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Q9R0B6 (LAMC3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. 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 gamma-3
Alternative name(s):
Laminin-12 subunit gamma
Laminin-14 subunit gamma
Laminin-15 subunit gamma
Gene names
Name:Lamc3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1581 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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. Gamma-3 is a subunit of laminin-12 (laminin-213), laminin-14 (laminin-423) and laminin-15 (laminin-523).

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane.

Tissue specificity

Strongly expressed in capillaries and arterioles of kidney as well as in interstitial Leydig cells of testis.

Domain

The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.

Domain IV is globular.

Sequence similarities

Contains 11 laminin EGF-like domains.

Contains 1 laminin IV type A domain.

Contains 1 laminin N-terminal domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 15811553Laminin subunit gamma-3
PRO_0000017080

Regions

Domain40 – 279240Laminin N-terminal
Domain280 – 33556Laminin EGF-like 1
Domain336 – 39156Laminin EGF-like 2
Domain392 – 43847Laminin EGF-like 3
Domain439 – 48850Laminin EGF-like 4
Domain489 – 49810Laminin EGF-like 5; first part
Domain508 – 684177Laminin IV type A
Domain685 – 71834Laminin EGF-like 5; second part
Domain719 – 76648Laminin EGF-like 6
Domain767 – 82155Laminin EGF-like 7
Domain822 – 87756Laminin EGF-like 8
Domain878 – 92750Laminin EGF-like 9
Domain928 – 97548Laminin EGF-like 10
Domain976 – 102449Laminin EGF-like 11
Region1025 – 1581557Domain II and I
Coiled coil1029 – 104618 Potential
Coiled coil1112 – 115342 Potential
Coiled coil1208 – 123124 Potential
Coiled coil1438 – 146831 Potential
Coiled coil1510 – 157566 Potential

Amino acid modifications

Glycosylation1281N-linked (GlcNAc...) Potential
Glycosylation3041N-linked (GlcNAc...) Potential
Glycosylation3371N-linked (GlcNAc...) Potential
Glycosylation6401N-linked (GlcNAc...) Potential
Glycosylation8491N-linked (GlcNAc...) Potential
Glycosylation9911N-linked (GlcNAc...) Potential
Glycosylation11621N-linked (GlcNAc...) Potential
Glycosylation11961N-linked (GlcNAc...) Potential
Glycosylation13201N-linked (GlcNAc...) Potential
Glycosylation15141N-linked (GlcNAc...) Potential
Disulfide bond280 ↔ 289 By similarity
Disulfide bond282 ↔ 299 By similarity
Disulfide bond301 ↔ 310 By similarity
Disulfide bond313 ↔ 333 By similarity
Disulfide bond336 ↔ 345 By similarity
Disulfide bond338 ↔ 361 By similarity
Disulfide bond364 ↔ 373 By similarity
Disulfide bond376 ↔ 389 By similarity
Disulfide bond392 ↔ 404 By similarity
Disulfide bond394 ↔ 410 By similarity
Disulfide bond412 ↔ 421 By similarity
Disulfide bond424 ↔ 436 By similarity
Disulfide bond439 ↔ 450 By similarity
Disulfide bond441 ↔ 457 By similarity
Disulfide bond459 ↔ 468 By similarity
Disulfide bond471 ↔ 486 By similarity
Disulfide bond719 ↔ 727 By similarity
Disulfide bond721 ↔ 734 By similarity
Disulfide bond736 ↔ 745 By similarity
Disulfide bond748 ↔ 764 By similarity
Disulfide bond767 ↔ 775 By similarity
Disulfide bond769 ↔ 786 By similarity
Disulfide bond789 ↔ 798 By similarity
Disulfide bond801 ↔ 819 By similarity
Disulfide bond822 ↔ 836 By similarity
Disulfide bond824 ↔ 843 By similarity
Disulfide bond846 ↔ 855 By similarity
Disulfide bond858 ↔ 875 By similarity
Disulfide bond878 ↔ 891 By similarity
Disulfide bond880 ↔ 898 By similarity
Disulfide bond900 ↔ 909 By similarity
Disulfide bond912 ↔ 925 By similarity
Disulfide bond928 ↔ 940 By similarity
Disulfide bond930 ↔ 947 By similarity
Disulfide bond949 ↔ 958 By similarity
Disulfide bond961 ↔ 973 By similarity
Disulfide bond976 ↔ 988 By similarity
Disulfide bond978 ↔ 994 By similarity
Disulfide bond996 ↔ 1005 By similarity
Disulfide bond1008 ↔ 1021 By similarity

Experimental info

Sequence conflict91L → F in AAD29851. Ref.5
Sequence conflict1901P → T in AAD29851. Ref.5
Sequence conflict1951R → K in AAD29851. Ref.5
Sequence conflict2211G → S in AAD29851. Ref.5
Sequence conflict3941C → R in AAD29851. Ref.5
Sequence conflict4711C → Y in AAD29851. Ref.5
Sequence conflict11501L → LDEPQLFSLLLK in AAD29851. Ref.5
Sequence conflict13871Q → H in AAF08983. Ref.1
Sequence conflict1438 – 14392AS → TI in AAD29851. Ref.5
Sequence conflict14791I → V in AAF08983. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9R0B6 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: A6E83A8F9C678830

FASTA1,581172,322
        10         20         30         40         50         60 
MAVSRVLSLL ATVASMALVI QETHFAAGAD MGSCYDGVGR AQRCLPEFEN AAFGRRAEAS 

        70         80         90        100        110        120 
HTCGRPPEDF CPHVGAPGAG LQCQRCDDAD PGRRHDASYL TDFHSPDDST WWQSPSMAFG 

       130        140        150        160        170        180 
VQYPTSVNLT LSLGKAYEIT YVRLKFHTSR PESFAIYKRT YASGPWEPYQ YYSASCQKTY 

       190        200        210        220        230        240 
GRPEGHYLRP GEDERVAFCT SEFSDISPLN GGNVAFSTLE GRPSAYNFEE SPVLQEWVTS 

       250        260        270        280        290        300 
TDILISLDRL NTFGDDIFKD PRVLQSYYYA VSDFSVGGRC KCNGHASECE PNAAGQLACR 

       310        320        330        340        350        360 
CQHNTTGVDC ERCLPFFQDR PWARGTAEDA NECLPCNCSG HSEECTFDRE LYRSTGHGGH 

       370        380        390        400        410        420 
CQRCRDHTTG PHCERCEKNY YRWSPKTPCQ PCDCHPAGSL SLQCDNSGVC PCKPTVTGWK 

       430        440        450        460        470        480 
CDRCLPGFHS LSEGGCRPCA CNVAGSLGTC DPRSGNCPCK ENVEGSLCDR CRPGTFNLQP 

       490        500        510        520        530        540 
HNPVGCSSCF CYGHSKVCSP AAGFQEHHIR SDFRHGAGGW QIRSMGVSKR PLQWSQSGLL 

       550        560        570        580        590        600 
LGLRGGEELS APKKFLGDQR LSYGQPVILT LQVPPGGSPP PIQLRLEGAG LALSLRPSSL 

       610        620        630        640        650        660 
PSPQDTRQPR RVQLQFLLQE TSEEAESPLP TFHFQRLLSN LTALSIWTSG QGPGHSGQVL 

       670        680        690        700        710        720 
LCEVQLTSAW PQRELAPPAS WVETCLCPQG YTGQFCEFCA LGYKREIPHG GPYANCIPCT 

       730        740        750        760        770        780 
CNQHGTCDPN TGICLCGHHT EGPSCERCMP GFYGNAFSGR ADDCQPCPCP GQSACATIPE 

       790        800        810        820        830        840 
SGDVVCTHCP PGQRGRRCES CEDGFFGDPL GLSGAPQPCR RCQCSGNVDL NAVGNCDPHS 

       850        860        870        880        890        900 
GHCLRCLYNT TGAHCEHCRE GFYGSAVATR PVDKCAPCSC DLRGSVSEKT CNPVTGQCVC 

       910        920        930        940        950        960 
LPYVSGRDCS RCSPGFYDLQ SGRGCQSCKC HPLGSLENKC HPKTGQCPCR PGVTGQACDR 

       970        980        990       1000       1010       1020 
CQLGFFGFSI KGCRDCRCSP LGAASSQCHE NSTCVCRPGF VGYKCDRCQD NFFLADGDTG 

      1030       1040       1050       1060       1070       1080 
CQECPTCYAL VKEEAAKLKA RLMLMEGWLQ RSDCGSPWGP LDILQGEAPL GDVYQGHHLL 

      1090       1100       1110       1120       1130       1140 
QETRGTFLQQ MVGLEDSVKA TWEQLQVLRG HVHCAQAGAQ KTCIQLAELE ETLQSSEEEV 

      1150       1160       1170       1180       1190       1200 
LRAASALSFL ASLQKGSSTP TNWSHLASEA QILARSHRDT ATKIEATSER ALLASNASYE 

      1210       1220       1230       1240       1250       1260 
LLKLMEGRVA SEAQQELEDR YQEVQAAQTA LGIAVAEALP KAEKALATVK QVIGDAAPHL 

      1270       1280       1290       1300       1310       1320 
GLLVTPEAMN FQARGLSWKV KALEQKLEQK EPEVGQSVGA LQVEAGRALE KMEPFMQLRN 

      1330       1340       1350       1360       1370       1380 
KTTAAFTRAS SAVQAAKVTV IGAETLLADL EGMKLRSPLP KEQAALKKKA GSIRTRLLED 

      1390       1400       1410       1420       1430       1440 
TKRKTKQAER MLGNAASLSS STKKKSKEAE LMSKDNAKLS RALLREGKQG YRHASRLASQ 

      1450       1460       1470       1480       1490       1500 
TQATLRRASR LLLTSEAHKQ ELEEAKQVTS GLSTVERQIR ESRISLEKDT KVLSELLVKL 

      1510       1520       1530       1540       1550       1560 
GSLGVHQAPA QTLNETQRAL ESLRLQLDSH GALHHKLRQL EEESARQELQ IQSFEDDLAE 

      1570       1580 
IRADKHNLET ILSSLPENCA S 

« Hide

References

« Hide 'large scale' references
[1]"Mouse laminin 12 gamma 3 chain."
Albus A.M., Burgeson B., Champliaud M.-F., Koch M., Olson P.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
Strain: FVB/N.
Tissue: Mammary tumor.
[5]"Molecular cloning and tissue-specific expression of a novel murine laminin gamma3 chain."
Iivanainen A., Morita T., Tryggvason K.
J. Biol. Chem. 274:14107-14111(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1526.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF083372 mRNA. Translation: AAF08983.1.
AL928893, BX511243 Genomic DNA. Translation: CAM26043.1.
BX511243, AL928893 Genomic DNA. Translation: CAM26482.1.
CH466542 Genomic DNA. Translation: EDL08519.1.
BC096366 mRNA. Translation: AAH96366.1.
AF079520 mRNA. Translation: AAD29851.1.
RefSeqNP_035966.2. NM_011836.3.
UniGeneMm.302362.

3D structure databases

ProteinModelPortalQ9R0B6.
SMRQ9R0B6. Positions 34-391.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204801. 1 interaction.

Proteomic databases

PaxDbQ9R0B6.
PRIDEQ9R0B6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028187; ENSMUSP00000028187; ENSMUSG00000026840.
GeneID23928.
KEGGmmu:23928.
UCSCuc008jef.1. mouse.

Organism-specific databases

CTD10319.
MGIMGI:1344394. Lamc3.

Phylogenomic databases

eggNOGNOG235720.
GeneTreeENSGT00750000117374.
HOGENOMHOG000019301.
HOVERGENHBG100808.
KOK06247.
OMAQRGRRCE.
TreeFamTF352481.

Gene expression databases

ArrayExpressQ9R0B6.
BgeeQ9R0B6.
CleanExMM_LAMC3.
GenevestigatorQ9R0B6.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
InterProIPR002049. EGF_laminin.
IPR008979. Galactose-bd-like.
IPR000034. Laminin_B_type_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 10 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTSM00180. EGF_Lam. 10 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEPS00022. EGF_1. 8 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 11 hits.
PS50027. EGF_LAM_2. 10 hits.
PS51115. LAMININ_IVA. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio303725.
PROQ9R0B6.
SOURCESearch...

Entry information

Entry nameLAMC3_MOUSE
AccessionPrimary (citable) accession number: Q9R0B6
Secondary accession number(s): Q4VAI3, Q9WTW6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 115 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