P24043 (LAMA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Laminin subunit alpha-2

Alternative name(s):
Laminin M chain
Laminin-12 subunit alpha
Laminin-2 subunit alpha
Laminin-4 subunit alpha
Merosin heavy chain

Gene names

Name:	LAMA2
Synonyms:	LAMM

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	3122 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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-2 is a subunit of laminin-2 (laminin-211 or merosin), laminin-4 (laminin-221 or S-merosin) and laminin-12 (laminin-213). Interacts with FBLN1, FBLN2 and NID2.
Subcellular location	Secreted › extracellular space › extracellular matrix › basement membrane. Note: Major component.
Tissue specificity	Placenta, striated muscle, peripheral nerve, cardiac muscle, pancreas, lung, spleen, kidney, adrenal gland, skin, testis, meninges, choroid plexus, and some other regions of the brain; not in liver, thymus and bone.
Domain	The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure. Domains VI, IV and G are globular.
Involvement in disease	Merosin-deficient congenital muscular dystrophy 1A (MDC1A) [MIM:607855]: Characterized by difficulty walking, hypotonia, proximal weakness, hyporeflexia, and white matter hypodensity on MRI. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.11
Sequence similarities	Contains 17 laminin EGF-like domains. Contains 5 laminin G-like domains. Contains 2 laminin IV type A domains. Contains 1 laminin N-terminal domain.
Sequence caution	The sequence AAA63215.1 differs from that shown. Reason: Frameshift at position 3098. The sequence AAB18388.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAA81394.1 differs from that shown. Reason: Frameshift at position 3098.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Basement membrane Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Disease	Congenital muscular dystrophy Disease mutation
Domain	Coiled coil Laminin EGF-like domain Repeat Signal
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Inferred from electronic annotation. Source: Compara cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW muscle organ development Traceable author statement PubMed 7550355. Source: ProtInc positive regulation of synaptic transmission, cholinergic Inferred from electronic annotation. Source: Compara regulation of cell adhesion Inferred from electronic annotation. Source: InterPro regulation of cell migration Inferred from electronic annotation. Source: InterPro regulation of embryonic development Inferred from electronic annotation. Source: InterPro
Cellular_component	basement membrane Inferred from direct assay PubMed 14557481PubMed 2099832. Source: UniProtKB laminin-1 complex Inferred from electronic annotation. Source: InterPro sarcolemma Inferred from electronic annotation. Source: Compara
Molecular_function	structural molecule activity Traceable author statement Ref.5. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Chain	23 – 3122	3100	Laminin subunit alpha-2		PRO_0000017056
Regions
	Domain	35 – 286	252	Laminin N-terminal
	Domain	287 – 343	57	Laminin EGF-like 1
	Domain	344 – 413	70	Laminin EGF-like 2
	Domain	414 – 468	55	Laminin EGF-like 3
	Domain	469 – 517	49	Laminin EGF-like 4
	Domain	518 – 527	10	Laminin EGF-like 5; first part
	Domain	531 – 723	193	Laminin IV type A 1
	Domain	724 – 756	33	Laminin EGF-like 5; second part
	Domain	757 – 806	50	Laminin EGF-like 6
	Domain	807 – 864	58	Laminin EGF-like 7
	Domain	865 – 917	53	Laminin EGF-like 8
	Domain	918 – 966	49	Laminin EGF-like 9
	Domain	967 – 1013	47	Laminin EGF-like 10
	Domain	1014 – 1059	46	Laminin EGF-like 11
	Domain	1060 – 1105	46	Laminin EGF-like 12
	Domain	1106 – 1165	60	Laminin EGF-like 13
	Domain	1166 – 1175	10	Laminin EGF-like 14; first part
	Domain	1176 – 1379	204	Laminin IV type A 2
	Domain	1380 – 1419	40	Laminin EGF-like 14; second part
	Domain	1420 – 1468	49	Laminin EGF-like 15
	Domain	1469 – 1526	58	Laminin EGF-like 16
	Domain	1527 – 1573	47	Laminin EGF-like 17
	Domain	2145 – 2328	184	Laminin G-like 1
	Domain	2340 – 2521	182	Laminin G-like 2
	Domain	2526 – 2710	185	Laminin G-like 3
	Domain	2763 – 2934	172	Laminin G-like 4
	Domain	2939 – 3110	172	Laminin G-like 5
	Region	1574 – 2144	571	Domain II and I
	Coiled coil	1630 – 2150	521	Potential
Amino acid modifications
	Glycosylation	55	1	N-linked (GlcNAc...) Potential
	Glycosylation	89	1	N-linked (GlcNAc...) Potential
	Glycosylation	303	1	N-linked (GlcNAc...) Potential
	Glycosylation	363	1	N-linked (GlcNAc...) Ref.6
	Glycosylation	380	1	N-linked (GlcNAc...) Potential
	Glycosylation	470	1	N-linked (GlcNAc...) Potential
	Glycosylation	746	1	N-linked (GlcNAc...) Potential
	Glycosylation	1061	1	N-linked (GlcNAc...) Potential
	Glycosylation	1597	1	N-linked (GlcNAc...) Potential
	Glycosylation	1614	1	N-linked (GlcNAc...) Potential
	Glycosylation	1700	1	N-linked (GlcNAc...) Potential
	Glycosylation	1810	1	N-linked (GlcNAc...) Potential
	Glycosylation	1901	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	1916	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	1920	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	2017	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	2028	1	N-linked (GlcNAc...) Potential
	Glycosylation	2045	1	N-linked (GlcNAc...) Potential
	Glycosylation	2126	1	N-linked (GlcNAc...) Potential
	Glycosylation	2240	1	N-linked (GlcNAc...) Potential
	Glycosylation	2360	1	N-linked (GlcNAc...) Potential
	Glycosylation	2435	1	N-linked (GlcNAc...) Potential
	Glycosylation	2478	1	N-linked (GlcNAc...) Potential
	Glycosylation	2551	1	N-linked (GlcNAc...) Potential
	Glycosylation	2558	1	N-linked (GlcNAc...) Potential
	Glycosylation	2648	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	2868	1	N-linked (GlcNAc...) Potential
	Glycosylation	2893	1	N-linked (GlcNAc...) Potential
	Disulfide bond	287 ↔ 296		By similarity
	Disulfide bond	289 ↔ 307		By similarity
	Disulfide bond	309 ↔ 318		By similarity
	Disulfide bond	321 ↔ 341		By similarity
	Disulfide bond	344 ↔ 353		By similarity
	Disulfide bond	346 ↔ 378		By similarity
	Disulfide bond	381 ↔ 390		By similarity
	Disulfide bond	393 ↔ 411		By similarity
	Disulfide bond	414 ↔ 426		By similarity
	Disulfide bond	416 ↔ 442		By similarity
	Disulfide bond	444 ↔ 453		By similarity
	Disulfide bond	456 ↔ 466		By similarity
	Disulfide bond	469 ↔ 482		By similarity
	Disulfide bond	471 ↔ 486		By similarity
	Disulfide bond	488 ↔ 497		By similarity
	Disulfide bond	500 ↔ 515		By similarity
	Disulfide bond	757 ↔ 766		By similarity
	Disulfide bond	759 ↔ 773		By similarity
	Disulfide bond	776 ↔ 785		By similarity
	Disulfide bond	788 ↔ 804		By similarity
	Disulfide bond	807 ↔ 822		By similarity
	Disulfide bond	809 ↔ 832		By similarity
	Disulfide bond	835 ↔ 844		By similarity
	Disulfide bond	847 ↔ 862		By similarity
	Disulfide bond	865 ↔ 879		By similarity
	Disulfide bond	867 ↔ 886		By similarity
	Disulfide bond	889 ↔ 898		By similarity
	Disulfide bond	901 ↔ 915		By similarity
	Disulfide bond	918 ↔ 930		By similarity
	Disulfide bond	920 ↔ 937		By similarity
	Disulfide bond	939 ↔ 948		By similarity
	Disulfide bond	951 ↔ 964		By similarity
	Disulfide bond	967 ↔ 979		By similarity
	Disulfide bond	969 ↔ 985		By similarity
	Disulfide bond	987 ↔ 996		By similarity
	Disulfide bond	999 ↔ 1011		By similarity
	Disulfide bond	1014 ↔ 1023		By similarity
	Disulfide bond	1016 ↔ 1030		By similarity
	Disulfide bond	1032 ↔ 1041		By similarity
	Disulfide bond	1044 ↔ 1057		By similarity
	Disulfide bond	1060 ↔ 1072		By similarity
	Disulfide bond	1062 ↔ 1079		By similarity
	Disulfide bond	1081 ↔ 1090		By similarity
	Disulfide bond	1093 ↔ 1103		By similarity
	Disulfide bond	1106 ↔ 1118		By similarity
	Disulfide bond	1108 ↔ 1134		By similarity
	Disulfide bond	1136 ↔ 1145		By similarity
	Disulfide bond	1148 ↔ 1163		By similarity
	Disulfide bond	1420 ↔ 1429		By similarity
	Disulfide bond	1422 ↔ 1436		By similarity
	Disulfide bond	1439 ↔ 1448		By similarity
	Disulfide bond	1451 ↔ 1466		By similarity
	Disulfide bond	1469 ↔ 1484		By similarity
	Disulfide bond	1471 ↔ 1494		By similarity
	Disulfide bond	1497 ↔ 1506		By similarity
	Disulfide bond	1509 ↔ 1524		By similarity
	Disulfide bond	1527 ↔ 1539		By similarity
	Disulfide bond	1529 ↔ 1546		By similarity
	Disulfide bond	1548 ↔ 1557		By similarity
	Disulfide bond	1560 ↔ 1571		By similarity
	Disulfide bond	1574		Interchain Probable
	Disulfide bond	1578		Interchain Probable
	Disulfide bond	2302 ↔ 2328		By similarity
	Disulfide bond	2495 ↔ 2521		By similarity
	Disulfide bond	2683 ↔ 2710		By similarity
	Disulfide bond	2909 ↔ 2934		By similarity
Natural variations
	Natural variant	96	1	R → S. Corresponds to variant rs34626728 [ dbSNP | Ensembl ].		VAR_047713
	Natural variant	240	1	Y → H. Corresponds to variant rs3778142 [ dbSNP | Ensembl ].		VAR_047714
	Natural variant	527	1	C → Y in MDC1A. Ref.11		VAR_015743
	Natural variant	545	1	L → Q. Ref.8		VAR_004165
	Natural variant	619	1	R → H. Ref.8 Corresponds to variant rs3816665 [ dbSNP | Ensembl ].		VAR_004166
	Natural variant	644	1	H → D. Corresponds to variant rs35879899 [ dbSNP | Ensembl ].		VAR_047715
	Natural variant	862	1	C → R in MDC1A. Ref.11		VAR_015744
	Natural variant	919	1	R → L. Ref.8 Corresponds to variant rs35277491 [ dbSNP | Ensembl ].		VAR_004167
	Natural variant	1138	1	V → M. Corresponds to variant rs2306942 [ dbSNP | Ensembl ].		VAR_047716
	Natural variant	1160	1	P → A in a breast cancer sample; somatic mutation. Ref.12		VAR_035819
	Natural variant	1205	1	T → A. Corresponds to variant rs35889149 [ dbSNP | Ensembl ].		VAR_047717
	Natural variant	1561	1	K → Q. Corresponds to variant rs4143752 [ dbSNP | Ensembl ].		VAR_047718
	Natural variant	1945	1	A → T. Corresponds to variant rs3828736 [ dbSNP | Ensembl ].		VAR_047719
	Natural variant	2564	1	L → P in MDC1A. Ref.10		VAR_015745
	Natural variant	2586	1	Y → H. Ref.8		VAR_004168
	Natural variant	2587	1	A → V. Ref.1 Ref.2 Ref.5 Corresponds to variant rs6569605 [ dbSNP | Ensembl ].		VAR_047720
	Natural variant	2614	1	E → K. Ref.8		VAR_004169
	Natural variant	2636	1	T → A. Corresponds to variant rs2244008 [ dbSNP | Ensembl ].		VAR_047721
	Natural variant	3029	1	T → A. Corresponds to variant rs34551216 [ dbSNP | Ensembl ].		VAR_047722
Experimental info
	Sequence conflict	588	1	A → R in AAB18388. Ref.2
	Sequence conflict	1740	1	A → D Ref.4
	Sequence conflict	1827	1	Q → G Ref.4
	Sequence conflict	1981	1	A → V in AAA63215. Ref.5
	Sequence conflict	2437	1	S → Y in AAB18388. Ref.2
	Sequence conflict	2624	1	H → R in AAA63215. Ref.5
	Sequence conflict	2807	1	R → A in CAA81394. Ref.1
	Sequence conflict	2807	1	R → A in AAB18388. Ref.2
	Sequence conflict	2969	1	R → A in CAA81394. Ref.1
	Sequence conflict	2969	1	R → A in AAB18388. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P24043 [UniParc]. Last modified November 25, 2008. Version 4. Checksum: E2C13BD6FC1B7BAC	FASTA	3,122	343,905
	10 20 30 40 50 60 MPGAAGVLLL LLLSGGLGGV QAQRPQQQRQ SQAHQQRGLF PAVLNLASNA LITTNATCGE 70 80 90 100 110 120 KGPEMYCKLV EHVPGQPVRN PQCRICNQNS SNPNQRHPIT NAIDGKNTWW QSPSIKNGIE 130 140 150 160 170 180 YHYVTITLDL QQVFQIAYVI VKAANSPRPG NWILERSLDD VEYKPWQYHA VTDTECLTLY 190 200 210 220 230 240 NIYPRTGPPS YAKDDEVICT SFYSKIHPLE NGEIHISLIN GRPSADDPSP ELLEFTSARY 250 260 270 280 290 300 IRLRFQRIRT LNADLMMFAH KDPREIDPIV TRRYYYSVKD ISVGGMCICY GHARACPLDP 310 320 330 340 350 360 ATNKSRCECE HNTCGDSCDQ CCPGFHQKPW RAGTFLTKTE CEACNCHGKA EECYYDENVA 370 380 390 400 410 420 RRNLSLNIRG KYIGGGVCIN CTQNTAGINC ETCTDGFFRP KGVSPNYPRP CQPCHCDPIG 430 440 450 460 470 480 SLNEVCVKDE KHARRGLAPG SCHCKTGFGG VSCDRCARGY TGYPDCKACN CSGLGSKNED 490 500 510 520 530 540 PCFGPCICKE NVEGGDCSRC KSGFFNLQED NWKGCDECFC SGVSNRCQSS YWTYGKIQDM 550 560 570 580 590 600 SGWYLTDLPG RIRVAPQQDD LDSPQQISIS NAEARQALPH SYYWSAPAPY LGNKLPAVGG 610 620 630 640 650 660 QLTFTISYDL EEEEEDTERV LQLMIILEGN DLSISTAQDE VYLHPSEEHT NVLLLKEESF 670 680 690 700 710 720 TIHGTHFPVR RKEFMTVLAN LKRVLLQITY SFGMDAIFRL SSVNLESAVS YPTDGSIAAA 730 740 750 760 770 780 VEVCQCPPGY TGSSCESCWP RHRRVNGTIF GGICEPCQCF GHAESCDDVT GECLNCKDHT 790 800 810 820 830 840 GGPYCDKCLP GFYGEPTKGT SEDCQPCACP LNIPSNNFSP TCHLDRSLGL ICDGCPVGYT 850 860 870 880 890 900 GPRCERCAEG YFGQPSVPGG SCQPCQCNDN LDFSIPGSCD SLSGSCLICK PGTTGRYCEL 910 920 930 940 950 960 CADGYFGDAV DAKNCQPCRC NAGGSFSEVC HSQTGQCECR ANVQGQRCDK CKAGTFGLQS 970 980 990 1000 1010 1020 ARGCVPCNCN SFGSKSFDCE ESGQCWCQPG VTGKKCDRCA HGYFNFQEGG CTACECSHLG 1030 1040 1050 1060 1070 1080 NNCDPKTGRC ICPPNTIGEK CSKCAPNTWG HSITTGCKAC NCSTVGSLDF QCNVNTGQCN 1090 1100 1110 1120 1130 1140 CHPKFSGAKC TECSRGHWNY PRCNLCDCFL PGTDATTCDS ETKKCSCSDQ TGQCTCKVNV 1150 1160 1170 1180 1190 1200 EGIHCDRCRP GKFGLDAKNP LGCSSCYCFG TTTQCSEAKG LIRTWVTLKA EQTILPLVDE 1210 1220 1230 1240 1250 1260 ALQHTTTKGI VFQHPEIVAH MDLMREDLHL EPFYWKLPEQ FEGKKLMAYG GKLKYAIYFE 1270 1280 1290 1300 1310 1320 AREETGFSTY NPQVIIRGGT PTHARIIVRH MAAPLIGQLT RHEIEMTEKE WKYYGDDPRV 1330 1340 1350 1360 1370 1380 HRTVTREDFL DILYDIHYIL IKATYGNFMR QSRISEISME VAEQGRGTTM TPPADLIEKC 1390 1400 1410 1420 1430 1440 DCPLGYSGLS CEACLPGFYR LRSQPGGRTP GPTLGTCVPC QCNGHSSLCD PETSICQNCQ 1450 1460 1470 1480 1490 1500 HHTAGDFCER CALGYYGIVK GLPNDCQQCA CPLISSSNNF SPSCVAEGLD DYRCTACPRG 1510 1520 1530 1540 1550 1560 YEGQYCERCA PGYTGSPGNP GGSCQECECD PYGSLPVPCD PVTGFCTCRP GATGRKCDGC 1570 1580 1590 1600 1610 1620 KHWHAREGWE CVFCGDECTG LLLGDLARLE QMVMSINLTG PLPAPYKMLY GLENMTQELK 1630 1640 1650 1660 1670 1680 HLLSPQRAPE RLIQLAEGNL NTLVTEMNEL LTRATKVTAD GEQTGQDAER TNTRAKSLGE 1690 1700 1710 1720 1730 1740 FIKELARDAE AVNEKAIKLN ETLGTRDEAF ERNLEGLQKE IDQMIKELRR KNLETQKEIA 1750 1760 1770 1780 1790 1800 EDELVAAEAL LKKVKKLFGE SRGENEEMEK DLREKLADYK NKVDDAWDLL REATDKIREA 1810 1820 1830 1840 1850 1860 NRLFAVNQKN MTALEKKKEA VESGKRQIEN TLKEGNDILD EANRLADEIN SIIDYVEDIQ 1870 1880 1890 1900 1910 1920 TKLPPMSEEL NDKIDDLSQE IKDRKLAEKV SQAESHAAQL NDSSAVLDGI LDEAKNISFN 1930 1940 1950 1960 1970 1980 ATAAFKAYSN IKDYIDEAEK VAKEAKDLAH EATKLATGPR GLLKEDAKGC LQKSFRILNE 1990 2000 2010 2020 2030 2040 AKKLANDVKE NEDHLNGLKT RIENADARNG DLLRTLNDTL GKLSAIPNDT AAKLQAVKDK 2050 2060 2070 2080 2090 2100 ARQANDTAKD VLAQITELHQ NLDGLKKNYN KLADSVAKTN AVVKDPSKNK IIADADATVK 2110 2120 2130 2140 2150 2160 NLEQEADRLI DKLKPIKELE DNLKKNISEI KELINQARKQ ANSIKVSVSS GGDCIRTYKP 2170 2180 2190 2200 2210 2220 EIKKGSYNNI VVNVKTAVAD NLLFYLGSAK FIDFLAIEMR KGKVSFLWDV GSGVGRVEYP 2230 2240 2250 2260 2270 2280 DLTIDDSYWY RIVASRTGRN GTISVRALDG PKASIVPSTH HSTSPPGYTI LDVDANAMLF 2290 2300 2310 2320 2330 2340 VGGLTGKLKK ADAVRVITFT GCMGETYFDN KPIGLWNFRE KEGDCKGCTV SPQVEDSEGT 2350 2360 2370 2380 2390 2400 IQFDGEGYAL VSRPIRWYPN ISTVMFKFRT FSSSALLMYL ATRDLRDFMS VELTDGHIKV 2410 2420 2430 2440 2450 2460 SYDLGSGMAS VVSNQNHNDG KWKSFTLSRI QKQANISIVD IDTNQEENIA TSSSGNNFGL 2470 2480 2490 2500 2510 2520 DLKADDKIYF GGLPTLRNLS MKARPEVNLK KYSGCLKDIE ISRTPYNILS SPDYVGVTKG 2530 2540 2550 2560 2570 2580 CSLENVYTVS FPKPGFVELS PVPIDVGTEI NLSFSTKNES GIILLGSGGT PAPPRRKRRQ 2590 2600 2610 2620 2630 2640 TGQAYYAILL NRGRLEVHLS TGARTMRKIV IRPEPNLFHD GREHSVHVER TRGIFTVQVD 2650 2660 2670 2680 2690 2700 ENRRYMQNLT VEQPIEVKKL FVGGAPPEFQ PSPLRNIPPF EGCIWNLVIN SVPMDFARPV 2710 2720 2730 2740 2750 2760 SFKNADIGRC AHQKLREDED GAAPAEIVIQ PEPVPTPAFP TPTPVLTHGP CAAESEPALL 2770 2780 2790 2800 2810 2820 IGSKQFGLSR NSHIAIAFDD TKVKNRLTIE LEVRTEAESG LLFYMARINH ADFATVQLRN 2830 2840 2850 2860 2870 2880 GLPYFSYDLG SGDTHTMIPT KINDGQWHKI KIMRSKQEGI LYVDGASNRT ISPKKADILD 2890 2900 2910 2920 2930 2940 VVGMLYVGGL PINYTTRRIG PVTYSIDGCV RNLHMAEAPA DLEQPTSSFH VGTCFANAQR 2950 2960 2970 2980 2990 3000 GTYFDGTGFA KAVGGFKVGL DLLVEFEFRT TTTTGVLLGI SSQKMDGMGI EMIDEKLMFH 3010 3020 3030 3040 3050 3060 VDNGAGRFTA VYDAGVPGHL CDGQWHKVTA NKIKHRIELT VDGNQVEAQS PNPASTSADT 3070 3080 3090 3100 3110 3120 NDPVFVGGFP DDLKQFGLTT SIPFRGCIRS LKLTKGTGKP LEVNFAKALE LRGVQPVSCP AN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human laminin M chain (merosin): complete primary structure, chromosomal assignment, and expression of the M and A chain in human fetal tissues." Vuolteenaho R., Nissinen M., Sainio K., Byers M., Eddy R., Hirvonen H., Shows T.B., Sariola H., Engvall E., Tryggvason K. J. Cell Biol. 124:381-394(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-2587. Tissue: Placenta.
[2]	"Structure of the human laminin alpha2-chain gene (LAMA2), which is affected in congenital muscular dystrophy." Zhang X., Vuolteenaho R., Tryggvason K. J. Biol. Chem. 271:27664-27669(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-2587.
[3]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Human laminin M chain: epitope analysis of its monoclonal antibodies by immunoscreening of cDNA clones and tissue expression." Hori H., Kanamori T., Mizuta T., Yamaguchi N., Liu Y., Nagai Y. J. Biochem. 116:1212-1219(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1360-3122.
[5]	"Merosin, a tissue-specific basement membrane protein, is a laminin-like protein." Ehrig K., Leivo I., Argraves W.S., Ruoslahti E., Engvall E. Proc. Natl. Acad. Sci. U.S.A. 87:3264-3268(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1981-3122, PARTIAL PROTEIN SEQUENCE, VARIANT VAL-2587. Tissue: Placenta.
[6]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-363, MASS SPECTROMETRY. Tissue: Plasma.
[7]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1901; ASN-1916; ASN-1920; ASN-2017 AND ASN-2648, MASS SPECTROMETRY. Tissue: Liver.
[8]	"Novel single base polymorphisms and rare sequence variants in the laminin 2-chain coding region detected by RNA/SSCP analysis." Panicker S.G., Mendell J.T., Chen L., Feng B., Sahenk Z., Marzluf G.A., Amato A.A., Mendell J.R. Hum. Mutat. 13:174-174(1999) Cited for: VARIANTS GLN-545; HIS-619; LEU-919; HIS-2586 AND LYS-2614.
[9]	Erratum Panicker S.G., Mendell J.T., Chen L., Feng B., Sahenk Z., Marzluf G.A., Amato A.A., Mendell J.R. Hum. Mutat. 13:340-340(1999)
[10]	"Congenital muscular dystrophy with primary partial laminin alpha-2 chain deficiency: molecular study." He Y., Jones K.J., Vignier N., Morgan G., Chevallay M., Barois A., Estournet-Mathiaud B., Hori H., Mizuta T., Tome F.M.S., North K.N., Guicheney P. Neurology 57:1319-1322(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MDC1A PRO-2564.
[11]	"Clinical and molecular study in congenital muscular dystrophy with partial laminin alpha-2 (LAMA2) deficiency." Tezak Z., Prandini P., Boscaro M., Marin A., Devaney J., Marino M., Fanin M., Trevisan C.P., Park J., Tyson W., Finkel R., Garcia C., Angelini C., Hoffman E.P., Pegoraro E. Hum. Mutat. 21:103-111(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MDC1A TYR-527 AND ARG-862.
[12]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-1160.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z26653 mRNA. Translation: CAA81394.1. Frameshift. U66796 , U66733, U66734, U66735, U66736, U66737, U66738, U66739, U66740, U66741, U66742, U66743, U66745, U66746, U66747, U66748, U66749, U66750, U66751, U66752, U66753, U66754, U66755, U66756, U66757, U66758, U66759, U66760, U66761, U66762, U66763, U66764, U66765, U66766, U66768, U66769, U66770, U66771, U66772, U66773, U66774, U66775, U66776, U66777, U66778, U66779, U66780, U66781, U66782, U66783, U66784, U66785, U66786, U66787, U66788, U66789, U66790, U66791, U66792, U66793, U66794, U66795 Genomic DNA. Translation: AAB18388.1. Sequence problems. AL583853 , AL356124, AL445439, AL513527, AL590613, AL669984 Genomic DNA. Translation: CAH70492.1. AL590613 , AL356124, AL445439, AL513527, AL583853, AL669984 Genomic DNA. Translation: CAH70771.1. AL445439 , AL356124, AL513527, AL583853, AL590613, AL669984 Genomic DNA. Translation: CAH72952.1. AL513527 , AL356124, AL445439, AL583853, AL590613, AL669984 Genomic DNA. Translation: CAI15185.1. AL669984 , AL356124, AL445439, AL513527, AL583853, AL590613 Genomic DNA. Translation: CAI16682.1. AL356124 , AL445439, AL513527, AL583853, AL590613, AL669984 Genomic DNA. Translation: CAI22470.1. AL589927 Genomic DNA. No translation available. M59832 mRNA. Translation: AAA63215.1. Frameshift.
IPI	IPI00873889.
PIR	MMHUMH. PX0082.
RefSeq	NP_000417.2. NM_000426.3. NP_001073291.1. NM_001079823.1.
UniGene	Hs.200841.
3D structure databases
ProteinModelPortal	P24043.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-42562N.
IntAct	P24043. 2 interactions.
MINT	MINT-2635209.
STRING	9606.ENSP00000400365.
PTM databases
PhosphoSite	P24043.
Polymorphism databases
DMDM	215274259.
Proteomic databases
PaxDb	P24043.
PRIDE	P24043.
Protocols and materials databases
DNASU	3908.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000421865; ENSP00000400365; ENSG00000196569.
GeneID	3908.
KEGG	hsa:3908.
UCSC	uc003qbn.3. human.
Organism-specific databases
CTD	3908.
GeneCards	GC06P129246.
HGNC	HGNC:6482. LAMA2.
HPA	CAB040310.
MIM	156225. gene. 607855. phenotype.
neXtProt	NX_P24043.
Orphanet	258. Congenital muscular dystrophy type 1A.
PharmGKB	PA30271.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0419.
HOGENOM	HOG000293201.
HOVERGEN	HBG052298.
KO	K05637.
OMA	NCNSFGS.
OrthoDB	EOG4RFKRM.
PhylomeDB	P24043.
Enzyme and pathway databases
Pathway_Interaction_DB	a6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling. amb2_neutrophils_pathway. amb2 Integrin signaling.
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	P24043.
Bgee	P24043.
CleanEx	HS_LAMA2.
Genevestigator	P24043.
GermOnline	ENSG00000196569. Homo sapiens.
Family and domain databases
Gene3D	2.60.120.200. 5 hits. 2.60.120.260. 2 hits.
InterPro	IPR008985. ConA-like_lec_gl_sf. IPR013320. ConA-like_subgrp. IPR002049. EGF_laminin. IPR008979. Galactose-bd-like. IPR018031. Laminin_B_subgr. IPR000034. Laminin_B_type_IV. IPR001791. Laminin_G. IPR009254. Laminin_I. IPR010307. Laminin_II. IPR008211. Laminin_N. [Graphical view]
Pfam	PF00052. Laminin_B. 2 hits. PF00053. Laminin_EGF. 17 hits. PF00054. Laminin_G_1. 4 hits. PF02210. Laminin_G_2. 1 hit. PF06008. Laminin_I. 1 hit. PF06009. Laminin_II. 1 hit. PF00055. Laminin_N. 1 hit. [Graphical view]
SMART	SM00180. EGF_Lam. 15 hits. SM00281. LamB. 2 hits. SM00282. LamG. 5 hits. SM00136. LamNT. 1 hit. [Graphical view]
SUPFAM	SSF49899. ConA_like_lec_gl. 5 hits.
PROSITE	PS00022. EGF_1. 11 hits. PS01186. EGF_2. 3 hits. PS01248. EGF_LAM_1. 14 hits. PS50027. EGF_LAM_2. 15 hits. PS50025. LAM_G_DOMAIN. 5 hits. PS51115. LAMININ_IVA. 2 hits. PS51117. LAMININ_NTER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	3908.
NextBio	15339.
SOURCE	Search...

Entry information

Entry name

LAMA2_HUMAN

Accession

Primary (citable) accession number: P24043
Secondary accession number(s): Q14736, Q5VUM2, Q93022

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	November 25, 2008
Last modified:	May 29, 2013
This is version 145 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.