Seroatlas · Human Serome Atlas

LAMC3

Laminin subunit gamma-3

Also known as: DKFZp434E202, LAMC3_HUMAN

Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene

Protein identityUniProt · HPA

UniProt accession
Q9Y6N6
Gene
LAMC3
Ensembl
ENSG00000050555
Chromosome
9
Canonical length
1575 aa
Protein class
Disease related genes, Human disease related genes, Plasma proteins, Predicted intracellular proteins, Predicted secreted proteins
Secretome location
Secreted to extracellular matrix

OverviewNCBI Gene

Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the gamma chain isoform laminin, gamma 3. The gamma 3 chain is most similar to the gamma 1 chain, and contains all the 6 domains expected of the gamma chain. It is a component of laminin 12. The gamma 3 chain is broadly expressed in skin, heart, lung, and the reproductive tracts. In skin, it is seen within the basement membrane of the dermal-epidermal junction at points of nerve penetration. Gamma 3 is also a prominent element of the apical surface of ciliated epithelial cells of lung, oviduct, epididymis, ductus deferens, and seminiferous tubules. The distribution of gamma 3-containing laminins along ciliated epithelial surfaces suggests that the apical laminins are important in the morphogenesis and structural stability of the ciliated processes of these cells. [provided by RefSeq, Aug 2011]

Canonical amino-acid sequenceUniProt

1575 residues, UniProt reviewed canonical sequence.

>Q9Y6N6|LAMC3
     1  MAAAALLLGL ALLAPRAAGA GMGACYDGAG RPQRCLPVFE NAAFGRLAQA SHTCGSPPED
    61  FCPHVGAAGA GAHCQRCDAA DPQRHHNASY LTDFHSQDES TWWQSPSMAF GVQYPTSVNI
   121  TLRLGKAYEI TYVRLKFHTS RPESFAIYKR SRADGPWEPY QFYSASCQKT YGRPEGQYLR
   181  PGEDERVAFC TSEFSDISPL SGGNVAFSTL EGRPSAYNFE ESPGLQEWVT STELLISLDR
   241  LNTFGDDIFK DPKVLQSYYY AVSDFSVGGR CKCNGHASEC GPDVAGQLAC RCQHNTTGTD
   301  CERCLPFFQD RPWARGTAEA AHECLPCNCS GRSEECTFDR ELFRSTGHGG RCHHCRDHTA
   361  GPHCERCQEN FYHWDPRMPC QPCDCQSAGS LHLQCDDTGT CACKPTVTGW KCDRCLPGFH
   421  SLSEGGCRPC TCNPAGSLDT CDPRSGRCPC KENVEGNLCD RCRPGTFNLQ PHNPAGCSSC
   481  FCYGHSKVCA STAQFQVHHI LSDFHQGAEG WWARSVGGSE HPPQWSPNGV LLSPEDEEEL
   541  TAPEKFLGDQ RFSYGQPLIL TFRVPPGDSP LPVQLRLEGT GLALSLRHSS LSGPQDAGHP
   601  REVELRFHLQ ETSEDVAPPL PPFHFQRLLA NLTSLRLRVS PGPSPAGPVF LTEVRLTSAR
   661  PGLSPPASWV EICSCPTGYT GQFCESCAPG YKREMPQGGP YASCVPCTCN QHGTCDPNTG
   721  ICVCSHHTEG PSCERCLPGF YGNPFAGQAD DCQPCPCPGQ SACTTIPESR EVVCTHCPPG
   781  QRGRRCEVCD DGFFGDPLGL FGHPQPCHQC QCSGNVDPNA VGNCDPLSGH CLRCLHNTTG
   841  DHCEHCQEGF YGSALAPRPA DKCMPCSCHP QGSVSEQMPC DPVTGQCSCL PHVTARDCSR
   901  CYPGFFDLQP GRGCRSCKCH PLGSQEDQCH PKTGQCTCRP GVTGQACDRC QLGFFGFSIK
   961  GCRACRCSPL GAASAQCHEN GTCVCRPGFE GYKCDRCHDN FFLTADGTHC QQCPSCYALV
  1021  KEEAAKLKAR LTLTEGWLQG SDCGSPWGPL DILLGEAPRG DVYQGHHLLP GAREAFLEQM
  1081  MSLEGAVKAA REQLQRLNKG ARCAQAGSQK TCTQLADLEA VLESSEEEIL HAAAILASLE
  1141  IPQEGPSQPT KWSHLATEAR ALARSHRDTA TKIAATAWRA LLASNTSYAL LWNLLEGRVA
  1201  LETQRDLEDR YQEVQAAQKA LRTAVAEVLP EAESVLATVQ QVGADTAPYL ALLASPGALP
  1261  QKSRAEDLGL KAKALEKTVA SWQHMATEAA RTLQTAAQAT LRQTEPLTKL HQEARAALTQ
  1321  ASSSVQAATV TVMGARTLLA DLEGMKLQFP RPKDQAALQR KADSVSDRLL ADTRKKTKQA
  1381  ERMLGNAAPL SSSAKKKGRE AEVLAKDSAK LAKALLRERK QAHRRASRLT SQTQATLQQA
  1441  SQQVLASEAR RQELEEAERV GAGLSEMEQQ IRESRISLEK DIETLSELLA RLGSLDTHQA
  1501  PAQALNETQW ALERLRLQLG SPGSLQRKLS LLEQESQQQE LQIQGFESDL AEIRADKQNL
  1561  EAILHSLPEN CASWQ

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against LAMC3 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability
Secreted
Secreted
Yes
Transmembrane segments
0
Mean surface accessibility (rSASA)
0.34
Highest tissue expression
46 nTPM

Expression across tissuesHPA

Tissue

  • placenta: 46 nTPM
  • lung: 17 nTPM
  • cervix: 16 nTPM
  • testis: 14 nTPM
  • urinary bladder: 11 nTPM
  • adrenal gland: 9.7 nTPM

Single-cell type

  • peritubular myoid cells: 772 nCPM
  • leydig cells: 301 nCPM
  • pericytes: 128 nCPM
  • endometrial stromal cells: 120 nCPM
  • fibroblasts: 80 nCPM
  • granulosa cells: 32 nCPM

Immune cell

  • neutrophil: 0.6 nTPM
  • basophil: 0.2 nTPM
  • memory B-cell: 0.1 nTPM
  • classical monocyte: 0 nTPM
  • eosinophil: 0 nTPM
  • gdT-cell: 0 nTPM

Brain region

  • choroid plexus: 4.4 nTPM
  • white matter: 4.4 nTPM
  • basal ganglia: 4 nTPM
  • cerebral cortex: 4 nTPM
  • thalamus: 3.7 nTPM
  • medulla oblongata: 3.3 nTPM

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about LAMC3.

Disease | AllUniProt

Conditions LAMC3 is implicated in, by any mechanism.

  • Cortical malformations occipital (OCCM) MIM:614115

Disease | GeneticClinVar

105 pathogenic / likely-pathogenic of 1,824 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)
0.84
gnomAD pLI
0
gnomAD missense Z
-0.43
DepMap mean gene effect
-0.17
DepMap dependency class
selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

Molecular functions

Cellular components

Protein domainsUniProt · Pfam · InterPro

KeywordsUniProt

Antibody and autoantibody relevanceSeroatlas analysis

Seroatlas reads LAMC3 as an antibody target. Whether an autoantibody or antibody against LAMC3 could matter depends on whether native LAMC3 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.

LAMC3 is annotated as secreted, so native LAMC3 circulates and is directly accessible to antibodies. Secreted and cell-surface proteins are the autoantibody targets most likely to act like drugs, blocking or depleting the native protein.

Annotation status

The present source text does not explicitly label LAMC3 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.

Canonical record: https://seroatlas.com/gene/LAMC3. Study-independent annotations aggregated from UniProt, Human Protein Atlas, PubMed, IEDB, Pfam, InterPro, Gene Ontology, AlphaFold, gnomAD, DepMap, ClinVar, TCGA. Catalog release seroatlas-reviewed-human-uniprot-20260313.

Seroatlas is the reference for exploring autoantibody and antibody serology at the human-protein level: the autoreactome and human serome, multiplex serology (HuProt, HuScan, VirScan, PhIP-Seq).

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