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Protein

Laminin subunit alpha-4

Gene

Lama4

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.

GO - Biological processi

  • blood vessel development Source: MGI
  • brown fat cell differentiation Source: MGI
  • cell adhesion Source: UniProtKB-KW
  • extracellular matrix organization Source: Reactome
  • regulation of cell adhesion Source: InterPro
  • regulation of cell migration Source: InterPro
  • regulation of embryonic development Source: InterPro
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-4
Alternative name(s):
Laminin-14 subunit alpha
Laminin-8 subunit alpha
Laminin-9 subunit alpha
Gene namesi
Name:Lama4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:109321. Lama4.

Subcellular locationi

GO - Cellular componenti

  • basal lamina Source: MGI
  • basement membrane Source: MGI
  • extracellular exosome Source: MGI
  • extracellular region Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
ChainiPRO_000001706125 – 1816Laminin subunit alpha-4Add BLAST1792

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi82 ↔ 91By similarity
Disulfide bondi84 ↔ 98By similarity
Disulfide bondi101 ↔ 110By similarity
Glycosylationi104N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi113 ↔ 129By similarity
Disulfide bondi132 ↔ 146By similarity
Disulfide bondi134 ↔ 155By similarity
Disulfide bondi157 ↔ 166By similarity
Disulfide bondi169 ↔ 184By similarity
Disulfide bondi187 ↔ 202By similarity
Disulfide bondi189 ↔ 209By similarity
Disulfide bondi212 ↔ 221By similarity
Glycosylationi215N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi224 ↔ 238By similarity
Disulfide bondi266InterchainCurated
Disulfide bondi269InterchainCurated
Glycosylationi308N-linked (GlcNAc...)Sequence analysis1
Glycosylationi333N-linked (GlcNAc...)Sequence analysis1
Glycosylationi458N-linked (GlcNAc...)Sequence analysis1
Glycosylationi550N-linked (GlcNAc...)Sequence analysis1
Glycosylationi571N-linked (GlcNAc...)Sequence analysis1
Glycosylationi574N-linked (GlcNAc...)Sequence analysis1
Glycosylationi631N-linked (GlcNAc...)Sequence analysis1
Glycosylationi639N-linked (GlcNAc...)Sequence analysis1
Glycosylationi735N-linked (GlcNAc...)Sequence analysis1
Glycosylationi751N-linked (GlcNAc...)Sequence analysis1
Glycosylationi754N-linked (GlcNAc...)Sequence analysis1
Glycosylationi780N-linked (GlcNAc...)Sequence analysis1
Glycosylationi803N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1000 ↔ 1030By similarity
Glycosylationi1088N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1196 ↔ 1222By similarity
Glycosylationi1283N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1361N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1365 ↔ 1397By similarity
Disulfide bondi1610 ↔ 1633By similarity
Disulfide bondi1785 ↔ 1813By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP97927.
PaxDbiP97927.
PeptideAtlasiP97927.
PRIDEiP97927.

PTM databases

PhosphoSitePlusiP97927.

Expressioni

Tissue specificityi

Strongly expressed in peripheral nerves, cardiac muscle, fat, dermis, lung stroma, aortic endothelium, endocardium and endothelium of blood vessels in skin and brain.

Gene expression databases

BgeeiENSMUSG00000019846.
CleanExiMM_LAMA4.
GenevisibleiP97927. 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-4 is a subunit of laminin-8 (laminin-411), laminin-9 (laminin-421) and laminin-14 (laminin-423).

Protein-protein interaction databases

IntActiP97927. 1 interactor.
MINTiMINT-4100077.
STRINGi10090.ENSMUSP00000019992.

Structurei

3D structure databases

ProteinModelPortaliP97927.
SMRiP97927.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini82 – 131Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST50
Domaini132 – 186Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST55
Domaini187 – 240Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST54
Domaini241 – 255Laminin EGF-like 4; truncatedPROSITE-ProRule annotationAdd BLAST15
Domaini826 – 1030Laminin G-like 1PROSITE-ProRule annotationAdd BLAST205
Domaini1042 – 1222Laminin G-like 2PROSITE-ProRule annotationAdd BLAST181
Domaini1229 – 1397Laminin G-like 3PROSITE-ProRule annotationAdd BLAST169
Domaini1462 – 1633Laminin G-like 4PROSITE-ProRule annotationAdd BLAST172
Domaini1640 – 1813Laminin G-like 5PROSITE-ProRule annotationAdd BLAST174

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni256 – 825Domain II and IAdd BLAST570

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili431 – 523Sequence analysisAdd BLAST93
Coiled coili556 – 604Sequence analysisAdd BLAST49
Coiled coili655 – 717Sequence analysisAdd BLAST63
Coiled coili770 – 799Sequence analysisAdd BLAST30

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi717 – 719Cell 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.
Domain G is globular.

Sequence similaritiesi

Contains 4 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 5 laminin G-like domains.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiENOG410KCXD. Eukaryota.
ENOG410Z3D5. LUCA.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000113278.
HOVERGENiHBG052299.
InParanoidiP97927.
KOiK06241.
OMAiQVSMMFD.
OrthoDBiEOG091G005L.
PhylomeDBiP97927.
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.
[Graphical view]
PfamiPF00053. Laminin_EGF. 3 hits.
PF02210. Laminin_G_2. 5 hits.
PF06008. Laminin_I. 1 hit.
PF06009. Laminin_II. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 3 hits.
SM00180. EGF_Lam. 3 hits.
SM00282. LamG. 5 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 6 hits.
PROSITEiPS00022. EGF_1. 1 hit.
PS01248. EGF_LAM_1. 3 hits.
PS50027. EGF_LAM_2. 3 hits.
PS50025. LAM_G_DOMAIN. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P97927-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGWSTAWCSV LALWLLWCAV CSNAASGDGN AFPFDIEGSA VVGRQDPSET
60 70 80 90 100
SDSGVTLGRL PPAAERCDAG FFRTLSGECA PCDCNGNSHE CLDGSGFCLH
110 120 130 140 150
CQRNTTGEHC EKCLDGYIGD SIRGTPRFCQ PCPCPLPHLA NFAESCYRKN
160 170 180 190 200
GAVRCICKEN YVGPNCERCA PGYYGNPLLI GSTCKKCDCS GNSDPNLIFE
210 220 230 240 250
DCDEITGQCR NCLRNTTGFK CERCAPGYYG DARTAKNCAV CNCGGGPCDS
260 270 280 290 300
VTGECLEEGF EVPTGCDKCV WDLTDDLRLA ALSIEESKSG LLSVSSGAAA
310 320 330 340 350
HRHVTDMNST IHLLRTRLSE RENQYTLRKI QINNSENTLR SLLPDVEGLH
360 370 380 390 400
EKGSQASRKG MLVEKESMDT IDQATHLVEQ AHNMRDKIQE INSKMLYYGE
410 420 430 440 450
NQELGPEEIA EKLVLAQKML EEIRSRQPFL THRELVDEEA DEAQELLSQA
460 470 480 490 500
ENWQRLHNDT RSLFPVVLEQ LDDYNAKLSD LQESINQALD HVRDAEDMNR
510 520 530 540 550
AITFKQRDHE KQHERVKEQM EVVGASLSMS ADSLTIPQLT LEELDEIIKN
560 570 580 590 600
ASGIYAEIDG AKNELQGKLS NLSNLSHDLV QEATDHAYNL QQEADELSRN
610 620 630 640 650
LHSSDMNGLV QKALDASNVY ENIANYVSEA NETAELALNI TDRIYDAVSG
660 670 680 690 700
IDTQIIYHKD ESDNLLNQAR ELQAKADSSN DEAVADTSRR VGGALWRKGA
710 720 730 740 750
LRDRLNDAVK QLQAAERGDA HQRLGQSKLF IEEANKTTAA VQQVTTPMAN
760 770 780 790 800
NLSNWSQNLQ TFDSSAYNTA VDSARDAVRN LTEVVPQLLD QLRTVEQKRP
810 820 830 840 850
ASNISASIQR IRELIAQTRS VASKIQVSMM FDGQSAVEVH PKVSVDDLKA
860 870 880 890 900
FTSISLYMKP PPKPAEPTGA WVADQFVLYL GSKNAKKEYM GLAIKNDNLV
910 920 930 940 950
YVYNLGMKDV EILLDSKPVS SWPAYFSIVK IERVGKHGKV FLTVPSLSST
960 970 980 990 1000
AEEKFIKKGE FAGDDSLLDL TPEDTVFYVG GVPANFKLPA SLNLPSYSGC
1010 1020 1030 1040 1050
LELATLNNDV ISLYNFKHIY NMDPSKSVPC ARDKLAFTQS RAASYFFDGS
1060 1070 1080 1090 1100
SYAVVRDITR RGKFGQVTRF DIEIRTPADN GLVLLMVNGS MFFSLEMRNG
1110 1120 1130 1140 1150
YLHVFYDFGF SNGPVHLEDT LKKAQINDAK YHEISIIYHN DKKMILVVDR
1160 1170 1180 1190 1200
RHVKSTDNEK KKIPFTDIYI GGAPQEVLQS RTLRAHLPLD INFRGCMKGF
1210 1220 1230 1240 1250
QFQKKDFNLL EQTETLGVGY GCPEDSLISR RAYFNGQSFI ASIQKISFFD
1260 1270 1280 1290 1300
GFEGGFNFRT LQPNGLLFYY TSGSDVFSIS LDNGTVVMDV KGIKVMSTDK
1310 1320 1330 1340 1350
QYHDGLPHFV VTSISDTRYE LVVDKSRLRG KNPTKGKAEQ TQTTEKKFYF
1360 1370 1380 1390 1400
GGSPISPQYA NFTGCISNAY FTRLDRDVEV EDFQRYSEKV HTSLYECPIE
1410 1420 1430 1440 1450
SSPLFLLHKK GKNSSKPKTN KQGEKSKDAP SWDPIGLKFL EQKAPRDSHC
1460 1470 1480 1490 1500
HLSSSPRAIE HAYQYGGTAN SRQEFEHEQG DFGEKSQFAI RLKTRSSHGM
1510 1520 1530 1540 1550
IFYVSDQEEN DFMTLFLAHG RLVFMFNVGH KKLKIRSQEK YNDGLWHDVI
1560 1570 1580 1590 1600
FIREKSSGRL VIDGLRVLEE RLPPSGAAWK IKGPIYLGGV APGRAVKNVQ
1610 1620 1630 1640 1650
ITSVYSFSGC LGNLQLNGAS ITSASQTFSV TPCFEGPMET GTYFSTEGGY
1660 1670 1680 1690 1700
VVLDESFNIG LKFEIAFEVR PRSSSGTLVH GHSVNGEYLN VHMRNGQVIV
1710 1720 1730 1740 1750
KVNNGVRDFS TSVTPKQNLC DGRWHRITVI RDSNVVQLDV DSEVNHVVGP
1760 1770 1780 1790 1800
LNPKPVDHRE PVFVGGVPES LLTPRLAPSK PFTGCIRHFV IDSRPVSFSK
1810
AALVSGAVSI NSCPTA
Length:1,816
Mass (Da):201,819
Last modified:December 13, 2001 - v2
Checksum:iB49C45F3A45999D8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti8C → S in AAC52982 (PubMed:9049981).Curated1
Sequence conflicti18C → Y (PubMed:9049981).Curated1
Sequence conflicti248C → R in AAC24725 (PubMed:9346933).Curated1
Sequence conflicti297G → A in AAC24725 (PubMed:9346933).Curated1
Sequence conflicti431 – 433THR → HPS in AAC52982 (PubMed:9049981).Curated3
Sequence conflicti679S → C in AAC24725 (PubMed:9346933).Curated1
Sequence conflicti703D → G in AAC52982 (PubMed:9049981).Curated1
Sequence conflicti706N → H in AAC52982 (PubMed:9049981).Curated1
Sequence conflicti728K → R (PubMed:9049981).Curated1
Sequence conflicti730F → I (PubMed:9049981).Curated1
Sequence conflicti779R → G AA sequence (PubMed:9219532).Curated1
Sequence conflicti810R → S in AAC24725 (PubMed:9346933).Curated1
Sequence conflicti865 – 867AEP → QT in AAC52982 (PubMed:9049981).Curated3
Sequence conflicti936K → E in AAC24725 (PubMed:9346933).Curated1
Sequence conflicti970L → V in AAC24725 (PubMed:9346933).Curated1
Sequence conflicti1132H → R in AAC52982 (PubMed:9049981).Curated1
Sequence conflicti1200F → I in AAC52982 (PubMed:9049981).Curated1
Sequence conflicti1382D → A in AAC52982 (PubMed:9049981).Curated1
Sequence conflicti1413 – 1414NS → EF in CAA70970 (PubMed:9219532).Curated2
Sequence conflicti1489A → S in AAC52982 (PubMed:9049981).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58950 mRNA. Translation: AAB41840.1.
Y09827 mRNA. Translation: CAA70970.1.
U59865 mRNA. Translation: AAC24725.1.
BC115942 mRNA. Translation: AAI15943.1.
U88352 mRNA. Translation: AAC53178.1.
U69176 mRNA. Translation: AAC52982.1.
CCDSiCCDS35882.1.
RefSeqiNP_034811.2. NM_010681.4.
UniGeneiMm.258065.

Genome annotation databases

EnsembliENSMUST00000019992; ENSMUSP00000019992; ENSMUSG00000019846.
GeneIDi16775.
KEGGimmu:16775.
UCSCiuc007evq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58950 mRNA. Translation: AAB41840.1.
Y09827 mRNA. Translation: CAA70970.1.
U59865 mRNA. Translation: AAC24725.1.
BC115942 mRNA. Translation: AAI15943.1.
U88352 mRNA. Translation: AAC53178.1.
U69176 mRNA. Translation: AAC52982.1.
CCDSiCCDS35882.1.
RefSeqiNP_034811.2. NM_010681.4.
UniGeneiMm.258065.

3D structure databases

ProteinModelPortaliP97927.
SMRiP97927.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP97927. 1 interactor.
MINTiMINT-4100077.
STRINGi10090.ENSMUSP00000019992.

PTM databases

PhosphoSitePlusiP97927.

Proteomic databases

MaxQBiP97927.
PaxDbiP97927.
PeptideAtlasiP97927.
PRIDEiP97927.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019992; ENSMUSP00000019992; ENSMUSG00000019846.
GeneIDi16775.
KEGGimmu:16775.
UCSCiuc007evq.2. mouse.

Organism-specific databases

CTDi3910.
MGIiMGI:109321. Lama4.

Phylogenomic databases

eggNOGiENOG410KCXD. Eukaryota.
ENOG410Z3D5. LUCA.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000113278.
HOVERGENiHBG052299.
InParanoidiP97927.
KOiK06241.
OMAiQVSMMFD.
OrthoDBiEOG091G005L.
PhylomeDBiP97927.
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

ChiTaRSiLama4. mouse.
PROiP97927.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000019846.
CleanExiMM_LAMA4.
GenevisibleiP97927. 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.
[Graphical view]
PfamiPF00053. Laminin_EGF. 3 hits.
PF02210. Laminin_G_2. 5 hits.
PF06008. Laminin_I. 1 hit.
PF06009. Laminin_II. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 3 hits.
SM00180. EGF_Lam. 3 hits.
SM00282. LamG. 5 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 6 hits.
PROSITEiPS00022. EGF_1. 1 hit.
PS01248. EGF_LAM_1. 3 hits.
PS50027. EGF_LAM_2. 3 hits.
PS50025. LAM_G_DOMAIN. 5 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLAMA4_MOUSE
AccessioniPrimary (citable) accession number: P97927
Secondary accession number(s): O88785, P70409, Q14BF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: December 13, 2001
Last modified: November 30, 2016
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.