LAMA2

Protein identityUniProt · HPA

UniProt accession

P24043

Gene

LAMA2

Ensembl

ENSG00000196569

Chromosome

6

Canonical length

3122 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

Laminin, an extracellular protein, is a major component of the basement membrane. It is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. It is composed of three subunits, alpha, beta, and gamma, which are bound to each other by disulfide bonds into a cross-shaped molecule. This gene encodes the alpha 2 chain, which constitutes one of the subunits of laminin 2 (merosin) and laminin 4 (s-merosin). Mutations in this gene have been identified as the cause of congenital merosin-deficient muscular dystrophy. Two transcript variants encoding different proteins have been found for this gene. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

3122 residues, UniProt reviewed canonical sequence.

>P24043|LAMA2
     1  MPGAAGVLLL LLLSGGLGGV QAQRPQQQRQ SQAHQQRGLF PAVLNLASNA LITTNATCGE
    61  KGPEMYCKLV EHVPGQPVRN PQCRICNQNS SNPNQRHPIT NAIDGKNTWW QSPSIKNGIE
   121  YHYVTITLDL QQVFQIAYVI VKAANSPRPG NWILERSLDD VEYKPWQYHA VTDTECLTLY
   181  NIYPRTGPPS YAKDDEVICT SFYSKIHPLE NGEIHISLIN GRPSADDPSP ELLEFTSARY
   241  IRLRFQRIRT LNADLMMFAH KDPREIDPIV TRRYYYSVKD ISVGGMCICY GHARACPLDP
   301  ATNKSRCECE HNTCGDSCDQ CCPGFHQKPW RAGTFLTKTE CEACNCHGKA EECYYDENVA
   361  RRNLSLNIRG KYIGGGVCIN CTQNTAGINC ETCTDGFFRP KGVSPNYPRP CQPCHCDPIG
   421  SLNEVCVKDE KHARRGLAPG SCHCKTGFGG VSCDRCARGY TGYPDCKACN CSGLGSKNED
   481  PCFGPCICKE NVEGGDCSRC KSGFFNLQED NWKGCDECFC SGVSNRCQSS YWTYGKIQDM
   541  SGWYLTDLPG RIRVAPQQDD LDSPQQISIS NAEARQALPH SYYWSAPAPY LGNKLPAVGG
   601  QLTFTISYDL EEEEEDTERV LQLMIILEGN DLSISTAQDE VYLHPSEEHT NVLLLKEESF
   661  TIHGTHFPVR RKEFMTVLAN LKRVLLQITY SFGMDAIFRL SSVNLESAVS YPTDGSIAAA
   721  VEVCQCPPGY TGSSCESCWP RHRRVNGTIF GGICEPCQCF GHAESCDDVT GECLNCKDHT
   781  GGPYCDKCLP GFYGEPTKGT SEDCQPCACP LNIPSNNFSP TCHLDRSLGL ICDGCPVGYT
   841  GPRCERCAEG YFGQPSVPGG SCQPCQCNDN LDFSIPGSCD SLSGSCLICK PGTTGRYCEL
   901  CADGYFGDAV DAKNCQPCRC NAGGSFSEVC HSQTGQCECR ANVQGQRCDK CKAGTFGLQS
   961  ARGCVPCNCN SFGSKSFDCE ESGQCWCQPG VTGKKCDRCA HGYFNFQEGG CTACECSHLG
  1021  NNCDPKTGRC ICPPNTIGEK CSKCAPNTWG HSITTGCKAC NCSTVGSLDF QCNVNTGQCN
  1081  CHPKFSGAKC TECSRGHWNY PRCNLCDCFL PGTDATTCDS ETKKCSCSDQ TGQCTCKVNV
  1141  EGIHCDRCRP GKFGLDAKNP LGCSSCYCFG TTTQCSEAKG LIRTWVTLKA EQTILPLVDE
  1201  ALQHTTTKGI VFQHPEIVAH MDLMREDLHL EPFYWKLPEQ FEGKKLMAYG GKLKYAIYFE
  1261  AREETGFSTY NPQVIIRGGT PTHARIIVRH MAAPLIGQLT RHEIEMTEKE WKYYGDDPRV
  1321  HRTVTREDFL DILYDIHYIL IKATYGNFMR QSRISEISME VAEQGRGTTM TPPADLIEKC
  1381  DCPLGYSGLS CEACLPGFYR LRSQPGGRTP GPTLGTCVPC QCNGHSSLCD PETSICQNCQ
  1441  HHTAGDFCER CALGYYGIVK GLPNDCQQCA CPLISSSNNF SPSCVAEGLD DYRCTACPRG
  1501  YEGQYCERCA PGYTGSPGNP GGSCQECECD PYGSLPVPCD PVTGFCTCRP GATGRKCDGC
  1561  KHWHAREGWE CVFCGDECTG LLLGDLARLE QMVMSINLTG PLPAPYKMLY GLENMTQELK
  1621  HLLSPQRAPE RLIQLAEGNL NTLVTEMNEL LTRATKVTAD GEQTGQDAER TNTRAKSLGE
  1681  FIKELARDAE AVNEKAIKLN ETLGTRDEAF ERNLEGLQKE IDQMIKELRR KNLETQKEIA
  1741  EDELVAAEAL LKKVKKLFGE SRGENEEMEK DLREKLADYK NKVDDAWDLL REATDKIREA
  1801  NRLFAVNQKN MTALEKKKEA VESGKRQIEN TLKEGNDILD EANRLADEIN SIIDYVEDIQ
  1861  TKLPPMSEEL NDKIDDLSQE IKDRKLAEKV SQAESHAAQL NDSSAVLDGI LDEAKNISFN
  1921  ATAAFKAYSN IKDYIDEAEK VAKEAKDLAH EATKLATGPR GLLKEDAKGC LQKSFRILNE
  1981  AKKLANDVKE NEDHLNGLKT RIENADARNG DLLRTLNDTL GKLSAIPNDT AAKLQAVKDK
  2041  ARQANDTAKD VLAQITELHQ NLDGLKKNYN KLADSVAKTN AVVKDPSKNK IIADADATVK
  2101  NLEQEADRLI DKLKPIKELE DNLKKNISEI KELINQARKQ ANSIKVSVSS GGDCIRTYKP
  2161  EIKKGSYNNI VVNVKTAVAD NLLFYLGSAK FIDFLAIEMR KGKVSFLWDV GSGVGRVEYP
  2221  DLTIDDSYWY RIVASRTGRN GTISVRALDG PKASIVPSTH HSTSPPGYTI LDVDANAMLF
  2281  VGGLTGKLKK ADAVRVITFT GCMGETYFDN KPIGLWNFRE KEGDCKGCTV SPQVEDSEGT
  2341  IQFDGEGYAL VSRPIRWYPN ISTVMFKFRT FSSSALLMYL ATRDLRDFMS VELTDGHIKV
  2401  SYDLGSGMAS VVSNQNHNDG KWKSFTLSRI QKQANISIVD IDTNQEENIA TSSSGNNFGL
  2461  DLKADDKIYF GGLPTLRNLS MKARPEVNLK KYSGCLKDIE ISRTPYNILS SPDYVGVTKG
  2521  CSLENVYTVS FPKPGFVELS PVPIDVGTEI NLSFSTKNES GIILLGSGGT PAPPRRKRRQ
  2581  TGQAYYAILL NRGRLEVHLS TGARTMRKIV IRPEPNLFHD GREHSVHVER TRGIFTVQVD
  2641  ENRRYMQNLT VEQPIEVKKL FVGGAPPEFQ PSPLRNIPPF EGCIWNLVIN SVPMDFARPV
  2701  SFKNADIGRC AHQKLREDED GAAPAEIVIQ PEPVPTPAFP TPTPVLTHGP CAAESEPALL
  2761  IGSKQFGLSR NSHIAIAFDD TKVKNRLTIE LEVRTEAESG LLFYMARINH ADFATVQLRN
  2821  GLPYFSYDLG SGDTHTMIPT KINDGQWHKI KIMRSKQEGI LYVDGASNRT ISPKKADILD
  2881  VVGMLYVGGL PINYTTRRIG PVTYSIDGCV RNLHMAEAPA DLEQPTSSFH VGTCFANAQR
  2941  GTYFDGTGFA KAVGGFKVGL DLLVEFEFRT TTTTGVLLGI SSQKMDGMGI EMIDEKLMFH
  3001  VDNGAGRFTA VYDAGVPGHL CDGQWHKVTA NKIKHRIELT VDGNQVEAQS PNPASTSADT
  3061  NDPVFVGGFP DDLKQFGLTT SIPFRGCIRS LKLTKGTGKP LEVNFAKALE LRGVQPVSCP
  3121  AN

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against LAMA2 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

Highest tissue expression

139 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about LAMA2.

Disease | AllUniProt

Conditions LAMA2 is implicated in, by any mechanism.

• Merosin-deficient congenital muscular dystrophy 1A (MDC1A) MIM:607855
• Muscular dystrophy, limb-girdle, autosomal recessive 23 (LGMDR23) MIM:618138

Disease | GeneticClinVar

974 pathogenic / likely-pathogenic of 5,454 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• LAMA2-related muscular dystrophy
• Merosin deficient congenital muscular dystrophy
• Muscular dystrophy, limb-girdle, autosomal recessive 23
• LAMA2-related disorder
• Inborn genetic diseases

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)

0.73

gnomAD pLI

0

gnomAD missense Z

-0.03

DepMap mean gene effect

0.01

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

• axon guidance
• cell adhesion
• maintenance of blood-brain barrier
• muscle organ development
• positive regulation of cell adhesion
• positive regulation of integrin-mediated signaling pathway
• positive regulation of muscle cell differentiation
• positive regulation of synaptic transmission, cholinergic
• regulation of basement membrane organization
• regulation of cell migration
• regulation of embryonic development
• Schwann cell differentiation

Molecular functions

• signaling receptor binding
• structural molecule activity

Cellular components

• basement membrane
• dendritic spine
• extracellular matrix
• extracellular region
• neuromuscular junction
• protein complex involved in cell-matrix adhesion
• sarcolemma
• synaptic cleft

Protein domainsUniProt · Pfam · InterPro

• Laminin IV
• EGF-like domain
• Laminin G domain
• Laminin-type EGF domain
• Laminin, N-terminal
• Laminin alpha, domain I
• Laminin domain II
• Concanavalin A-like lectin/glucanase domain superfamily
• Laminin/Netrin Extracellular Matrix
• Laminin/attractin/netrin-like, EGF domain
• Laminin B (Domain IV)
• Laminin EGF domain
• Laminin G domain
• Laminin N-terminal (Domain VI)
• Laminin G domain
• Laminin Domain I
• Laminin Domain II
• Laminin/attractin EGF domain

KeywordsUniProt

• Basement membrane
• Cell adhesion
• Coiled coil
• Congenital muscular dystrophy
• Disulfide bond
• Extracellular matrix
• Glycoprotein
• Laminin EGF-like domain
• Limb-girdle muscular dystrophy
• Repeat
• Secreted
• Signal

InteractionsUniProt · HPA

Protein binding partners of LAMA2 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• FBLN1
• FBLN2
• NID2