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Q16787

- LAMA3_HUMAN

UniProt

Q16787 - LAMA3_HUMAN

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Protein

Laminin subunit alpha-3

Gene

LAMA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- 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

  1. structural molecule activity Source: ProtInc

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. cell junction assembly Source: Reactome
  3. endodermal cell differentiation Source: UniProtKB
  4. epidermis development Source: ProtInc
  5. extracellular matrix disassembly Source: Reactome
  6. extracellular matrix organization Source: Reactome
  7. hemidesmosome assembly Source: Reactome
  8. regulation of cell adhesion Source: InterPro
  9. regulation of cell migration Source: InterPro
  10. regulation of embryonic development Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150268. Anchoring fibril formation.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_169262. Laminin interactions.
REACT_20537. Type I hemidesmosome assembly.

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
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:6483. LAMA3.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: ProtInc
  2. extracellular region Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. laminin-1 complex Source: InterPro
  5. laminin-5 complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Epidermolysis bullosa, junctional, Herlitz type (H-JEB) [MIM:226700]: An 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.
Laryngoonychocutaneous syndrome (LOCS) [MIM:245660]: Autosomal 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Epidermolysis bullosa

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535Sequence AnalysisAdd
BLAST
Chaini36 – 33333298Laminin subunit alpha-3PRO_0000017058Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi142 – 1421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi242 – 2421N-linked (GlcNAc...)Sequence Analysis
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 bondi1822 – 1822InterchainCurated
Disulfide bondi1825 – 1825InterchainCurated
Glycosylationi2365 – 23651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2502 – 25021N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2561 ↔ 2591By similarity
Glycosylationi2584 – 25841N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2737 ↔ 2760By similarity
Disulfide bondi2895 ↔ 2927By similarity
Disulfide bondi3127 ↔ 3150By similarity
Disulfide bondi3302 ↔ 3330By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ16787.
PaxDbiQ16787.
PRIDEiQ16787.

PTM databases

PhosphoSiteiQ16787.

Miscellaneous databases

PMAP-CutDBQ6VU68.

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

BgeeiQ16787.
CleanExiHS_LAMA3.
ExpressionAtlasiQ16787. baseline and differential.
GenevestigatoriQ16787.

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).

Protein-protein interaction databases

BioGridi110103. 8 interactions.
IntActiQ16787. 3 interactions.
MINTiMINT-1431248.
STRINGi9606.ENSP00000324532.

Structurei

3D structure databases

ProteinModelPortaliQ16787.
SMRiQ16787. Positions 44-427.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini43 – 298256Laminin N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini299 – 35557Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini356 – 42570Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini426 – 46944Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini491 – 53545Laminin EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini536 – 58853Laminin EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini590 – 63041Laminin EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini631 – 68353Laminin EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini684 – 72845Laminin EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini1266 – 131146Laminin EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini1312 – 135544Laminin EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini1356 – 140449Laminin EGF-like 11PROSITE-ProRule annotationAdd
BLAST
Domaini1405 – 145551Laminin EGF-like 12PROSITE-ProRule annotationAdd
BLAST
Domaini1476 – 1653178Laminin IV type APROSITE-ProRule annotationAdd
BLAST
Domaini1687 – 173347Laminin EGF-like 13PROSITE-ProRule annotationAdd
BLAST
Domaini1734 – 178653Laminin EGF-like 14PROSITE-ProRule annotationAdd
BLAST
Domaini1787 – 182135Laminin EGF-like 15; truncatedPROSITE-ProRule annotationAdd
BLAST
Domaini2390 – 2591202Laminin G-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini2598 – 2760163Laminin G-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini2767 – 2927161Laminin G-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini2986 – 3150165Laminin G-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini3157 – 3330174Laminin G-like 5PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni298 – 728431Domain VAdd
BLAST
Regioni796 – 1265470Domain IV 1 (domain IV B)Add
BLAST
Regioni1266 – 1465200Domain III BAdd
BLAST
Regioni1654 – 1821168Domain III AAdd
BLAST
Regioni1822 – 2389568Domain II and IAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1852 – 194190Sequence AnalysisAdd
BLAST
Coiled coili1987 – 2169183Sequence AnalysisAdd
BLAST
Coiled coili2322 – 238867Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi2278 – 22803Cell attachment siteSequence Analysis

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.

Sequence similaritiesi

Contains 15 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 5 laminin G-like domains.PROSITE-ProRule annotation
Contains 1 laminin IV type A domain.PROSITE-ProRule annotation
Contains 1 laminin N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG292643.
GeneTreeiENSGT00760000118860.
HOGENOMiHOG000231235.
HOVERGENiHBG052300.
InParanoidiQ16787.
KOiK06240.
OMAiRGLYFTE.
OrthoDBiEOG7DFXB9.
PhylomeDBiQ16787.
TreeFamiTF335359.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR013320. ConA-like_dom.
IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR010307. Laminin_domII.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 12 hits.
PF00054. Laminin_G_1. 1 hit.
PF02210. Laminin_G_2. 4 hits.
PF06008. Laminin_I. 1 hit.
PF06009. Laminin_II. 1 hit.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00180. EGF_Lam. 14 hits.
SM00281. LamB. 1 hit.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 5 hits.
PROSITEiPS00022. 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.
[Graphical view]

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. Align

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1544 – 15441G → A in CAA59429. (PubMed:8586427)Curated
Sequence conflicti1544 – 15441G → A in CAA59325. 1 PublicationCurated
Sequence conflicti1743 – 17453ATG → GMC in CAA59428. (PubMed:8586427)Curated
Sequence conflicti1743 – 17453ATG → GMC in CAA59429. (PubMed:8586427)Curated
Sequence conflicti2101 – 21011M → K in CAA59428. (PubMed:8586427)Curated
Sequence conflicti2101 – 21011M → K in CAA59429. (PubMed:8586427)Curated
Sequence conflicti2374 – 23741R → L in CAA59428. (PubMed:8586427)Curated
Sequence conflicti2374 – 23741R → L in CAA59429. (PubMed:8586427)Curated
Sequence conflicti2589 – 25891E → Q in CAA59428. (PubMed:8586427)Curated
Sequence conflicti2589 – 25891E → Q in CAA59429. (PubMed:8586427)Curated
Sequence conflicti2672 – 26721D → A in CAA59428. (PubMed:8586427)Curated
Sequence conflicti2672 – 26721D → A in CAA59429. (PubMed:8586427)Curated
Sequence conflicti2804 – 28041G → A in CAA59428. (PubMed:8586427)Curated
Sequence conflicti2804 – 28041G → A in CAA59429. (PubMed:8586427)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti796 – 7961T → N.
Corresponds to variant rs17187262 [ dbSNP | Ensembl ].
VAR_050078
Natural varianti1206 – 12061V → A.
Corresponds to variant rs12457323 [ dbSNP | Ensembl ].
VAR_050079
Natural varianti1208 – 12081P → T.
Corresponds to variant rs17202961 [ dbSNP | Ensembl ].
VAR_050080
Natural varianti1774 – 17741F → L.
Corresponds to variant rs958631 [ dbSNP | Ensembl ].
VAR_059444
Natural varianti2702 – 27021T → A.
Corresponds to variant rs9952370 [ dbSNP | Ensembl ].
VAR_047374
Natural varianti2815 – 28151N → K.
Corresponds to variant rs1154232 [ dbSNP | Ensembl ].
VAR_047375
Natural varianti2834 – 28341S → G.3 Publications
Corresponds to variant rs1154233 [ dbSNP | Ensembl ].
VAR_059445

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 16201620Missing in isoform 1. 1 PublicationVSP_035738Add
BLAST
Alternative sequencei1 – 16091609Missing in isoform 4. 1 PublicationVSP_047079Add
BLAST
Alternative sequencei1610 – 166556LSRLA…AGDSC → MPPAVRRSACSMGWLWIFGA ALGQCLGYSSQQQRVPFLQP PGQSQLQASYVEFRPS in isoform 4. 1 PublicationVSP_047080Add
BLAST
Alternative sequencei1621 – 166545LYFTE…AGDSC → MPPAVRRSACSMGWLWIFGA ALGQCLGYSSQQQRVPFLQP PGQSQLQASYVEFRPS in isoform 1. 1 PublicationVSP_035739Add
BLAST
Alternative sequencei1946 – 200257ILLKQ…ESQLL → M in isoform 3 and isoform 4. 1 PublicationVSP_043487Add
BLAST

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_000218.2. NM_000227.3. [Q16787-1]
NP_001121189.1. NM_001127717.1. [Q16787-3]
NP_001121190.1. NM_001127718.1. [Q16787-4]
NP_937762.1. NM_198129.1. [Q16787-2]
UniGeneiHs.436367.

Genome annotation databases

EnsembliENST00000313654; ENSP00000324532; ENSG00000053747.
GeneIDi3909.
KEGGihsa:3909.
UCSCiuc002kuq.3. human. [Q16787-2]
uc002kur.3. human. [Q16787-3]

Polymorphism databases

DMDMi215274012.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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 .
CCDSi CCDS11880.1. [Q16787-1 ]
CCDS42419.1. [Q16787-2 ]
CCDS45838.1. [Q16787-3 ]
CCDS59307.1. [Q16787-4 ]
PIRi A55347.
RefSeqi NP_000218.2. NM_000227.3. [Q16787-1 ]
NP_001121189.1. NM_001127717.1. [Q16787-3 ]
NP_001121190.1. NM_001127718.1. [Q16787-4 ]
NP_937762.1. NM_198129.1. [Q16787-2 ]
UniGenei Hs.436367.

3D structure databases

ProteinModelPortali Q16787.
SMRi Q16787. Positions 44-427.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110103. 8 interactions.
IntActi Q16787. 3 interactions.
MINTi MINT-1431248.
STRINGi 9606.ENSP00000324532.

Chemistry

ChEMBLi CHEMBL2364187.

PTM databases

PhosphoSitei Q16787.

Polymorphism databases

DMDMi 215274012.

Proteomic databases

MaxQBi Q16787.
PaxDbi Q16787.
PRIDEi Q16787.

Protocols and materials databases

DNASUi 3909.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000313654 ; ENSP00000324532 ; ENSG00000053747 .
GeneIDi 3909.
KEGGi hsa:3909.
UCSCi uc002kuq.3. human. [Q16787-2 ]
uc002kur.3. human. [Q16787-3 ]

Organism-specific databases

CTDi 3909.
GeneCardsi GC18P021269.
GeneReviewsi LAMA3.
HGNCi HGNC:6483. LAMA3.
HPAi CAB010757.
HPA009309.
MIMi 226700. phenotype.
245660. phenotype.
600805. gene.
neXtProti NX_Q16787.
Orphaneti 79402. Generalized junctional epidermolysis bullosa, non-Herlitz type.
79404. Junctional epidermolysis bullosa, Herlitz type.
2407. LOC syndrome.
PharmGKBi PA30272.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG292643.
GeneTreei ENSGT00760000118860.
HOGENOMi HOG000231235.
HOVERGENi HBG052300.
InParanoidi Q16787.
KOi K06240.
OMAi RGLYFTE.
OrthoDBi EOG7DFXB9.
PhylomeDBi Q16787.
TreeFami TF335359.

Enzyme and pathway databases

Reactomei REACT_118572. Degradation of the extracellular matrix.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150268. Anchoring fibril formation.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_169262. Laminin interactions.
REACT_20537. Type I hemidesmosome assembly.

Miscellaneous databases

ChiTaRSi LAMA3. human.
GeneWikii Laminin,_alpha_3.
GenomeRNAii 3909.
NextBioi 15345.
PMAP-CutDB Q6VU68.
PROi Q16787.
SOURCEi Search...

Gene expression databases

Bgeei Q16787.
CleanExi HS_LAMA3.
ExpressionAtlasi Q16787. baseline and differential.
Genevestigatori Q16787.

Family and domain databases

Gene3Di 2.60.120.200. 5 hits.
InterProi IPR013320. ConA-like_dom.
IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR010307. Laminin_domII.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
IPR008211. Laminin_N.
[Graphical view ]
Pfami PF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 12 hits.
PF00054. Laminin_G_1. 1 hit.
PF02210. Laminin_G_2. 4 hits.
PF06008. Laminin_I. 1 hit.
PF06009. Laminin_II. 1 hit.
PF00055. Laminin_N. 1 hit.
[Graphical view ]
SMARTi SM00180. EGF_Lam. 14 hits.
SM00281. LamB. 1 hit.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 5 hits.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), DISEASE.
  2. "Characterization of laminin 5B and NH2-terminal proteolytic fragment of its alpha3B chain: promotion of cellular adhesion, migration, and proliferation."
    Kariya Y., Yasuda C., Nakashima Y., Ishida K., Tsubota Y., Miyazaki K.
    J. Biol. Chem. 279:24774-24784(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), VARIANT GLY-2834.
  3. Stockwell T.B., Busam D.A., Ferriera S.M., Brownley A.N., Strausberg R.L., Kirkness E.F., Rogers Y.-H., Levy S.
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Cloning of the laminin alpha 3 chain gene (LAMA3) and identification of a homozygous deletion in a patient with Herlitz junctional epidermolysis bullosa."
    Vidal F., Baudoin C., Miquel C., Galliano M.-F., Christiano A.M., Uitto J., Ortonne J.-P., Meneguzzi G.
    Genomics 30:273-280(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-2858 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 1528-2858 (ISOFORMS 1/2).
    Tissue: Keratinocyte.
  6. "Mutation in LAMA3 gene in a patient affected by H-Jeb."
    Aberdam D., Vidal F., Baudoin C., Miquel C., Ortonne J.-P., Meneguzzi G.
    Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1528-3333 (ISOFORMS 1/2), VARIANT GLY-2834.
  7. "Cloning of the LamA3 gene encoding the alpha 3 chain of the adhesive ligand epiligrin. Expression in wound repair."
    Ryan M.C., Tizard R., Vandevanter D.R., Carter W.G.
    J. Biol. Chem. 269:22779-22787(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-2834.
    Tissue: Keratinocyte.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLAMA3_HUMAN
AccessioniPrimary (citable) accession number: Q16787
Secondary accession number(s): B0YJ33
, Q13679, Q13680, Q6VU67, Q6VU68, Q6VU69, Q76E14, Q96TG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 25, 2008
Last modified: November 26, 2014
This is version 150 of the entry and version 2 of the sequence. [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
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3