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Q16787

- LAMA3_HUMAN

UniProt

Q16787 - LAMA3_HUMAN

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Protein
Laminin subunit alpha-3
Gene
LAMA3, LAMNA
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
Complete GO annotation...

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. cell junction assembly Source: Reactome
  3. epidermis development Source: ProtInc
  4. extracellular matrix disassembly Source: Reactome
  5. extracellular matrix organization Source: Reactome
  6. hemidesmosome assembly Source: Reactome
  7. regulation of cell adhesion Source: InterPro
  8. regulation of cell migration Source: InterPro
  9. 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. laminin-1 complex Source: InterPro
  4. 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.1 Publication
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.1 Publication

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 – 3535 Reviewed prediction
Add
BLAST
Chaini36 – 33333298Laminin subunit alpha-3
PRO_0000017058Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi142 – 1421N-linked (GlcNAc...) Reviewed prediction
Glycosylationi242 – 2421N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi299 ↔ 308 By similarity
Disulfide bondi301 ↔ 319 By similarity
Disulfide bondi321 ↔ 330 By similarity
Disulfide bondi333 ↔ 353 By similarity
Disulfide bondi356 ↔ 365 By similarity
Disulfide bondi358 ↔ 390 By similarity
Disulfide bondi393 ↔ 402 By similarity
Disulfide bondi405 ↔ 423 By similarity
Disulfide bondi426 ↔ 436 By similarity
Disulfide bondi428 ↔ 443 By similarity
Disulfide bondi445 ↔ 454 By similarity
Disulfide bondi457 ↔ 467 By similarity
Disulfide bondi491 ↔ 503 By similarity
Disulfide bondi493 ↔ 509 By similarity
Disulfide bondi511 ↔ 520 By similarity
Disulfide bondi523 ↔ 533 By similarity
Disulfide bondi536 ↔ 548 By similarity
Disulfide bondi538 ↔ 555 By similarity
Disulfide bondi557 ↔ 566 By similarity
Disulfide bondi569 ↔ 586 By similarity
Disulfide bondi601 ↔ 610 By similarity
Disulfide bondi613 ↔ 628 By similarity
Disulfide bondi631 ↔ 645 By similarity
Disulfide bondi633 ↔ 652 By similarity
Disulfide bondi654 ↔ 663 By similarity
Disulfide bondi666 ↔ 681 By similarity
Disulfide bondi684 ↔ 696 By similarity
Disulfide bondi686 ↔ 703 By similarity
Disulfide bondi705 ↔ 714 By similarity
Disulfide bondi1266 ↔ 1278 By similarity
Disulfide bondi1268 ↔ 1285 By similarity
Disulfide bondi1287 ↔ 1296 By similarity
Disulfide bondi1299 ↔ 1309 By similarity
Disulfide bondi1312 ↔ 1319 By similarity
Disulfide bondi1314 ↔ 1326 By similarity
Disulfide bondi1328 ↔ 1337 By similarity
Disulfide bondi1340 ↔ 1353 By similarity
Disulfide bondi1356 ↔ 1371 By similarity
Disulfide bondi1358 ↔ 1378 By similarity
Disulfide bondi1380 ↔ 1389 By similarity
Disulfide bondi1392 ↔ 1402 By similarity
Disulfide bondi1405 ↔ 1417 By similarity
Disulfide bondi1407 ↔ 1424 By similarity
Disulfide bondi1426 ↔ 1435 By similarity
Disulfide bondi1438 ↔ 1453 By similarity
Disulfide bondi1687 ↔ 1696 By similarity
Disulfide bondi1689 ↔ 1703 By similarity
Disulfide bondi1706 ↔ 1715 By similarity
Disulfide bondi1718 ↔ 1731 By similarity
Disulfide bondi1734 ↔ 1746 By similarity
Disulfide bondi1736 ↔ 1755 By similarity
Disulfide bondi1757 ↔ 1766 By similarity
Disulfide bondi1769 ↔ 1784 By similarity
Disulfide bondi1822 – 1822Interchain Inferred
Disulfide bondi1825 – 1825Interchain Inferred
Glycosylationi2365 – 23651N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2502 – 25021N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2561 ↔ 2591 By similarity
Glycosylationi2584 – 25841N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2737 ↔ 2760 By similarity
Disulfide bondi2895 ↔ 2927 By similarity
Disulfide bondi3127 ↔ 3150 By similarity
Disulfide bondi3302 ↔ 3330 By 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

ArrayExpressiQ16787.
BgeeiQ16787.
CleanExiHS_LAMA3.
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. 4 interactions.
IntActiQ16787. 3 interactions.
MINTiMINT-1431248.
STRINGi9606.ENSP00000324532.

Structurei

3D structure databases

ProteinModelPortaliQ16787.
SMRiQ16787. Positions 44-427.

Family & Domainsi

Domains and Repeats

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

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1852 – 194190 Reviewed prediction
Add
BLAST
Coiled coili1987 – 2169183 Reviewed prediction
Add
BLAST
Coiled coili2322 – 238867 Reviewed prediction
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi2278 – 22803Cell attachment site Reviewed prediction

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

Keywords - Domaini

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

Phylogenomic databases

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

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
IPR010307. Laminin_II.
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

MAAAARPRGR ALGPVLPPTP LLLLVLRVLP ACGATARDPG AAAGLSLHPT     50
YFNLAEAARI WATATCGERG PGEGRPQPEL YCKLVGGPTA PGSGHTIQGQ 100
FCDYCNSEDP RKAHPVTNAI DGSERWWQSP PLSSGTQYNR VNLTLDLGQL 150
FHVAYILIKF ANSPRPDLWV LERSVDFGST YSPWQYFAHS KVDCLKEFGR 200
EANMAVTRDD DVLCVTEYSR IVPLENGEVV VSLINGRPGA KNFTFSHTLR 250
EFTKATNIRL RFLRTNTLLG HLISKAQRDP TVTRRYYYSI KDISIGGQCV 300
CNGHAEVCNI NNPEKLFRCE CQHHTCGETC DRCCTGYNQR RWRPAAWEQS 350
HECEACNCHG HASNCYYDPD VERQQASLNT QGIYAGGGVC INCQHNTAGV 400
NCEQCAKGYY RPYGVPVDAP DGCIPCSCDP EHADGCEQGS GRCHCKPNFH 450
GDNCEKCAIG YYNFPFCLRI PIFPVSTPSS EDPVAGDIKG CDCNLEGVLP 500
EICDAHGRCL CRPGVEGPRC DTCRSGFYSF PICQACWCSA LGSYQMPCSS 550
VTGQCECRPG VTGQRCDRCL SGAYDFPHCQ GSSSACDPAG TINSNLGYCQ 600
CKLHVEGPTC SRCKLLYWNL DKENPSGCSE CKCHKAGTVS GTGECRQGDG 650
DCHCKSHVGG DSCDTCEDGY FALEKSNYFG CQGCQCDIGG ALSSMCSGPS 700
GVCQCREHVV GKVCQRPENN YYFPDLHHMK YEIEDGSTPN GRDLRFGFDP 750
LAFPEFSWRG YAQMTSVQND VRITLNVGKS SGSLFRVILR YVNPGTEAVS 800
GHITIYPSWG AAQSKEIIFL PSKEPAFVTV PGNGFADPFS ITPGIWVACI 850
KAEGVLLDYL VLLPRDYYEA SVLQLPVTEP CAYAGPPQEN CLLYQHLPVT 900
RFPCTLACEA RHFLLDGEPR PVAVRQPTPA HPVMVDLSGR EVELHLRLRI 950
PQVGHYVVVV EYSTEAAQLF VVDVNVKSSG SVLAGQVNIY SCNYSVLCRS 1000
AVIDHMSRIA MYELLADADI QLKGHMARFL LHQVCIIPIE EFSAEYVRPQ 1050
VHCIASYGRF VNQSATCVSL AHETPPTALI LDVLSGRPFP HLPQQSSPSV 1100
DVLPGVTLKA PQNQVTLRGR VPHLGRYVFV IHFYQAAHPT FPAQVSVDGG 1150
WPRAGSFHAS FCPHVLGCRD QVIAEGQIEF DISEPEVAAT VKVPEGKSLV 1200
LVRVLVVPAE NYDYQILHKK SMDKSLEFIT NCGKNSFYLD PQTASRFCKN 1250
SARSLVAFYH KGALPCECHP TGATGPHCSP EGGQCPCQPN VIGRQCTRCA 1300
TGHYGFPRCK PCSCGRRLCE EMTGQCRCPP RTVRPQCEVC ETHSFSFHPM 1350
AGCEGCNCSR RGTIEAAMPE CDRDSGQCRC KPRITGRQCD RCASGFYRFP 1400
ECVPCNCNRD GTEPGVCDPG TGACLCKENV EGTECNVCRE GSFHLDPANL 1450
KGCTSCFCFG VNNQCHSSHK RRTKFVDMLG WHLETADRVD IPVSFNPGSN 1500
SMVADLQELP ATIHSASWVA PTSYLGDKVS SYGGYLTYQA KSFGLPGDMV 1550
LLEKKPDVQL TGQHMSIIYE ETNTPRPDRL HHGRVHVVEG NFRHASSRAP 1600
VSREELMTVL SRLADVRIQG LYFTETQRLT LSEVGLEEAS DTGSGRIALA 1650
VEICACPPAY AGDSCQGCSP GYYRDHKGLY TGRCVPCNCN GHSNQCQDGS 1700
GICVNCQHNT AGEHCERCQE GYYGNAVHGS CRACPCPHTN SFATGCVVNG 1750
GDVRCSCKAG YTGTQCERCA PGYFGNPQKF GGSCQPCSCN SNGQLGSCHP 1800
LTGDCINQEP KDSSPAEECD DCDSCVMTLL NDLATMGEQL RLVKSQLQGL 1850
SASAGLLEQM RHMETQAKDL RNQLLNYRSA ISNHGSKIEG LERELTDLNQ 1900
EFETLQEKAQ VNSRKAQTLN NNVNRATQSA KELDVKIKNV IRNVHILLKQ 1950
ISGTDGEGNN VPSGDFSREW AEAQRMMREL RNRNFGKHLR EAEADKRESQ 2000
LLLNRIRTWQ KTHQGENNGL ANSIRDSLNE YEAKLSDLRA RLQEAAAQAK 2050
QANGLNQENE RALGAIQRQV KEINSLQSDF TKYLTTADSS LLQTNIALQL 2100
MEKSQKEYEK LAASLNEARQ ELSDKVRELS RSAGKTSLVE EAEKHARSLQ 2150
ELAKQLEEIK RNASGDELVR CAVDAATAYE NILNAIKAAE DAANRAASAS 2200
ESALQTVIKE DLPRKAKTLS SNSDKLLNEA KMTQKKLKQE VSPALNNLQQ 2250
TLNIVTVQKE VIDTNLTTLR DGLHGIQRGD IDAMISSAKS MVRKANDITD 2300
EVLDGLNPIQ TDVERIKDTY GRTQNEDFKK ALTDADNSVN KLTNKLPDLW 2350
RKIESINQQL LPLGNISDNM DRIRELIQQA RDAASKVAVP MRFNGKSGVE 2400
VRLPNDLEDL KGYTSLSLFL QRPNSRENGG TENMFVMYLG NKDASRDYIG 2450
MAVVDGQLTC VYNLGDREAE LQVDQILTKS ETKEAVMDRV KFQRIYQFAR 2500
LNYTKGATSS KPETPGVYDM DGRNSNTLLN LDPENVVFYV GGYPPDFKLP 2550
SRLSFPPYKG CIELDDLNEN VLSLYNFKKT FNLNTTEVEP CRRRKEESDK 2600
NYFEGTGYAR VPTQPHAPIP TFGQTIQTTV DRGLLFFAEN GDRFISLNIE 2650
DGKLMVRYKL NSELPKERGV GDAINNGRDH SIQIKIGKLQ KRMWINVDVQ 2700
NTIIDGEVFD FSTYYLGGIP IAIRERFNIS TPAFRGCMKN LKKTSGVVRL 2750
NDTVGVTKKC SEDWKLVRSA SFSRGGQLSF TDLGLPPTDH LQASFGFQTF 2800
QPSGILLDHQ TWTRNLQVTL EDGYIELSTS DSGSPIFKSP QTYMDGLLHY 2850
VSVISDNSGL RLLIDDQLLR NSKRLKHISS SRQSLRLGGS NFEGCISNVF 2900
VQRLSLSPEV LDLTSNSLKR DVSLGGCSLN KPPFLMLLKG STRFNKTKTF 2950
RINQLLQDTP VASPRSVKVW QDACSPLPKT QANHGALQFG DIPTSHLLFK 3000
LPQELLKPRS QFAVDMQTTS SRGLVFHTGT KNSFMALYLS KGRLVFALGT 3050
DGKKLRIKSK EKCNDGKWHT VVFGHDGEKG RLVVDGLRAR EGSLPGNSTI 3100
SIRAPVYLGS PPSGKPKSLP TNSFVGCLKN FQLDSKPLYT PSSSFGVSSC 3150
LGGPLEKGIY FSEEGGHVVL AHSVLLGPEF KLVFSIRPRS LTGILIHIGS 3200
QPGKHLCVYL EAGKVTASMD SGAGGTSTSV TPKQSLCDGQ WHSVAVTIKQ 3250
HILHLELDTD SSYTAGQIPF PPASTQEPLH LGGAPANLTT LRIPVWKSFF 3300
GCLRNIHVNH IPVPVTEALE VQGPVSLNGC PDQ 3333
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

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.
VSP_035738Add
BLAST
Alternative sequencei1 – 16091609Missing in isoform 4.
VSP_047079Add
BLAST
Alternative sequencei1610 – 166556LSRLA…AGDSC → MPPAVRRSACSMGWLWIFGA ALGQCLGYSSQQQRVPFLQP PGQSQLQASYVEFRPS in isoform 4.
VSP_047080Add
BLAST
Alternative sequencei1621 – 166545LYFTE…AGDSC → MPPAVRRSACSMGWLWIFGA ALGQCLGYSSQQQRVPFLQP PGQSQLQASYVEFRPS in isoform 1.
VSP_035739Add
BLAST
Alternative sequencei1946 – 200257ILLKQ…ESQLL → M in isoform 3 and isoform 4.
VSP_043487Add
BLAST

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSiCCDS42419.1. [Q16787-2]
CCDS45838.1. [Q16787-3]
CCDS59307.1. [Q16787-4]
PIRiA55347.
RefSeqiNP_000218.2. NM_000227.3.
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

EnsembliENST00000269217; ENSP00000269217; ENSG00000053747.
ENST00000313654; ENSP00000324532; ENSG00000053747. [Q16787-2]
ENST00000399516; ENSP00000382432; ENSG00000053747. [Q16787-3]
ENST00000587184; ENSP00000466557; ENSG00000053747. [Q16787-4]
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:
EMBL
GenBank
DDBJ
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 CCDS42419.1. [Q16787-2 ]
CCDS45838.1. [Q16787-3 ]
CCDS59307.1. [Q16787-4 ]
PIRi A55347.
RefSeqi NP_000218.2. NM_000227.3.
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...

Protein-protein interaction databases

BioGridi 110103. 4 interactions.
IntActi Q16787. 3 interactions.
MINTi MINT-1431248.
STRINGi 9606.ENSP00000324532.

Chemistry

ChEMBLi CHEMBL2364187.
DrugBanki DB00009. Alteplase.
DB00029. Anistreplase.
DB00015. Reteplase.
DB00031. Tenecteplase.

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 ENST00000269217 ; ENSP00000269217 ; ENSG00000053747 .
ENST00000313654 ; ENSP00000324532 ; ENSG00000053747 . [Q16787-2 ]
ENST00000399516 ; ENSP00000382432 ; ENSG00000053747 . [Q16787-3 ]
ENST00000587184 ; ENSP00000466557 ; ENSG00000053747 . [Q16787-4 ]
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.
HOGENOMi HOG000231235.
HOVERGENi HBG052300.
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

ArrayExpressi Q16787.
Bgeei Q16787.
CleanExi HS_LAMA3.
Genevestigatori Q16787.

Family and domain databases

Gene3Di 2.60.120.200. 5 hits.
InterProi IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
IPR010307. Laminin_II.
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: September 3, 2014
This is version 147 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

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