCRTLVL 1350
CEGQTMLDVT DNELTVTVRV PEGRWLWLDY VLIVPEDAYS SSYLQEEPLD 1400
KSYDFISHCA TQGYHISPSS SSPFCRNAAT SLSLFYNNGA LPCGCHEVGA 1450
VSPTCEPFGG QCPCRGHVIG RDCSRCATGY WGFPNCRPCD CGARLCDELT 1500
GQCICPPRTV PPDCLVCQPQ SFGCHPLVGC EECNCSGPGV QELTDPTCDM 1550
DSGQCRCRPN VAGRRCDTCA PGFYGYPSCR PCDCHEAGTM ASVCDPLTGQ 1600
CHCKENVQGS RCDQCRVGTF SLDAANPKGC TRCFCFGATE RCGNSNLARH 1650
EFVDMEGWVL LSSDRQVVPH EHRPEIELLH ADLRSVADTF SELYWQAPPS 1700
YLGDRVSSYG GTLHYELHSE TQRGDIFIPY ESRPDVVLQG NQMSIAFLEL 1750
AYPPPGQVHR GQLQLVEGNF RHLETHNPVS REELMMVLAG LEQLQIRALF 1800
SQTSSSVSLR RVVLEVASEA GRGPPASNVE LCMCPANYRG DSCQECAPGY 1850
YRDTKGLFLG RCVPCQCHGH SDRCLPGSGI CVGCQHNTEG DQCERCRPGF 1900
VSSDPSNPAS PCVSCPCPLA VPSNNFADGC VLRNGRTQCL CRPGYAGASC 1950
ERCAPGFFGN PLVLGSSCQP CDCSGNGDPN MIFSDCDPLT GACRGCLRHT 2000
TGPHCERCAP GFYGNALLPG NCTRCDCSPC GTETCDPQSG RCLCKAGVTG 2050
QRCDRCLEGY FGFEQCQGCR PCACGPAAKG SECHPQSGQC HCQPGTTGPQ 2100
CLECAPGYWG LPEKGCRRCQ CPRGHCDPHT GHCTCPPGLS GERCDTCSQQ 2150
HQVPVPGKPG GHGIHCEVCD HCVVLLLDDL ERAGALLPAI REQLQGINAS 2200
SAAWARLHRL NASIADLQSK LRSPPGPRYQ AAQQLQTLEQ QSISLQQDTE 2250
RLGSQATGVQ GQAGQLLDTT ESTLGRAQKL LESVRAVGRA LNELASRMGQ 2300
GSPGDALVPS GEQLRWALAE VERLLWDMRT RDLGAQGAVA EAELAEAQRL 2350
MARVQEQLTS FWEENQSLAT HIRDQLAQYE SGLMDLREAL NQAVNTTREA 2400
EELNSRNQER LKEALQWKQE LSQDNATLKA TLQAASLILG HVSELLQGID 2450
QAKEDLEHLA ASLDGAWTPL LKRMQAFSPA SSKVDLVEAA EAHAQKLNQL 2500
AINLSGIILG INQDRFIQRA VEASNAYSSI LQAVQAAEDA AGQALRQASR 2550
TWEMVVQRGL AAGARQLLAN SSALEETILG HQGRLGLAQG RLQAAGIQLH 2600
NVWARKNQLA AQIQEAQAML AMDTSETSEK IAHAKAVAAE ALSTATHVQS 2650
QLQGMQKNVE RWQSQLGGLQ GQDLSQVERD ASSSVSTLEK TLPQLLAKLS 2700
RLENRGVHNA SLALSANIGR VRKLIAQARS AASKVKVSMK FNGRSGVRLR 2750
TPRDLADLAA YTALKFHIQS PVPAPEPGKN TGDHFVLYMG SRQATGDYMG 2800
VSLRNQKVHW VYRLGKAGPT TLSIDENIGE QFAAVSIDRT LQFGHMSVTV 2850
EKQMVHEIKG DTVAPGSEGL LNLHPDDFVF YVGGYPSNFT PPEPLRFPGY 2900
LGCIEMETLN EEVVSLYNFE QTFMLDTAVD KPCARSKATG DPWLTDGSYL 2950
DGSGFARISF EKQFSNTKRF DQELRLVSYN GIIFFLKQES QFLCLAVQEG 3000
TLVLFYDFGS GLKKADPLQP PQALTAASKA IQVFLLAGNR KRVLVRVERA 3050
TVFSVDQDNM LEMADAYYLG GVPPEQLPLS LRQLFPSGGS VRGCIKGIKA 3100
LGKYVDLKRL NTTGISFGCT ADLLVGRTMT FHGHGFLPLA LPDVAPITEV 3150
VYSGFGFRGT QDNNLLYYRT SPDGPYQVSL REGHVTLRFM NQEVETQRVF 3200
ADGAPHYVAF YSNVTGVWLY VDDQLQLVKS HERTTPMLQL QPEEPSRLLL 3250
GGLPVSGTFH NFSGCISNVF VQRLRGPQRV FDLHQNMGSV NVSVGCTPAQ 3300
LIETSRATAQ KVSRRSRQPS QDLACTTPWL PGTIQDAYQF GGPLPSYLQF 3350
VGISPSHRNR LHLSMLVRPH AASQGLLLST APMSGRSPSL VLFLNHGHFV 3400
AQTEGPGPRL QVQSRQHSRA GQWHRVSVRW GMQQIQLVVD GSQTWSQKAL 3450
HHRVPRAERP QPYTLSVGGL PASSYSSKLP VSVGFSGCLK KLQLDKRPLR 3500
TPTQMVGVTP CVSGPLEDGL FFPGSEGVVT LELPKAKMPY VSLELEMRPL 3550
AAAGLIFHLG QALATPYMQL KVLTEQVLLQ ANDGAGEFST WVTYPKLCDG 3600
RWHRVAVIMG RDTLRLEVDT QSNHTTGRLP ESLAGSPALL HLGSLPKSST 3650
ARPELPAYRG CLRKLLINGA PVNVTASVQI QGAVGMRGCP SGTLALSKQG 3700
KALTQRQAKP SVSPLLWH 3718
Length:3,718
Mass (Da):404,054
Last modified:July 27, 2011 - v4
Checksum:i18542A9661BA82E9
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti662 – 6621Y → N in AAC53430. 1 Publication
Sequence conflicti1171 – 11711Y → H in AAC53430. 1 Publication
Sequence conflicti2223 – 22231S → R in AAC53430. 1 Publication
Sequence conflicti2411 – 24111L → V in AAC53430. 1 Publication
Sequence conflicti2751 – 27511T → P in AAC53430. 1 Publication
Sequence conflicti3497 – 34971R → Q in AAC53430. 1 Publication
Sequence conflicti3707 – 37071Q → H in AAC53430. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AL663027 Genomic DNA. Translation: CAM16215.1 .
AJ293593 mRNA. Translation: CAB99255.1 .
U37501 mRNA. Translation: AAC53430.1 .
CCDSi CCDS38375.1.
PIRi T10053.
RefSeqi NP_001074640.1. NM_001081171.2.
UniGenei Mm.4339.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2Y38 X-ray 2.90 A 44-433 [» ]
ProteinModelPortali Q61001.
SMRi Q61001. Positions 47-433.
ModBasei Search...

Protein-protein interaction databases

BioGridi 201100. 1 interaction.
IntActi Q61001. 4 interactions.
MINTi MINT-4997223.

PTM databases

PhosphoSitei Q61001.

Proteomic databases

MaxQBi Q61001.
PaxDbi Q61001.
PRIDEi Q61001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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.

Phylogenomic databases

eggNOGi NOG292643.
GeneTreei ENSGT00750000117549.
HOGENOMi HOG000231235.
HOVERGENi HBG052300.
InParanoidi A2ABW7.
KOi K06240.
OMAi HTTGPRC.
OrthoDBi EOG7DFXB9.
TreeFami TF335359.

Enzyme and pathway databases

Reactomei REACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_199052. Degradation of the extracellular matrix.
REACT_202342. Laminin interactions.

Miscellaneous databases

ChiTaRSi LAMA5. mouse.
EvolutionaryTracei Q61001.
NextBioi 290620.
PROi Q61001.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q61001.
Bgeei Q61001.
CleanExi MM_LAMA5.
Genevestigatori Q61001.

Family and domain databases

Gene3Di 2.60.120.200. 5 hits.
InterProi IPR008985. 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 ]
Pfami 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.
[Graphical view ]
SMARTi SM00180. EGF_Lam. 20 hits.
SM00281. LamB. 1 hit.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 5 hits.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.

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: September 3, 2014
This is version 145 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

External Data

Dasty 3

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