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P97927 (LAMA4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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-4
Alternative name(s):
Laminin-14 subunit alpha
Laminin-8 subunit alpha
Laminin-9 subunit alpha
Gene names
Name:Lama4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1816 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.

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

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane. Note: Major component.

Tissue specificity

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

Domain

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 similarities

Contains 4 laminin EGF-like domains.

Contains 5 laminin G-like domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 18161792Laminin subunit alpha-4
PRO_0000017061

Regions

Domain82 – 13150Laminin EGF-like 1
Domain132 – 18655Laminin EGF-like 2
Domain187 – 24054Laminin EGF-like 3
Domain241 – 25515Laminin EGF-like 4; truncated
Domain826 – 1030205Laminin G-like 1
Domain1042 – 1222181Laminin G-like 2
Domain1229 – 1397169Laminin G-like 3
Domain1462 – 1633172Laminin G-like 4
Domain1640 – 1813174Laminin G-like 5
Region256 – 825570Domain II and I
Coiled coil431 – 52393 Potential
Coiled coil556 – 60449 Potential
Coiled coil655 – 71763 Potential
Coiled coil770 – 79930 Potential
Motif717 – 7193Cell attachment site Potential

Amino acid modifications

Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation2151N-linked (GlcNAc...) Potential
Glycosylation3081N-linked (GlcNAc...) Potential
Glycosylation3331N-linked (GlcNAc...) Potential
Glycosylation4581N-linked (GlcNAc...) Potential
Glycosylation5501N-linked (GlcNAc...) Potential
Glycosylation5711N-linked (GlcNAc...) Potential
Glycosylation5741N-linked (GlcNAc...) Potential
Glycosylation6311N-linked (GlcNAc...) Potential
Glycosylation6391N-linked (GlcNAc...) Potential
Glycosylation7351N-linked (GlcNAc...) Potential
Glycosylation7511N-linked (GlcNAc...) Potential
Glycosylation7541N-linked (GlcNAc...) Potential
Glycosylation7801N-linked (GlcNAc...) Potential
Glycosylation8031N-linked (GlcNAc...) Potential
Glycosylation10881N-linked (GlcNAc...) Potential
Glycosylation12831N-linked (GlcNAc...) Potential
Glycosylation13611N-linked (GlcNAc...) Potential
Disulfide bond82 ↔ 91 By similarity
Disulfide bond84 ↔ 98 By similarity
Disulfide bond101 ↔ 110 By similarity
Disulfide bond113 ↔ 129 By similarity
Disulfide bond132 ↔ 146 By similarity
Disulfide bond134 ↔ 155 By similarity
Disulfide bond157 ↔ 166 By similarity
Disulfide bond169 ↔ 184 By similarity
Disulfide bond187 ↔ 202 By similarity
Disulfide bond189 ↔ 209 By similarity
Disulfide bond212 ↔ 221 By similarity
Disulfide bond224 ↔ 238 By similarity
Disulfide bond266Interchain Probable
Disulfide bond269Interchain Probable
Disulfide bond1000 ↔ 1030 By similarity
Disulfide bond1196 ↔ 1222 By similarity
Disulfide bond1365 ↔ 1397 By similarity
Disulfide bond1610 ↔ 1633 By similarity
Disulfide bond1785 ↔ 1813 By similarity

Experimental info

Sequence conflict81C → S in AAC52982. Ref.2
Sequence conflict181C → Y Ref.2
Sequence conflict2481C → R in AAC24725. Ref.3
Sequence conflict2971G → A in AAC24725. Ref.3
Sequence conflict431 – 4333THR → HPS in AAC52982. Ref.2
Sequence conflict6791S → C in AAC24725. Ref.3
Sequence conflict7031D → G in AAC52982. Ref.2
Sequence conflict7061N → H in AAC52982. Ref.2
Sequence conflict7281K → R Ref.2
Sequence conflict7301F → I Ref.2
Sequence conflict7791R → G AA sequence Ref.1
Sequence conflict8101R → S in AAC24725. Ref.3
Sequence conflict865 – 8673AEP → QT in AAC52982. Ref.2
Sequence conflict9361K → E in AAC24725. Ref.3
Sequence conflict9701L → V in AAC24725. Ref.3
Sequence conflict11321H → R in AAC52982. Ref.2
Sequence conflict12001F → I in AAC52982. Ref.2
Sequence conflict13821D → A in AAC52982. Ref.2
Sequence conflict1413 – 14142NS → EF in CAA70970. Ref.1
Sequence conflict14891A → S in AAC52982. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P97927 [UniParc].

Last modified December 13, 2001. Version 2.
Checksum: B49C45F3A45999D8

FASTA1,816201,819
        10         20         30         40         50         60 
MGWSTAWCSV LALWLLWCAV CSNAASGDGN AFPFDIEGSA VVGRQDPSET SDSGVTLGRL 

        70         80         90        100        110        120 
PPAAERCDAG FFRTLSGECA PCDCNGNSHE CLDGSGFCLH CQRNTTGEHC EKCLDGYIGD 

       130        140        150        160        170        180 
SIRGTPRFCQ PCPCPLPHLA NFAESCYRKN GAVRCICKEN YVGPNCERCA PGYYGNPLLI 

       190        200        210        220        230        240 
GSTCKKCDCS GNSDPNLIFE DCDEITGQCR NCLRNTTGFK CERCAPGYYG DARTAKNCAV 

       250        260        270        280        290        300 
CNCGGGPCDS VTGECLEEGF EVPTGCDKCV WDLTDDLRLA ALSIEESKSG LLSVSSGAAA 

       310        320        330        340        350        360 
HRHVTDMNST IHLLRTRLSE RENQYTLRKI QINNSENTLR SLLPDVEGLH EKGSQASRKG 

       370        380        390        400        410        420 
MLVEKESMDT IDQATHLVEQ AHNMRDKIQE INSKMLYYGE NQELGPEEIA EKLVLAQKML 

       430        440        450        460        470        480 
EEIRSRQPFL THRELVDEEA DEAQELLSQA ENWQRLHNDT RSLFPVVLEQ LDDYNAKLSD 

       490        500        510        520        530        540 
LQESINQALD HVRDAEDMNR AITFKQRDHE KQHERVKEQM EVVGASLSMS ADSLTIPQLT 

       550        560        570        580        590        600 
LEELDEIIKN ASGIYAEIDG AKNELQGKLS NLSNLSHDLV QEATDHAYNL QQEADELSRN 

       610        620        630        640        650        660 
LHSSDMNGLV QKALDASNVY ENIANYVSEA NETAELALNI TDRIYDAVSG IDTQIIYHKD 

       670        680        690        700        710        720 
ESDNLLNQAR ELQAKADSSN DEAVADTSRR VGGALWRKGA LRDRLNDAVK QLQAAERGDA 

       730        740        750        760        770        780 
HQRLGQSKLF IEEANKTTAA VQQVTTPMAN NLSNWSQNLQ TFDSSAYNTA VDSARDAVRN 

       790        800        810        820        830        840 
LTEVVPQLLD QLRTVEQKRP ASNISASIQR IRELIAQTRS VASKIQVSMM FDGQSAVEVH 

       850        860        870        880        890        900 
PKVSVDDLKA FTSISLYMKP PPKPAEPTGA WVADQFVLYL GSKNAKKEYM GLAIKNDNLV 

       910        920        930        940        950        960 
YVYNLGMKDV EILLDSKPVS SWPAYFSIVK IERVGKHGKV FLTVPSLSST AEEKFIKKGE 

       970        980        990       1000       1010       1020 
FAGDDSLLDL TPEDTVFYVG GVPANFKLPA SLNLPSYSGC LELATLNNDV ISLYNFKHIY 

      1030       1040       1050       1060       1070       1080 
NMDPSKSVPC ARDKLAFTQS RAASYFFDGS SYAVVRDITR RGKFGQVTRF DIEIRTPADN 

      1090       1100       1110       1120       1130       1140 
GLVLLMVNGS MFFSLEMRNG YLHVFYDFGF SNGPVHLEDT LKKAQINDAK YHEISIIYHN 

      1150       1160       1170       1180       1190       1200 
DKKMILVVDR RHVKSTDNEK KKIPFTDIYI GGAPQEVLQS RTLRAHLPLD INFRGCMKGF 

      1210       1220       1230       1240       1250       1260 
QFQKKDFNLL EQTETLGVGY GCPEDSLISR RAYFNGQSFI ASIQKISFFD GFEGGFNFRT 

      1270       1280       1290       1300       1310       1320 
LQPNGLLFYY TSGSDVFSIS LDNGTVVMDV KGIKVMSTDK QYHDGLPHFV VTSISDTRYE 

      1330       1340       1350       1360       1370       1380 
LVVDKSRLRG KNPTKGKAEQ TQTTEKKFYF GGSPISPQYA NFTGCISNAY FTRLDRDVEV 

      1390       1400       1410       1420       1430       1440 
EDFQRYSEKV HTSLYECPIE SSPLFLLHKK GKNSSKPKTN KQGEKSKDAP SWDPIGLKFL 

      1450       1460       1470       1480       1490       1500 
EQKAPRDSHC HLSSSPRAIE HAYQYGGTAN SRQEFEHEQG DFGEKSQFAI RLKTRSSHGM 

      1510       1520       1530       1540       1550       1560 
IFYVSDQEEN DFMTLFLAHG RLVFMFNVGH KKLKIRSQEK YNDGLWHDVI FIREKSSGRL 

      1570       1580       1590       1600       1610       1620 
VIDGLRVLEE RLPPSGAAWK IKGPIYLGGV APGRAVKNVQ ITSVYSFSGC LGNLQLNGAS 

      1630       1640       1650       1660       1670       1680 
ITSASQTFSV TPCFEGPMET GTYFSTEGGY VVLDESFNIG LKFEIAFEVR PRSSSGTLVH 

      1690       1700       1710       1720       1730       1740 
GHSVNGEYLN VHMRNGQVIV KVNNGVRDFS TSVTPKQNLC DGRWHRITVI RDSNVVQLDV 

      1750       1760       1770       1780       1790       1800 
DSEVNHVVGP LNPKPVDHRE PVFVGGVPES LLTPRLAPSK PFTGCIRHFV IDSRPVSFSK 

      1810 
AALVSGAVSI NSCPTA 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the mouse laminin alpha 4 cDNA. Expression in a subset of endothelium."
Frieser M., Noeckel H., Pausch F., Roeder C., Hahn A., Deutzmann R., Sorokin L.M.
Eur. J. Biochem. 246:727-735(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 462-469; 478-483; 776-782 AND 940-945.
Strain: BALB/c.
Tissue: Endothelial cell.
[2]"The complete cDNA coding sequence and tissue-specific expression of the mouse laminin alpha 4 chain."
Liu J., Mayne R.
Matrix Biol. 15:433-437(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[3]"Primary structure, developmental expression, and immunolocalization of the murine laminin alpha4 chain."
Iivanainen A., Kortesmaa J., Sahlberg C., Morita T., Bergmann U., Thesleff I., Tryggvason K.
J. Biol. Chem. 272:27862-27868(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The laminin alpha chains: expression, developmental transitions, and chromosomal locations of alpha1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel alpha3 isoform."
Miner J.H., Patton B.L., Lentz S.I., Gilbert D.J., Snider W.D., Jenkins N.A., Copeland N.G., Sanes J.R.
J. Cell Biol. 137:685-701(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 836-1106.
Strain: ICR.
Tissue: Placenta.
[6]"Distribution of the ten known laminin chains in the pathways and targets of developing sensory axons."
Lentz S.I., Miner J.H., Sanes J.R., Snider W.D.
J. Comp. Neurol. 378:547-561(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1467-1691.
Tissue: Placenta.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_034811.2. NM_010681.4.
UniGeneMm.258065.

3D structure databases

ProteinModelPortalP97927.
SMRP97927. Positions 9-300, 829-1373, 1450-1815.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP97927. 1 interaction.
MINTMINT-4100077.

PTM databases

PhosphoSiteP97927.

Proteomic databases

PaxDbP97927.
PRIDEP97927.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000019992; ENSMUSP00000019992; ENSMUSG00000019846.
GeneID16775.
KEGGmmu:16775.
UCSCuc007evq.2. mouse.

Organism-specific databases

CTD3910.
MGIMGI:109321. Lama4.

Phylogenomic databases

eggNOGNOG247347.
GeneTreeENSGT00750000117549.
HOGENOMHOG000113278.
HOVERGENHBG052299.
InParanoidQ14BF2.
KOK06241.
OMAPKPVDHR.
OrthoDBEOG7VX8V2.
PhylomeDBP97927.
TreeFamTF335359.

Gene expression databases

ArrayExpressP97927.
BgeeP97927.
CleanExMM_LAMA4.
GenevestigatorP97927.

Family and domain databases

Gene3D2.60.120.200. 5 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR002049. EGF_laminin.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
IPR010307. Laminin_II.
[Graphical view]
PfamPF00053. Laminin_EGF. 3 hits.
PF02210. Laminin_G_2. 5 hits.
PF06008. Laminin_I. 1 hit.
PF06009. Laminin_II. 1 hit.
[Graphical view]
SMARTSM00180. EGF_Lam. 3 hits.
SM00282. LamG. 5 hits.
[Graphical view]
SUPFAMSSF49899. SSF49899. 6 hits.
PROSITEPS00022. EGF_1. 1 hit.
PS01248. EGF_LAM_1. 3 hits.
PS50027. EGF_LAM_2. 3 hits.
PS50025. LAM_G_DOMAIN. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLAMA4. mouse.
NextBio290616.
PROP97927.
SOURCESearch...

Entry information

Entry nameLAMA4_MOUSE
AccessionPrimary (citable) accession number: P97927
Secondary accession number(s): O88785, P70409, Q14BF2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: December 13, 2001
Last modified: April 16, 2014
This is version 126 of the entry and version 2 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

MGD cross-references

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