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Protein

Laminin subunit alpha-3

Gene

LAMA3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.
Laminin-5 is thought to be involved in (1) cell adhesion via integrin alpha-3/beta-1 in focal adhesion and integrin alpha-6/beta-4 in hemidesmosomes, (2) signal transduction via tyrosine phosphorylation of pp125-FAK and p80, (3) differentiation of keratinocytes.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processCell adhesion

Enzyme and pathway databases

ReactomeiR-HSA-1474228 Degradation of the extracellular matrix
R-HSA-2022090 Assembly of collagen fibrils and other multimeric structures
R-HSA-2214320 Anchoring fibril formation
R-HSA-3000157 Laminin interactions
R-HSA-3000171 Non-integrin membrane-ECM interactions
R-HSA-3000178 ECM proteoglycans
R-HSA-446107 Type I hemidesmosome assembly
R-HSA-8874081 MET activates PTK2 signaling
SIGNORiQ16787

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit alpha-3
Alternative name(s):
Epiligrin 170 kDa subunit
Short name:
E170
Epiligrin subunit alpha
Kalinin subunit alpha
Laminin-5 subunit alpha
Laminin-6 subunit alpha
Laminin-7 subunit alpha
Nicein subunit alpha
Gene namesi
Name:LAMA3
Synonyms:LAMNA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

EuPathDBiHostDB:ENSG00000053747.15
HGNCiHGNC:6483 LAMA3
MIMi600805 gene
neXtProtiNX_Q16787

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Epidermolysis bullosa, junctional, Herlitz type (H-JEB)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn infantile and lethal form of junctional epidermolysis bullosa, a group of blistering skin diseases characterized by tissue separation which occurs within the dermo-epidermal basement In the Herlitz type, death occurs usually within the first six months of life. Occasionally, children survive to teens. It is marked by bullous lesions at birth and extensive denudation of skin and mucous membranes that may be hemorrhagic.
See also OMIM:226700
Laryngoonychocutaneous syndrome (LOCS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal recessive epithelial disorder confined to the Punjabi Muslim population. The condition is characterized by cutaneous erosions, nail dystrophy and exuberant vascular granulation tissue in certain epithelia, especially conjunctiva and larynx.
See also OMIM:245660

Keywords - Diseasei

Epidermolysis bullosa

Organism-specific databases

DisGeNETi3909
GeneReviewsiLAMA3
MalaCardsiLAMA3
MIMi226700 phenotype
245660 phenotype
Orphaneti79402 Generalized junctional epidermolysis bullosa, non-Herlitz type
79404 Junctional epidermolysis bullosa, Herlitz type
2407 LOC syndrome
PharmGKBiPA30272

Chemistry databases

ChEMBLiCHEMBL2364187

Polymorphism and mutation databases

BioMutaiLAMA3
DMDMi215274012

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 35Sequence analysisAdd BLAST35
ChainiPRO_000001705836 – 3333Laminin subunit alpha-3Add BLAST3298

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi142N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi242N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi299 ↔ 308By similarity
Disulfide bondi301 ↔ 319By similarity
Disulfide bondi321 ↔ 330By similarity
Disulfide bondi333 ↔ 353By similarity
Disulfide bondi356 ↔ 365By similarity
Disulfide bondi358 ↔ 390By similarity
Disulfide bondi393 ↔ 402By similarity
Disulfide bondi405 ↔ 423By similarity
Disulfide bondi426 ↔ 436By similarity
Disulfide bondi428 ↔ 443By similarity
Disulfide bondi445 ↔ 454By similarity
Disulfide bondi457 ↔ 467By similarity
Disulfide bondi491 ↔ 503By similarity
Disulfide bondi493 ↔ 509By similarity
Disulfide bondi511 ↔ 520By similarity
Disulfide bondi523 ↔ 533By similarity
Disulfide bondi536 ↔ 548By similarity
Disulfide bondi538 ↔ 555By similarity
Disulfide bondi557 ↔ 566By similarity
Disulfide bondi569 ↔ 586By similarity
Disulfide bondi601 ↔ 610By similarity
Disulfide bondi613 ↔ 628By similarity
Disulfide bondi631 ↔ 645By similarity
Disulfide bondi633 ↔ 652By similarity
Disulfide bondi654 ↔ 663By similarity
Disulfide bondi666 ↔ 681By similarity
Disulfide bondi684 ↔ 696By similarity
Disulfide bondi686 ↔ 703By similarity
Disulfide bondi705 ↔ 714By similarity
Disulfide bondi1266 ↔ 1278By similarity
Disulfide bondi1268 ↔ 1285By similarity
Disulfide bondi1287 ↔ 1296By similarity
Disulfide bondi1299 ↔ 1309By similarity
Disulfide bondi1312 ↔ 1319By similarity
Disulfide bondi1314 ↔ 1326By similarity
Disulfide bondi1328 ↔ 1337By similarity
Disulfide bondi1340 ↔ 1353By similarity
Disulfide bondi1356 ↔ 1371By similarity
Disulfide bondi1358 ↔ 1378By similarity
Disulfide bondi1380 ↔ 1389By similarity
Disulfide bondi1392 ↔ 1402By similarity
Disulfide bondi1405 ↔ 1417By similarity
Disulfide bondi1407 ↔ 1424By similarity
Disulfide bondi1426 ↔ 1435By similarity
Disulfide bondi1438 ↔ 1453By similarity
Disulfide bondi1687 ↔ 1696By similarity
Disulfide bondi1689 ↔ 1703By similarity
Disulfide bondi1706 ↔ 1715By similarity
Disulfide bondi1718 ↔ 1731By similarity
Disulfide bondi1734 ↔ 1746By similarity
Disulfide bondi1736 ↔ 1755By similarity
Disulfide bondi1757 ↔ 1766By similarity
Disulfide bondi1769 ↔ 1784By similarity
Disulfide bondi1822InterchainCurated
Disulfide bondi1825InterchainCurated
Glycosylationi2365N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2502N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2561 ↔ 2591By similarity
Glycosylationi2584N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2737 ↔ 2760By similarity
Disulfide bondi2895 ↔ 2927By similarity
Disulfide bondi3127 ↔ 3150By similarity
Disulfide bondi3302 ↔ 3330By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ16787
PaxDbiQ16787
PeptideAtlasiQ16787
PRIDEiQ16787
ProteomicsDBi61068
61069 [Q16787-1]
61070 [Q16787-3]

PTM databases

iPTMnetiQ16787
PhosphoSitePlusiQ16787
SwissPalmiQ16787

Expressioni

Tissue specificityi

Skin; respiratory, urinary, and digestive epithelia and in other specialized tissues with prominent secretory or protective functions. Epithelial basement membrane, and epithelial cell tongue that migrates into a wound bed. A differential and focal expression of the subunit alpha-3 is observed in the CNS.

Inductioni

Laminin-5 is up-regulated in wound sites of human skin.

Gene expression databases

BgeeiENSG00000053747 Expressed in 173 organ(s), highest expression level in ectocervix
CleanExiHS_LAMA3
ExpressionAtlasiQ16787 baseline and differential
GenevisibleiQ16787 HS

Organism-specific databases

HPAiCAB010757
HPA009309

Interactioni

Subunit structurei

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-3 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein), laminin-6 (laminin-311 or K-laminin) and laminin-7 (laminin-321 or KS-laminin).

GO - Molecular functioni

Protein-protein interaction databases

BioGridi110103, 25 interactors
ComplexPortaliCPX-1774 Laminin-332 complex variant A [Q16787-1]
CPX-1775 Laminin-311 complex variant A [Q16787-1]
CPX-1776 Laminin-321 complex [Q16787-1]
CPX-3165 Laminin-332 complex variant B [Q16787-2]
CPX-3166 Laminin-311 complex variant B [Q16787-2]
CORUMiQ16787
IntActiQ16787, 5 interactors
MINTiQ16787
STRINGi9606.ENSP00000324532

Structurei

3D structure databases

ProteinModelPortaliQ16787
SMRiQ16787
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini43 – 298Laminin N-terminalPROSITE-ProRule annotationAdd BLAST256
Domaini299 – 355Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST57
Domaini356 – 425Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST70
Domaini426 – 469Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST44
Domaini491 – 535Laminin EGF-like 4PROSITE-ProRule annotationAdd BLAST45
Domaini536 – 588Laminin EGF-like 5PROSITE-ProRule annotationAdd BLAST53
Domaini590 – 630Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST41
Domaini631 – 683Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST53
Domaini684 – 728Laminin EGF-like 8PROSITE-ProRule annotationAdd BLAST45
Domaini1266 – 1311Laminin EGF-like 9PROSITE-ProRule annotationAdd BLAST46
Domaini1312 – 1355Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST44
Domaini1356 – 1404Laminin EGF-like 11PROSITE-ProRule annotationAdd BLAST49
Domaini1405 – 1455Laminin EGF-like 12PROSITE-ProRule annotationAdd BLAST51
Domaini1476 – 1653Laminin IV type APROSITE-ProRule annotationAdd BLAST178
Domaini1687 – 1733Laminin EGF-like 13PROSITE-ProRule annotationAdd BLAST47
Domaini1734 – 1786Laminin EGF-like 14PROSITE-ProRule annotationAdd BLAST53
Domaini1787 – 1821Laminin EGF-like 15; truncatedPROSITE-ProRule annotationAdd BLAST35
Domaini2390 – 2591Laminin G-like 1PROSITE-ProRule annotationAdd BLAST202
Domaini2598 – 2760Laminin G-like 2PROSITE-ProRule annotationAdd BLAST163
Domaini2767 – 2927Laminin G-like 3PROSITE-ProRule annotationAdd BLAST161
Domaini2986 – 3150Laminin G-like 4PROSITE-ProRule annotationAdd BLAST165
Domaini3157 – 3330Laminin G-like 5PROSITE-ProRule annotationAdd BLAST174

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni298 – 728Domain VAdd BLAST431
Regioni796 – 1265Domain IV 1 (domain IV B)Add BLAST470
Regioni1266 – 1465Domain III BAdd BLAST200
Regioni1654 – 1821Domain III AAdd BLAST168
Regioni1822 – 2389Domain II and IAdd BLAST568

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1852 – 1941Sequence analysisAdd BLAST90
Coiled coili1987 – 2169Sequence analysisAdd BLAST183
Coiled coili2322 – 2388Sequence analysisAdd BLAST67

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi2278 – 2280Cell attachment siteSequence analysis3

Domaini

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

Keywords - Domaini

Coiled coil, Laminin EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiKOG1836 Eukaryota
ENOG410XRDC LUCA
HOGENOMiHOG000231235
HOVERGENiHBG052300
InParanoidiQ16787
KOiK06240
OrthoDBiEOG091G005L
PhylomeDBiQ16787
TreeFamiTF335359

Family and domain databases

Gene3Di2.60.120.1490, 1 hit
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR009254 Laminin_aI
IPR010307 Laminin_dom_II
IPR002049 Laminin_EGF
IPR001791 Laminin_G
IPR000034 Laminin_IV
IPR008211 Laminin_N
IPR038684 Laminin_N_sf
PfamiView protein in Pfam
PF00052 Laminin_B, 1 hit
PF00053 Laminin_EGF, 12 hits
PF02210 Laminin_G_2, 5 hits
PF06008 Laminin_I, 1 hit
PF06009 Laminin_II, 1 hit
PF00055 Laminin_N, 1 hit
SMARTiView protein in SMART
SM00181 EGF, 8 hits
SM00180 EGF_Lam, 14 hits
SM00281 LamB, 1 hit
SM00282 LamG, 5 hits
SM00136 LamNT, 1 hit
SUPFAMiSSF49899 SSF49899, 5 hits
PROSITEiView protein in PROSITE
PS00022 EGF_1, 12 hits
PS01186 EGF_2, 1 hit
PS01248 EGF_LAM_1, 13 hits
PS50027 EGF_LAM_2, 14 hits
PS50025 LAM_G_DOMAIN, 5 hits
PS51115 LAMININ_IVA, 1 hit
PS51117 LAMININ_NTER, 1 hit

Sequences (4+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 4 described isoforms and 9 potential isoforms that are computationally mapped.Show allAlign All

Isoform 2 (identifier: Q16787-2) [UniParc]FASTAAdd to basket
Also known as: B

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAAAARPRGR ALGPVLPPTP LLLLVLRVLP ACGATARDPG AAAGLSLHPT
60 70 80 90 100
YFNLAEAARI WATATCGERG PGEGRPQPEL YCKLVGGPTA PGSGHTIQGQ
110 120 130 140 150
FCDYCNSEDP RKAHPVTNAI DGSERWWQSP PLSSGTQYNR VNLTLDLGQL
160 170 180 190 200
FHVAYILIKF ANSPRPDLWV LERSVDFGST YSPWQYFAHS KVDCLKEFGR
210 220 230 240 250
EANMAVTRDD DVLCVTEYSR IVPLENGEVV VSLINGRPGA KNFTFSHTLR
260 270 280 290 300
EFTKATNIRL RFLRTNTLLG HLISKAQRDP TVTRRYYYSI KDISIGGQCV
310 320 330 340 350
CNGHAEVCNI NNPEKLFRCE CQHHTCGETC DRCCTGYNQR RWRPAAWEQS
360 370 380 390 400
HECEACNCHG HASNCYYDPD VERQQASLNT QGIYAGGGVC INCQHNTAGV
410 420 430 440 450
NCEQCAKGYY RPYGVPVDAP DGCIPCSCDP EHADGCEQGS GRCHCKPNFH
460 470 480 490 500
GDNCEKCAIG YYNFPFCLRI PIFPVSTPSS EDPVAGDIKG CDCNLEGVLP
510 520 530 540 550
EICDAHGRCL CRPGVEGPRC DTCRSGFYSF PICQACWCSA LGSYQMPCSS
560 570 580 590 600
VTGQCECRPG VTGQRCDRCL SGAYDFPHCQ GSSSACDPAG TINSNLGYCQ
610 620 630 640 650
CKLHVEGPTC SRCKLLYWNL DKENPSGCSE CKCHKAGTVS GTGECRQGDG
660 670 680 690 700
DCHCKSHVGG DSCDTCEDGY FALEKSNYFG CQGCQCDIGG ALSSMCSGPS
710 720 730 740 750
GVCQCREHVV GKVCQRPENN YYFPDLHHMK YEIEDGSTPN GRDLRFGFDP
760 770 780 790 800
LAFPEFSWRG YAQMTSVQND VRITLNVGKS SGSLFRVILR YVNPGTEAVS
810 820 830 840 850
GHITIYPSWG AAQSKEIIFL PSKEPAFVTV PGNGFADPFS ITPGIWVACI
860 870 880 890 900
KAEGVLLDYL VLLPRDYYEA SVLQLPVTEP CAYAGPPQEN CLLYQHLPVT
910 920 930 940 950
RFPCTLACEA RHFLLDGEPR PVAVRQPTPA HPVMVDLSGR EVELHLRLRI
960 970 980 990 1000
PQVGHYVVVV EYSTEAAQLF VVDVNVKSSG SVLAGQVNIY SCNYSVLCRS
1010 1020 1030 1040 1050
AVIDHMSRIA MYELLADADI QLKGHMARFL LHQVCIIPIE EFSAEYVRPQ
1060 1070 1080 1090 1100
VHCIASYGRF VNQSATCVSL AHETPPTALI LDVLSGRPFP HLPQQSSPSV
1110 1120 1130 1140 1150
DVLPGVTLKA PQNQVTLRGR VPHLGRYVFV IHFYQAAHPT FPAQVSVDGG
1160 1170 1180 1190 1200
WPRAGSFHAS FCPHVLGCRD QVIAEGQIEF DISEPEVAAT VKVPEGKSLV
1210 1220 1230 1240 1250
LVRVLVVPAE NYDYQILHKK SMDKSLEFIT NCGKNSFYLD PQTASRFCKN
1260 1270 1280 1290 1300
SARSLVAFYH KGALPCECHP TGATGPHCSP EGGQCPCQPN VIGRQCTRCA
1310 1320 1330 1340 1350
TGHYGFPRCK PCSCGRRLCE EMTGQCRCPP RTVRPQCEVC ETHSFSFHPM
1360 1370 1380 1390 1400
AGCEGCNCSR RGTIEAAMPE CDRDSGQCRC KPRITGRQCD RCASGFYRFP
1410 1420 1430 1440 1450
ECVPCNCNRD GTEPGVCDPG TGACLCKENV EGTECNVCRE GSFHLDPANL
1460 1470 1480 1490 1500
KGCTSCFCFG VNNQCHSSHK RRTKFVDMLG WHLETADRVD IPVSFNPGSN
1510 1520 1530 1540 1550
SMVADLQELP ATIHSASWVA PTSYLGDKVS SYGGYLTYQA KSFGLPGDMV
1560 1570 1580 1590 1600
LLEKKPDVQL TGQHMSIIYE ETNTPRPDRL HHGRVHVVEG NFRHASSRAP
1610 1620 1630 1640 1650
VSREELMTVL SRLADVRIQG LYFTETQRLT LSEVGLEEAS DTGSGRIALA
1660 1670 1680 1690 1700
VEICACPPAY AGDSCQGCSP GYYRDHKGLY TGRCVPCNCN GHSNQCQDGS
1710 1720 1730 1740 1750
GICVNCQHNT AGEHCERCQE GYYGNAVHGS CRACPCPHTN SFATGCVVNG
1760 1770 1780 1790 1800
GDVRCSCKAG YTGTQCERCA PGYFGNPQKF GGSCQPCSCN SNGQLGSCHP
1810 1820 1830 1840 1850
LTGDCINQEP KDSSPAEECD DCDSCVMTLL NDLATMGEQL RLVKSQLQGL
1860 1870 1880 1890 1900
SASAGLLEQM RHMETQAKDL RNQLLNYRSA ISNHGSKIEG LERELTDLNQ
1910 1920 1930 1940 1950
EFETLQEKAQ VNSRKAQTLN NNVNRATQSA KELDVKIKNV IRNVHILLKQ
1960 1970 1980 1990 2000
ISGTDGEGNN VPSGDFSREW AEAQRMMREL RNRNFGKHLR EAEADKRESQ
2010 2020 2030 2040 2050
LLLNRIRTWQ KTHQGENNGL ANSIRDSLNE YEAKLSDLRA RLQEAAAQAK
2060 2070 2080 2090 2100
QANGLNQENE RALGAIQRQV KEINSLQSDF TKYLTTADSS LLQTNIALQL
2110 2120 2130 2140 2150
MEKSQKEYEK LAASLNEARQ ELSDKVRELS RSAGKTSLVE EAEKHARSLQ
2160 2170 2180 2190 2200
ELAKQLEEIK RNASGDELVR CAVDAATAYE NILNAIKAAE DAANRAASAS
2210 2220 2230 2240 2250
ESALQTVIKE DLPRKAKTLS SNSDKLLNEA KMTQKKLKQE VSPALNNLQQ
2260 2270 2280 2290 2300
TLNIVTVQKE VIDTNLTTLR DGLHGIQRGD IDAMISSAKS MVRKANDITD
2310 2320 2330 2340 2350
EVLDGLNPIQ TDVERIKDTY GRTQNEDFKK ALTDADNSVN KLTNKLPDLW
2360 2370 2380 2390 2400
RKIESINQQL LPLGNISDNM DRIRELIQQA RDAASKVAVP MRFNGKSGVE
2410 2420 2430 2440 2450
VRLPNDLEDL KGYTSLSLFL QRPNSRENGG TENMFVMYLG NKDASRDYIG
2460 2470 2480 2490 2500
MAVVDGQLTC VYNLGDREAE LQVDQILTKS ETKEAVMDRV KFQRIYQFAR
2510 2520 2530 2540 2550
LNYTKGATSS KPETPGVYDM DGRNSNTLLN LDPENVVFYV GGYPPDFKLP
2560 2570 2580 2590 2600
SRLSFPPYKG CIELDDLNEN VLSLYNFKKT FNLNTTEVEP CRRRKEESDK
2610 2620 2630 2640 2650
NYFEGTGYAR VPTQPHAPIP TFGQTIQTTV DRGLLFFAEN GDRFISLNIE
2660 2670 2680 2690 2700
DGKLMVRYKL NSELPKERGV GDAINNGRDH SIQIKIGKLQ KRMWINVDVQ
2710 2720 2730 2740 2750
NTIIDGEVFD FSTYYLGGIP IAIRERFNIS TPAFRGCMKN LKKTSGVVRL
2760 2770 2780 2790 2800
NDTVGVTKKC SEDWKLVRSA SFSRGGQLSF TDLGLPPTDH LQASFGFQTF
2810 2820 2830 2840 2850
QPSGILLDHQ TWTRNLQVTL EDGYIELSTS DSGSPIFKSP QTYMDGLLHY
2860 2870 2880 2890 2900
VSVISDNSGL RLLIDDQLLR NSKRLKHISS SRQSLRLGGS NFEGCISNVF
2910 2920 2930 2940 2950
VQRLSLSPEV LDLTSNSLKR DVSLGGCSLN KPPFLMLLKG STRFNKTKTF
2960 2970 2980 2990 3000
RINQLLQDTP VASPRSVKVW QDACSPLPKT QANHGALQFG DIPTSHLLFK
3010 3020 3030 3040 3050
LPQELLKPRS QFAVDMQTTS SRGLVFHTGT KNSFMALYLS KGRLVFALGT
3060 3070 3080 3090 3100
DGKKLRIKSK EKCNDGKWHT VVFGHDGEKG RLVVDGLRAR EGSLPGNSTI
3110 3120 3130 3140 3150
SIRAPVYLGS PPSGKPKSLP TNSFVGCLKN FQLDSKPLYT PSSSFGVSSC
3160 3170 3180 3190 3200
LGGPLEKGIY FSEEGGHVVL AHSVLLGPEF KLVFSIRPRS LTGILIHIGS
3210 3220 3230 3240 3250
QPGKHLCVYL EAGKVTASMD SGAGGTSTSV TPKQSLCDGQ WHSVAVTIKQ
3260 3270 3280 3290 3300
HILHLELDTD SSYTAGQIPF PPASTQEPLH LGGAPANLTT LRIPVWKSFF
3310 3320 3330
GCLRNIHVNH IPVPVTEALE VQGPVSLNGC PDQ
Length:3,333
Mass (Da):366,649
Last modified:November 25, 2008 - v2
Checksum:i9F99AF49B8EF27DD
GO
Isoform 1 (identifier: Q16787-1) [UniParc]FASTAAdd to basket
Also known as: A

The sequence of this isoform differs from the canonical sequence as follows:
     1-1620: Missing.
     1621-1665: LYFTETQRLT...CPPAYAGDSC → MPPAVRRSAC...QASYVEFRPS

Show »
Length:1,724
Mass (Da):190,491
Checksum:i0477C729951763A5
GO
Isoform 3 (identifier: Q16787-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1946-2002: ILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLL → M

Show »
Length:3,277
Mass (Da):360,212
Checksum:i3ACFFE998357122E
GO
Isoform 4 (identifier: Q16787-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1609: Missing.
     1610-1665: LSRLADVRIQ...CPPAYAGDSC → MPPAVRRSAC...QASYVEFRPS
     1946-2002: ILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLL → M

Show »
Length:1,668
Mass (Da):184,054
Checksum:i9EBF5FC45637645C
GO

Computationally mapped potential isoform sequencesi

There are 9 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0A0MSA0A0A0A0MSA0_HUMAN
Laminin subunit alpha-3
LAMA3
3,277Annotation score:
A0A0A6YYF2A0A0A6YYF2_HUMAN
HCG1811249, isoform CRA_e
LAMA3 hCG_1811249
1,724Annotation score:
A0A0A0MTS5A0A0A0MTS5_HUMAN
HCG1811249, isoform CRA_f
LAMA3 hCG_1811249
1,668Annotation score:
K7EIP4K7EIP4_HUMAN
Laminin subunit alpha-3
LAMA3
1,147Annotation score:
A0A075B783A0A075B783_HUMAN
Laminin subunit alpha-3
LAMA3
576Annotation score:
K7ERM0K7ERM0_HUMAN
Laminin subunit alpha-3
LAMA3
134Annotation score:
K7EPP3K7EPP3_HUMAN
Laminin subunit alpha-3
LAMA3
94Annotation score:
K7EQ42K7EQ42_HUMAN
Laminin subunit alpha-3
LAMA3
59Annotation score:
K7EMU9K7EMU9_HUMAN
Laminin subunit alpha-3
LAMA3
37Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1544G → A in CAA59429 (PubMed:8586427).Curated1
Sequence conflicti1544G → A in CAA59325 (Ref. 6) Curated1
Sequence conflicti1743 – 1745ATG → GMC in CAA59428 (PubMed:8586427).Curated3
Sequence conflicti1743 – 1745ATG → GMC in CAA59429 (PubMed:8586427).Curated3
Sequence conflicti2101M → K in CAA59428 (PubMed:8586427).Curated1
Sequence conflicti2101M → K in CAA59429 (PubMed:8586427).Curated1
Sequence conflicti2374R → L in CAA59428 (PubMed:8586427).Curated1
Sequence conflicti2374R → L in CAA59429 (PubMed:8586427).Curated1
Sequence conflicti2589E → Q in CAA59428 (PubMed:8586427).Curated1
Sequence conflicti2589E → Q in CAA59429 (PubMed:8586427).Curated1
Sequence conflicti2672D → A in CAA59428 (PubMed:8586427).Curated1
Sequence conflicti2672D → A in CAA59429 (PubMed:8586427).Curated1
Sequence conflicti2804G → A in CAA59428 (PubMed:8586427).Curated1
Sequence conflicti2804G → A in CAA59429 (PubMed:8586427).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_050078796T → N. Corresponds to variant dbSNP:rs17187262Ensembl.1
Natural variantiVAR_0500791206V → A. Corresponds to variant dbSNP:rs12457323Ensembl.1
Natural variantiVAR_0500801208P → T. Corresponds to variant dbSNP:rs17202961Ensembl.1
Natural variantiVAR_0594441774F → L. Corresponds to variant dbSNP:rs958631Ensembl.1
Natural variantiVAR_0473742702T → A. Corresponds to variant dbSNP:rs9952370Ensembl.1
Natural variantiVAR_0473752815N → K. Corresponds to variant dbSNP:rs1154232Ensembl.1
Natural variantiVAR_0594452834S → G3 PublicationsCorresponds to variant dbSNP:rs1154233Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0357381 – 1620Missing in isoform 1. 1 PublicationAdd BLAST1620
Alternative sequenceiVSP_0470791 – 1609Missing in isoform 4. 1 PublicationAdd BLAST1609
Alternative sequenceiVSP_0470801610 – 1665LSRLA…AGDSC → MPPAVRRSACSMGWLWIFGA ALGQCLGYSSQQQRVPFLQP PGQSQLQASYVEFRPS in isoform 4. 1 PublicationAdd BLAST56
Alternative sequenceiVSP_0357391621 – 1665LYFTE…AGDSC → MPPAVRRSACSMGWLWIFGA ALGQCLGYSSQQQRVPFLQP PGQSQLQASYVEFRPS in isoform 1. 1 PublicationAdd BLAST45
Alternative sequenceiVSP_0434871946 – 2002ILLKQ…ESQLL → M in isoform 3 and isoform 4. 1 PublicationAdd BLAST57

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY327114 mRNA Translation: AAQ72569.1
AY327115 mRNA Translation: AAQ72570.1
AY327116 mRNA Translation: AAQ72571.1
AB107369 Genomic DNA Translation: BAD13428.1
EF444992 Genomic DNA Translation: ACA06011.1
AC010754 Genomic DNA No translation available.
AC067796 Genomic DNA No translation available.
AC090366 Genomic DNA No translation available.
X85107 mRNA Translation: CAA59428.1
X85108 mRNA Translation: CAA59429.1
X84900 mRNA Translation: CAA59325.1
L34155 mRNA Translation: AAA59483.1
CCDSiCCDS11880.1 [Q16787-1]
CCDS42419.1 [Q16787-2]
CCDS45838.1 [Q16787-3]
CCDS59307.1 [Q16787-4]
PIRiA55347
RefSeqiNP_000218.3, NM_000227.4
NP_001121189.2, NM_001127717.2
NP_001121190.2, NM_001127718.2
NP_001289925.1, NM_001302996.1
NP_937762.2, NM_198129.2
UniGeneiHs.436367

Genome annotation databases

EnsembliENST00000313654; ENSP00000324532; ENSG00000053747
GeneIDi3909
KEGGihsa:3909
UCSCiuc002kuq.4 human [Q16787-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY327114 mRNA Translation: AAQ72569.1
AY327115 mRNA Translation: AAQ72570.1
AY327116 mRNA Translation: AAQ72571.1
AB107369 Genomic DNA Translation: BAD13428.1
EF444992 Genomic DNA Translation: ACA06011.1
AC010754 Genomic DNA No translation available.
AC067796 Genomic DNA No translation available.
AC090366 Genomic DNA No translation available.
X85107 mRNA Translation: CAA59428.1
X85108 mRNA Translation: CAA59429.1
X84900 mRNA Translation: CAA59325.1
L34155 mRNA Translation: AAA59483.1
CCDSiCCDS11880.1 [Q16787-1]
CCDS42419.1 [Q16787-2]
CCDS45838.1 [Q16787-3]
CCDS59307.1 [Q16787-4]
PIRiA55347
RefSeqiNP_000218.3, NM_000227.4
NP_001121189.2, NM_001127717.2
NP_001121190.2, NM_001127718.2
NP_001289925.1, NM_001302996.1
NP_937762.2, NM_198129.2
UniGeneiHs.436367

3D structure databases

ProteinModelPortaliQ16787
SMRiQ16787
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110103, 25 interactors
ComplexPortaliCPX-1774 Laminin-332 complex variant A [Q16787-1]
CPX-1775 Laminin-311 complex variant A [Q16787-1]
CPX-1776 Laminin-321 complex [Q16787-1]
CPX-3165 Laminin-332 complex variant B [Q16787-2]
CPX-3166 Laminin-311 complex variant B [Q16787-2]
CORUMiQ16787
IntActiQ16787, 5 interactors
MINTiQ16787
STRINGi9606.ENSP00000324532

Chemistry databases

ChEMBLiCHEMBL2364187

PTM databases

iPTMnetiQ16787
PhosphoSitePlusiQ16787
SwissPalmiQ16787

Polymorphism and mutation databases

BioMutaiLAMA3
DMDMi215274012

Proteomic databases

EPDiQ16787
PaxDbiQ16787
PeptideAtlasiQ16787
PRIDEiQ16787
ProteomicsDBi61068
61069 [Q16787-1]
61070 [Q16787-3]

Protocols and materials databases

DNASUi3909
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000313654; ENSP00000324532; ENSG00000053747
GeneIDi3909
KEGGihsa:3909
UCSCiuc002kuq.4 human [Q16787-2]

Organism-specific databases

CTDi3909
DisGeNETi3909
EuPathDBiHostDB:ENSG00000053747.15
GeneCardsiLAMA3
GeneReviewsiLAMA3
HGNCiHGNC:6483 LAMA3
HPAiCAB010757
HPA009309
MalaCardsiLAMA3
MIMi226700 phenotype
245660 phenotype
600805 gene
neXtProtiNX_Q16787
Orphaneti79402 Generalized junctional epidermolysis bullosa, non-Herlitz type
79404 Junctional epidermolysis bullosa, Herlitz type
2407 LOC syndrome
PharmGKBiPA30272
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1836 Eukaryota
ENOG410XRDC LUCA
HOGENOMiHOG000231235
HOVERGENiHBG052300
InParanoidiQ16787
KOiK06240
OrthoDBiEOG091G005L
PhylomeDBiQ16787
TreeFamiTF335359

Enzyme and pathway databases

ReactomeiR-HSA-1474228 Degradation of the extracellular matrix
R-HSA-2022090 Assembly of collagen fibrils and other multimeric structures
R-HSA-2214320 Anchoring fibril formation
R-HSA-3000157 Laminin interactions
R-HSA-3000171 Non-integrin membrane-ECM interactions
R-HSA-3000178 ECM proteoglycans
R-HSA-446107 Type I hemidesmosome assembly
R-HSA-8874081 MET activates PTK2 signaling
SIGNORiQ16787

Miscellaneous databases

ChiTaRSiLAMA3 human
GeneWikiiLaminin,_alpha_3
GenomeRNAii3909
PROiPR:Q16787
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000053747 Expressed in 173 organ(s), highest expression level in ectocervix
CleanExiHS_LAMA3
ExpressionAtlasiQ16787 baseline and differential
GenevisibleiQ16787 HS

Family and domain databases

Gene3Di2.60.120.1490, 1 hit
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR009254 Laminin_aI
IPR010307 Laminin_dom_II
IPR002049 Laminin_EGF
IPR001791 Laminin_G
IPR000034 Laminin_IV
IPR008211 Laminin_N
IPR038684 Laminin_N_sf
PfamiView protein in Pfam
PF00052 Laminin_B, 1 hit
PF00053 Laminin_EGF, 12 hits
PF02210 Laminin_G_2, 5 hits
PF06008 Laminin_I, 1 hit
PF06009 Laminin_II, 1 hit
PF00055 Laminin_N, 1 hit
SMARTiView protein in SMART
SM00181 EGF, 8 hits
SM00180 EGF_Lam, 14 hits
SM00281 LamB, 1 hit
SM00282 LamG, 5 hits
SM00136 LamNT, 1 hit
SUPFAMiSSF49899 SSF49899, 5 hits
PROSITEiView protein in PROSITE
PS00022 EGF_1, 12 hits
PS01186 EGF_2, 1 hit
PS01248 EGF_LAM_1, 13 hits
PS50027 EGF_LAM_2, 14 hits
PS50025 LAM_G_DOMAIN, 5 hits
PS51115 LAMININ_IVA, 1 hit
PS51117 LAMININ_NTER, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiLAMA3_HUMAN
AccessioniPrimary (citable) accession number: Q16787
Secondary accession number(s): B0YJ33
, Q13679, Q13680, Q6VU67, Q6VU68, Q6VU69, Q76E14, Q96TG0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 25, 2008
Last modified: October 10, 2018
This is version 186 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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