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Q9Y6N6 (LAMC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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

Clusters with 100%, 90%, 50% identity | Documents (5) | 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1575 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. 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

Broadly expressed in: skin, heart, lung, and the reproductive tracts.

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.

Involvement in disease

Cortical malformations occipital (OCCM) [MIM:614115]: A disease in which affected individuals develop seizures, sometimes associated with transient visual changes. Brain MRI shows both pachygyria and polymicrogyria restricted to the lateral occipital lobes.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4

Sequence similarities

Contains 11 laminin EGF-like domains.

Contains 1 laminin IV type A domain.

Contains 1 laminin N-terminal domain.

Sequence caution

The sequence AAD36991.1 differs from that shown. Reason: Frameshift at positions 598 and 609.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 15751556Laminin subunit gamma-3
PRO_0000017079

Regions

Domain31 – 270240Laminin N-terminal
Domain271 – 32656Laminin EGF-like 1
Domain327 – 38256Laminin EGF-like 2
Domain383 – 42947Laminin EGF-like 3
Domain430 – 47950Laminin EGF-like 4
Domain480 – 48910Laminin EGF-like 5; first part
Domain499 – 672174Laminin IV type A
Domain673 – 70634Laminin EGF-like 5; second part
Domain707 – 75448Laminin EGF-like 6
Domain755 – 80955Laminin EGF-like 7
Domain810 – 86556Laminin EGF-like 8
Domain866 – 91651Laminin EGF-like 9
Domain917 – 96448Laminin EGF-like 10
Domain965 – 101349Laminin EGF-like 11
Region1014 – 1575562Domain II and I
Coiled coil1073 – 113462 Potential
Coiled coil1201 – 122828 Potential
Coiled coil1410 – 149283 Potential
Coiled coil1523 – 156745 Potential
Motif1059 – 10613Cell attachment site Potential

Amino acid modifications

Glycosylation871N-linked (GlcNAc...) Potential
Glycosylation1191N-linked (GlcNAc...) Potential
Glycosylation2951N-linked (GlcNAc...) Potential
Glycosylation3281N-linked (GlcNAc...) Potential
Glycosylation6311N-linked (GlcNAc...) Potential
Glycosylation8371N-linked (GlcNAc...) Potential
Glycosylation9801N-linked (GlcNAc...) Potential
Glycosylation11851N-linked (GlcNAc...) Potential
Disulfide bond271 ↔ 280 By similarity
Disulfide bond273 ↔ 290 By similarity
Disulfide bond292 ↔ 301 By similarity
Disulfide bond304 ↔ 324 By similarity
Disulfide bond327 ↔ 336 By similarity
Disulfide bond329 ↔ 352 By similarity
Disulfide bond355 ↔ 364 By similarity
Disulfide bond367 ↔ 380 By similarity
Disulfide bond383 ↔ 395 By similarity
Disulfide bond385 ↔ 401 By similarity
Disulfide bond403 ↔ 412 By similarity
Disulfide bond415 ↔ 427 By similarity
Disulfide bond430 ↔ 441 By similarity
Disulfide bond432 ↔ 448 By similarity
Disulfide bond450 ↔ 459 By similarity
Disulfide bond462 ↔ 477 By similarity
Disulfide bond707 ↔ 715 By similarity
Disulfide bond709 ↔ 722 By similarity
Disulfide bond724 ↔ 733 By similarity
Disulfide bond736 ↔ 752 By similarity
Disulfide bond755 ↔ 763 By similarity
Disulfide bond757 ↔ 774 By similarity
Disulfide bond777 ↔ 786 By similarity
Disulfide bond789 ↔ 807 By similarity
Disulfide bond810 ↔ 824 By similarity
Disulfide bond812 ↔ 831 By similarity
Disulfide bond834 ↔ 843 By similarity
Disulfide bond846 ↔ 863 By similarity
Disulfide bond866 ↔ 880 By similarity
Disulfide bond868 ↔ 887 By similarity
Disulfide bond889 ↔ 898 By similarity
Disulfide bond901 ↔ 914 By similarity
Disulfide bond917 ↔ 929 By similarity
Disulfide bond919 ↔ 936 By similarity
Disulfide bond938 ↔ 947 By similarity
Disulfide bond950 ↔ 962 By similarity
Disulfide bond965 ↔ 977 By similarity
Disulfide bond967 ↔ 983 By similarity
Disulfide bond985 ↔ 994 By similarity
Disulfide bond997 ↔ 1010 By similarity

Natural variations

Natural variant3501G → R in OCCM. Ref.4
VAR_066404
Natural variant5221P → S. Ref.1
Corresponds to variant rs869457 [ dbSNP | Ensembl ].
VAR_056145
Natural variant5441E → G. Ref.1 Ref.3
Corresponds to variant rs10901333 [ dbSNP | Ensembl ].
VAR_056146
Natural variant7701R → G. Ref.1 Ref.3
Corresponds to variant rs3739510 [ dbSNP | Ensembl ].
VAR_056147
Natural variant10821S → G. Ref.1 Ref.3
Corresponds to variant rs2275140 [ dbSNP | Ensembl ].
VAR_056148
Natural variant12641R → W.
Corresponds to variant rs11244275 [ dbSNP | Ensembl ].
VAR_056149

Experimental info

Sequence conflict9571F → S in AAD36991. Ref.1
Sequence conflict9791E → Y in AAD36991. Ref.1
Sequence conflict9991D → Y in AAD36991. Ref.1
Sequence conflict10241A → T in AAD36991. Ref.1
Sequence conflict11571T → I in AAD36991. Ref.1
Sequence conflict13091K → KARSRLTATSASQ in CAH69983. Ref.2
Sequence conflict13091K → MARSRLTATFASQ in AAD36991. Ref.1
Sequence conflict13131E → G in AAD36991. Ref.1
Sequence conflict14331T → M in BAD92124. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9Y6N6 [UniParc].

Last modified October 5, 2010. Version 3.
Checksum: D09DAFB3A900E1BD

FASTA1,575171,227
        10         20         30         40         50         60 
MAAAALLLGL ALLAPRAAGA GMGACYDGAG RPQRCLPVFE NAAFGRLAQA SHTCGSPPED 

        70         80         90        100        110        120 
FCPHVGAAGA GAHCQRCDAA DPQRHHNASY LTDFHSQDES TWWQSPSMAF GVQYPTSVNI 

       130        140        150        160        170        180 
TLRLGKAYEI TYVRLKFHTS RPESFAIYKR SRADGPWEPY QFYSASCQKT YGRPEGQYLR 

       190        200        210        220        230        240 
PGEDERVAFC TSEFSDISPL SGGNVAFSTL EGRPSAYNFE ESPGLQEWVT STELLISLDR 

       250        260        270        280        290        300 
LNTFGDDIFK DPKVLQSYYY AVSDFSVGGR CKCNGHASEC GPDVAGQLAC RCQHNTTGTD 

       310        320        330        340        350        360 
CERCLPFFQD RPWARGTAEA AHECLPCNCS GRSEECTFDR ELFRSTGHGG RCHHCRDHTA 

       370        380        390        400        410        420 
GPHCERCQEN FYHWDPRMPC QPCDCQSAGS LHLQCDDTGT CACKPTVTGW KCDRCLPGFH 

       430        440        450        460        470        480 
SLSEGGCRPC TCNPAGSLDT CDPRSGRCPC KENVEGNLCD RCRPGTFNLQ PHNPAGCSSC 

       490        500        510        520        530        540 
FCYGHSKVCA STAQFQVHHI LSDFHQGAEG WWARSVGGSE HPPQWSPNGV LLSPEDEEEL 

       550        560        570        580        590        600 
TAPEKFLGDQ RFSYGQPLIL TFRVPPGDSP LPVQLRLEGT GLALSLRHSS LSGPQDAGHP 

       610        620        630        640        650        660 
REVELRFHLQ ETSEDVAPPL PPFHFQRLLA NLTSLRLRVS PGPSPAGPVF LTEVRLTSAR 

       670        680        690        700        710        720 
PGLSPPASWV EICSCPTGYT GQFCESCAPG YKREMPQGGP YASCVPCTCN QHGTCDPNTG 

       730        740        750        760        770        780 
ICVCSHHTEG PSCERCLPGF YGNPFAGQAD DCQPCPCPGQ SACTTIPESR EVVCTHCPPG 

       790        800        810        820        830        840 
QRGRRCEVCD DGFFGDPLGL FGHPQPCHQC QCSGNVDPNA VGNCDPLSGH CLRCLHNTTG 

       850        860        870        880        890        900 
DHCEHCQEGF YGSALAPRPA DKCMPCSCHP QGSVSEQMPC DPVTGQCSCL PHVTARDCSR 

       910        920        930        940        950        960 
CYPGFFDLQP GRGCRSCKCH PLGSQEDQCH PKTGQCTCRP GVTGQACDRC QLGFFGFSIK 

       970        980        990       1000       1010       1020 
GCRACRCSPL GAASAQCHEN GTCVCRPGFE GYKCDRCHDN FFLTADGTHC QQCPSCYALV 

      1030       1040       1050       1060       1070       1080 
KEEAAKLKAR LTLTEGWLQG SDCGSPWGPL DILLGEAPRG DVYQGHHLLP GAREAFLEQM 

      1090       1100       1110       1120       1130       1140 
MSLEGAVKAA REQLQRLNKG ARCAQAGSQK TCTQLADLEA VLESSEEEIL HAAAILASLE 

      1150       1160       1170       1180       1190       1200 
IPQEGPSQPT KWSHLATEAR ALARSHRDTA TKIAATAWRA LLASNTSYAL LWNLLEGRVA 

      1210       1220       1230       1240       1250       1260 
LETQRDLEDR YQEVQAAQKA LRTAVAEVLP EAESVLATVQ QVGADTAPYL ALLASPGALP 

      1270       1280       1290       1300       1310       1320 
QKSRAEDLGL KAKALEKTVA SWQHMATEAA RTLQTAAQAT LRQTEPLTKL HQEARAALTQ 

      1330       1340       1350       1360       1370       1380 
ASSSVQAATV TVMGARTLLA DLEGMKLQFP RPKDQAALQR KADSVSDRLL ADTRKKTKQA 

      1390       1400       1410       1420       1430       1440 
ERMLGNAAPL SSSAKKKGRE AEVLAKDSAK LAKALLRERK QAHRRASRLT SQTQATLQQA 

      1450       1460       1470       1480       1490       1500 
SQQVLASEAR RQELEEAERV GAGLSEMEQQ IRESRISLEK DIETLSELLA RLGSLDTHQA 

      1510       1520       1530       1540       1550       1560 
PAQALNETQW ALERLRLQLG SPGSLQRKLS LLEQESQQQE LQIQGFESDL AEIRADKQNL 

      1570 
EAILHSLPEN CASWQ 

« Hide

References

« Hide 'large scale' references
[1]"Characterization and expression of the laminin gamma3 chain: a novel, non-basement membrane-associated, laminin chain."
Koch M., Olson P.F., Albus A., Jin W., Hunter D.D., Brunken W.J., Burgeson R.E., Champliaud M.-F.
J. Cell Biol. 145:605-618(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SER-522; GLY-544; GLY-770 AND GLY-1082.
Tissue: Placenta.
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Homo sapiens protein coding cDNA."
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 197-1575, VARIANTS GLY-544; GLY-770 AND GLY-1082.
Tissue: Spleen.
[4]"Recessive LAMC3 mutations cause malformations of occipital cortical development."
Barak T., Kwan K.Y., Louvi A., Demirbilek V., Saygi S., Tuysuz B., Choi M., Boyaci H., Doerschner K., Zhu Y., Kaymakcalan H., Yilmaz S., Bakircioglu M., Caglayan A.O., Ozturk A.K., Yasuno K., Brunken W.J., Atalar E. expand/collapse author list , Yalcinkaya C., Dincer A., Bronen R.A., Mane S., Ozcelik T., Lifton R.P., Sestan N., Bilguvar K., Gunel M.
Nat. Genet. 43:590-594(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OCCM ARG-350.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF041835 mRNA. Translation: AAD36991.1. Frameshift.
AL583807, AL355872 Genomic DNA. Translation: CAH69983.1.
AL583807, AL355872 Genomic DNA. Translation: CAH69984.3.
AL355872, AL583807 Genomic DNA. Translation: CAX14981.1.
AB208887 mRNA. Translation: BAD92124.1.
RefSeqNP_006050.3. NM_006059.3.
UniGeneHs.201805.

3D structure databases

ProteinModelPortalQ9Y6N6.
SMRQ9Y6N6. Positions 25-470, 662-1016, 1546-1571.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115603. 21 interactions.
IntActQ9Y6N6. 21 interactions.
MINTMINT-7034525.
STRING9606.ENSP00000354360.

Chemistry

ChEMBLCHEMBL2364187.

Polymorphism databases

DMDM308153586.

Proteomic databases

PaxDbQ9Y6N6.
PRIDEQ9Y6N6.

Protocols and materials databases

DNASU10319.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361069; ENSP00000354360; ENSG00000050555.
GeneID10319.
KEGGhsa:10319.
UCSCuc004caa.1. human.

Organism-specific databases

CTD10319.
GeneCardsGC09P133884.
H-InvDBHIX0008477.
HGNCHGNC:6494. LAMC3.
HPAHPA022814.
MIM604349. gene.
614115. phenotype.
neXtProtNX_Q9Y6N6.
Orphanet280640. Occipital pachygyria and polymicrogyria.
PharmGKBPA30282.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG235720.
HOGENOMHOG000019301.
HOVERGENHBG100808.
KOK06247.
OrthoDBEOG7SR4KJ.
PhylomeDBQ9Y6N6.
TreeFamTF352481.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ9Y6N6.
BgeeQ9Y6N6.
CleanExHS_LAMC3.
GenevestigatorQ9Y6N6.

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. 11 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTSM00180. EGF_Lam. 10 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEPS00022. EGF_1. 7 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 10 hits.
PS50027. EGF_LAM_2. 10 hits.
PS51115. LAMININ_IVA. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLAMC3. human.
GeneWikiLAMC3.
GenomeRNAi10319.
NextBio39119.
PROQ9Y6N6.
SOURCESearch...

Entry information

Entry nameLAMC3_HUMAN
AccessionPrimary (citable) accession number: Q9Y6N6
Secondary accession number(s): B1APX9, B1APY0, Q59H72
Entry history
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: October 5, 2010
Last modified: April 16, 2014
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM