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Q16787 (LAMA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:LAMA3
Synonyms:LAMNA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3333 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

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.

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-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).

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane. Note: Major component.

Tissue specificity

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.

Induction

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

Domain

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.

Involvement in disease

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. Ref.1

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. Ref.1

Sequence similarities

Contains 15 laminin EGF-like domains.

Contains 5 laminin G-like domains.

Contains 1 laminin IV type A domain.

Contains 1 laminin N-terminal domain.

Ontologies

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: Q16787-2)

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.
Isoform 1 (identifier: Q16787-1)

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
Isoform 3 (identifier: Q16787-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1946-2002: ILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLL → M
Isoform 4 (identifier: Q16787-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Chain36 – 33333298Laminin subunit alpha-3
PRO_0000017058

Regions

Domain43 – 298256Laminin N-terminal
Domain299 – 35557Laminin EGF-like 1
Domain356 – 42570Laminin EGF-like 2
Domain426 – 46944Laminin EGF-like 3
Domain491 – 53545Laminin EGF-like 4
Domain536 – 58853Laminin EGF-like 5
Domain590 – 63041Laminin EGF-like 6
Domain631 – 68353Laminin EGF-like 7
Domain684 – 72845Laminin EGF-like 8
Domain1266 – 131146Laminin EGF-like 9
Domain1312 – 135544Laminin EGF-like 10
Domain1356 – 140449Laminin EGF-like 11
Domain1405 – 145551Laminin EGF-like 12
Domain1476 – 1653178Laminin IV type A
Domain1687 – 173347Laminin EGF-like 13
Domain1734 – 178653Laminin EGF-like 14
Domain1787 – 182135Laminin EGF-like 15; truncated
Domain2390 – 2591202Laminin G-like 1
Domain2598 – 2760163Laminin G-like 2
Domain2767 – 2927161Laminin G-like 3
Domain2986 – 3150165Laminin G-like 4
Domain3157 – 3330174Laminin G-like 5
Region298 – 728431Domain V
Region796 – 1265470Domain IV 1 (domain IV B)
Region1266 – 1465200Domain III B
Region1654 – 1821168Domain III A
Region1822 – 2389568Domain II and I
Coiled coil1852 – 194190 Potential
Coiled coil1987 – 2169183 Potential
Coiled coil2322 – 238867 Potential
Motif2278 – 22803Cell attachment site Potential

Amino acid modifications

Glycosylation1421N-linked (GlcNAc...) Potential
Glycosylation2421N-linked (GlcNAc...) Potential
Glycosylation23651N-linked (GlcNAc...) Potential
Glycosylation25021N-linked (GlcNAc...) Potential
Glycosylation25841N-linked (GlcNAc...) Potential
Disulfide bond299 ↔ 308 By similarity
Disulfide bond301 ↔ 319 By similarity
Disulfide bond321 ↔ 330 By similarity
Disulfide bond333 ↔ 353 By similarity
Disulfide bond356 ↔ 365 By similarity
Disulfide bond358 ↔ 390 By similarity
Disulfide bond393 ↔ 402 By similarity
Disulfide bond405 ↔ 423 By similarity
Disulfide bond426 ↔ 436 By similarity
Disulfide bond428 ↔ 443 By similarity
Disulfide bond445 ↔ 454 By similarity
Disulfide bond457 ↔ 467 By similarity
Disulfide bond491 ↔ 503 By similarity
Disulfide bond493 ↔ 509 By similarity
Disulfide bond511 ↔ 520 By similarity
Disulfide bond523 ↔ 533 By similarity
Disulfide bond536 ↔ 548 By similarity
Disulfide bond538 ↔ 555 By similarity
Disulfide bond557 ↔ 566 By similarity
Disulfide bond569 ↔ 586 By similarity
Disulfide bond601 ↔ 610 By similarity
Disulfide bond613 ↔ 628 By similarity
Disulfide bond631 ↔ 645 By similarity
Disulfide bond633 ↔ 652 By similarity
Disulfide bond654 ↔ 663 By similarity
Disulfide bond666 ↔ 681 By similarity
Disulfide bond684 ↔ 696 By similarity
Disulfide bond686 ↔ 703 By similarity
Disulfide bond705 ↔ 714 By similarity
Disulfide bond1266 ↔ 1278 By similarity
Disulfide bond1268 ↔ 1285 By similarity
Disulfide bond1287 ↔ 1296 By similarity
Disulfide bond1299 ↔ 1309 By similarity
Disulfide bond1312 ↔ 1319 By similarity
Disulfide bond1314 ↔ 1326 By similarity
Disulfide bond1328 ↔ 1337 By similarity
Disulfide bond1340 ↔ 1353 By similarity
Disulfide bond1356 ↔ 1371 By similarity
Disulfide bond1358 ↔ 1378 By similarity
Disulfide bond1380 ↔ 1389 By similarity
Disulfide bond1392 ↔ 1402 By similarity
Disulfide bond1405 ↔ 1417 By similarity
Disulfide bond1407 ↔ 1424 By similarity
Disulfide bond1426 ↔ 1435 By similarity
Disulfide bond1438 ↔ 1453 By similarity
Disulfide bond1687 ↔ 1696 By similarity
Disulfide bond1689 ↔ 1703 By similarity
Disulfide bond1706 ↔ 1715 By similarity
Disulfide bond1718 ↔ 1731 By similarity
Disulfide bond1734 ↔ 1746 By similarity
Disulfide bond1736 ↔ 1755 By similarity
Disulfide bond1757 ↔ 1766 By similarity
Disulfide bond1769 ↔ 1784 By similarity
Disulfide bond1822Interchain Probable
Disulfide bond1825Interchain Probable
Disulfide bond2561 ↔ 2591 By similarity
Disulfide bond2737 ↔ 2760 By similarity
Disulfide bond2895 ↔ 2927 By similarity
Disulfide bond3127 ↔ 3150 By similarity
Disulfide bond3302 ↔ 3330 By similarity

Natural variations

Alternative sequence1 – 16201620Missing in isoform 1.
VSP_035738
Alternative sequence1 – 16091609Missing in isoform 4.
VSP_047079
Alternative sequence1610 – 166556LSRLA…AGDSC → MPPAVRRSACSMGWLWIFGA ALGQCLGYSSQQQRVPFLQP PGQSQLQASYVEFRPS in isoform 4.
VSP_047080
Alternative sequence1621 – 166545LYFTE…AGDSC → MPPAVRRSACSMGWLWIFGA ALGQCLGYSSQQQRVPFLQP PGQSQLQASYVEFRPS in isoform 1.
VSP_035739
Alternative sequence1946 – 200257ILLKQ…ESQLL → M in isoform 3 and isoform 4.
VSP_043487
Natural variant7961T → N.
Corresponds to variant rs17187262 [ dbSNP | Ensembl ].
VAR_050078
Natural variant12061V → A.
Corresponds to variant rs12457323 [ dbSNP | Ensembl ].
VAR_050079
Natural variant12081P → T.
Corresponds to variant rs17202961 [ dbSNP | Ensembl ].
VAR_050080
Natural variant17741F → L.
Corresponds to variant rs958631 [ dbSNP | Ensembl ].
VAR_059444
Natural variant27021T → A.
Corresponds to variant rs9952370 [ dbSNP | Ensembl ].
VAR_047374
Natural variant28151N → K.
Corresponds to variant rs1154232 [ dbSNP | Ensembl ].
VAR_047375
Natural variant28341S → G. Ref.2 Ref.6 Ref.7
Corresponds to variant rs1154233 [ dbSNP | Ensembl ].
VAR_059445

Experimental info

Sequence conflict15441G → A in CAA59429. Ref.5
Sequence conflict15441G → A in CAA59325. Ref.6
Sequence conflict1743 – 17453ATG → GMC in CAA59428. Ref.5
Sequence conflict1743 – 17453ATG → GMC in CAA59429. Ref.5
Sequence conflict21011M → K in CAA59428. Ref.5
Sequence conflict21011M → K in CAA59429. Ref.5
Sequence conflict23741R → L in CAA59428. Ref.5
Sequence conflict23741R → L in CAA59429. Ref.5
Sequence conflict25891E → Q in CAA59428. Ref.5
Sequence conflict25891E → Q in CAA59429. Ref.5
Sequence conflict26721D → A in CAA59428. Ref.5
Sequence conflict26721D → A in CAA59429. Ref.5
Sequence conflict28041G → A in CAA59428. Ref.5
Sequence conflict28041G → A in CAA59429. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 (B) [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 9F99AF49B8EF27DD

FASTA3,333366,649
        10         20         30         40         50         60 
MAAAARPRGR ALGPVLPPTP LLLLVLRVLP ACGATARDPG AAAGLSLHPT YFNLAEAARI 

        70         80         90        100        110        120 
WATATCGERG PGEGRPQPEL YCKLVGGPTA PGSGHTIQGQ FCDYCNSEDP RKAHPVTNAI 

       130        140        150        160        170        180 
DGSERWWQSP PLSSGTQYNR VNLTLDLGQL FHVAYILIKF ANSPRPDLWV LERSVDFGST 

       190        200        210        220        230        240 
YSPWQYFAHS KVDCLKEFGR EANMAVTRDD DVLCVTEYSR IVPLENGEVV VSLINGRPGA 

       250        260        270        280        290        300 
KNFTFSHTLR EFTKATNIRL RFLRTNTLLG HLISKAQRDP TVTRRYYYSI KDISIGGQCV 

       310        320        330        340        350        360 
CNGHAEVCNI NNPEKLFRCE CQHHTCGETC DRCCTGYNQR RWRPAAWEQS HECEACNCHG 

       370        380        390        400        410        420 
HASNCYYDPD VERQQASLNT QGIYAGGGVC INCQHNTAGV NCEQCAKGYY RPYGVPVDAP 

       430        440        450        460        470        480 
DGCIPCSCDP EHADGCEQGS GRCHCKPNFH GDNCEKCAIG YYNFPFCLRI PIFPVSTPSS 

       490        500        510        520        530        540 
EDPVAGDIKG CDCNLEGVLP EICDAHGRCL CRPGVEGPRC DTCRSGFYSF PICQACWCSA 

       550        560        570        580        590        600 
LGSYQMPCSS VTGQCECRPG VTGQRCDRCL SGAYDFPHCQ GSSSACDPAG TINSNLGYCQ 

       610        620        630        640        650        660 
CKLHVEGPTC SRCKLLYWNL DKENPSGCSE CKCHKAGTVS GTGECRQGDG DCHCKSHVGG 

       670        680        690        700        710        720 
DSCDTCEDGY FALEKSNYFG CQGCQCDIGG ALSSMCSGPS GVCQCREHVV GKVCQRPENN 

       730        740        750        760        770        780 
YYFPDLHHMK YEIEDGSTPN GRDLRFGFDP LAFPEFSWRG YAQMTSVQND VRITLNVGKS 

       790        800        810        820        830        840 
SGSLFRVILR YVNPGTEAVS GHITIYPSWG AAQSKEIIFL PSKEPAFVTV PGNGFADPFS 

       850        860        870        880        890        900 
ITPGIWVACI KAEGVLLDYL VLLPRDYYEA SVLQLPVTEP CAYAGPPQEN CLLYQHLPVT 

       910        920        930        940        950        960 
RFPCTLACEA RHFLLDGEPR PVAVRQPTPA HPVMVDLSGR EVELHLRLRI PQVGHYVVVV 

       970        980        990       1000       1010       1020 
EYSTEAAQLF VVDVNVKSSG SVLAGQVNIY SCNYSVLCRS AVIDHMSRIA MYELLADADI 

      1030       1040       1050       1060       1070       1080 
QLKGHMARFL LHQVCIIPIE EFSAEYVRPQ VHCIASYGRF VNQSATCVSL AHETPPTALI 

      1090       1100       1110       1120       1130       1140 
LDVLSGRPFP HLPQQSSPSV DVLPGVTLKA PQNQVTLRGR VPHLGRYVFV IHFYQAAHPT 

      1150       1160       1170       1180       1190       1200 
FPAQVSVDGG WPRAGSFHAS FCPHVLGCRD QVIAEGQIEF DISEPEVAAT VKVPEGKSLV 

      1210       1220       1230       1240       1250       1260 
LVRVLVVPAE NYDYQILHKK SMDKSLEFIT NCGKNSFYLD PQTASRFCKN SARSLVAFYH 

      1270       1280       1290       1300       1310       1320 
KGALPCECHP TGATGPHCSP EGGQCPCQPN VIGRQCTRCA TGHYGFPRCK PCSCGRRLCE 

      1330       1340       1350       1360       1370       1380 
EMTGQCRCPP RTVRPQCEVC ETHSFSFHPM AGCEGCNCSR RGTIEAAMPE CDRDSGQCRC 

      1390       1400       1410       1420       1430       1440 
KPRITGRQCD RCASGFYRFP ECVPCNCNRD GTEPGVCDPG TGACLCKENV EGTECNVCRE 

      1450       1460       1470       1480       1490       1500 
GSFHLDPANL KGCTSCFCFG VNNQCHSSHK RRTKFVDMLG WHLETADRVD IPVSFNPGSN 

      1510       1520       1530       1540       1550       1560 
SMVADLQELP ATIHSASWVA PTSYLGDKVS SYGGYLTYQA KSFGLPGDMV LLEKKPDVQL 

      1570       1580       1590       1600       1610       1620 
TGQHMSIIYE ETNTPRPDRL HHGRVHVVEG NFRHASSRAP VSREELMTVL SRLADVRIQG 

      1630       1640       1650       1660       1670       1680 
LYFTETQRLT LSEVGLEEAS DTGSGRIALA VEICACPPAY AGDSCQGCSP GYYRDHKGLY 

      1690       1700       1710       1720       1730       1740 
TGRCVPCNCN GHSNQCQDGS GICVNCQHNT AGEHCERCQE GYYGNAVHGS CRACPCPHTN 

      1750       1760       1770       1780       1790       1800 
SFATGCVVNG GDVRCSCKAG YTGTQCERCA PGYFGNPQKF GGSCQPCSCN SNGQLGSCHP 

      1810       1820       1830       1840       1850       1860 
LTGDCINQEP KDSSPAEECD DCDSCVMTLL NDLATMGEQL RLVKSQLQGL SASAGLLEQM 

      1870       1880       1890       1900       1910       1920 
RHMETQAKDL RNQLLNYRSA ISNHGSKIEG LERELTDLNQ EFETLQEKAQ VNSRKAQTLN 

      1930       1940       1950       1960       1970       1980 
NNVNRATQSA KELDVKIKNV IRNVHILLKQ ISGTDGEGNN VPSGDFSREW AEAQRMMREL 

      1990       2000       2010       2020       2030       2040 
RNRNFGKHLR EAEADKRESQ LLLNRIRTWQ KTHQGENNGL ANSIRDSLNE YEAKLSDLRA 

      2050       2060       2070       2080       2090       2100 
RLQEAAAQAK QANGLNQENE RALGAIQRQV KEINSLQSDF TKYLTTADSS LLQTNIALQL 

      2110       2120       2130       2140       2150       2160 
MEKSQKEYEK LAASLNEARQ ELSDKVRELS RSAGKTSLVE EAEKHARSLQ ELAKQLEEIK 

      2170       2180       2190       2200       2210       2220 
RNASGDELVR CAVDAATAYE NILNAIKAAE DAANRAASAS ESALQTVIKE DLPRKAKTLS 

      2230       2240       2250       2260       2270       2280 
SNSDKLLNEA KMTQKKLKQE VSPALNNLQQ TLNIVTVQKE VIDTNLTTLR DGLHGIQRGD 

      2290       2300       2310       2320       2330       2340 
IDAMISSAKS MVRKANDITD EVLDGLNPIQ TDVERIKDTY GRTQNEDFKK ALTDADNSVN 

      2350       2360       2370       2380       2390       2400 
KLTNKLPDLW RKIESINQQL LPLGNISDNM DRIRELIQQA RDAASKVAVP MRFNGKSGVE 

      2410       2420       2430       2440       2450       2460 
VRLPNDLEDL KGYTSLSLFL QRPNSRENGG TENMFVMYLG NKDASRDYIG MAVVDGQLTC 

      2470       2480       2490       2500       2510       2520 
VYNLGDREAE LQVDQILTKS ETKEAVMDRV KFQRIYQFAR LNYTKGATSS KPETPGVYDM 

      2530       2540       2550       2560       2570       2580 
DGRNSNTLLN LDPENVVFYV GGYPPDFKLP SRLSFPPYKG CIELDDLNEN VLSLYNFKKT 

      2590       2600       2610       2620       2630       2640 
FNLNTTEVEP CRRRKEESDK NYFEGTGYAR VPTQPHAPIP TFGQTIQTTV DRGLLFFAEN 

      2650       2660       2670       2680       2690       2700 
GDRFISLNIE DGKLMVRYKL NSELPKERGV GDAINNGRDH SIQIKIGKLQ KRMWINVDVQ 

      2710       2720       2730       2740       2750       2760 
NTIIDGEVFD FSTYYLGGIP IAIRERFNIS TPAFRGCMKN LKKTSGVVRL NDTVGVTKKC 

      2770       2780       2790       2800       2810       2820 
SEDWKLVRSA SFSRGGQLSF TDLGLPPTDH LQASFGFQTF QPSGILLDHQ TWTRNLQVTL 

      2830       2840       2850       2860       2870       2880 
EDGYIELSTS DSGSPIFKSP QTYMDGLLHY VSVISDNSGL RLLIDDQLLR NSKRLKHISS 

      2890       2900       2910       2920       2930       2940 
SRQSLRLGGS NFEGCISNVF VQRLSLSPEV LDLTSNSLKR DVSLGGCSLN KPPFLMLLKG 

      2950       2960       2970       2980       2990       3000 
STRFNKTKTF RINQLLQDTP VASPRSVKVW QDACSPLPKT QANHGALQFG DIPTSHLLFK 

      3010       3020       3030       3040       3050       3060 
LPQELLKPRS QFAVDMQTTS SRGLVFHTGT KNSFMALYLS KGRLVFALGT DGKKLRIKSK 

      3070       3080       3090       3100       3110       3120 
EKCNDGKWHT VVFGHDGEKG RLVVDGLRAR EGSLPGNSTI SIRAPVYLGS PPSGKPKSLP 

      3130       3140       3150       3160       3170       3180 
TNSFVGCLKN FQLDSKPLYT PSSSFGVSSC LGGPLEKGIY FSEEGGHVVL AHSVLLGPEF 

      3190       3200       3210       3220       3230       3240 
KLVFSIRPRS LTGILIHIGS QPGKHLCVYL EAGKVTASMD SGAGGTSTSV TPKQSLCDGQ 

      3250       3260       3270       3280       3290       3300 
WHSVAVTIKQ HILHLELDTD SSYTAGQIPF PPASTQEPLH LGGAPANLTT LRIPVWKSFF 

      3310       3320       3330 
GCLRNIHVNH IPVPVTEALE VQGPVSLNGC PDQ 

« Hide

Isoform 1 (A) [UniParc].

Checksum: 0477C729951763A5
Show »

FASTA1,724190,491
Isoform 3 [UniParc].

Checksum: 3ACFFE998357122E
Show »

FASTA3,277360,212
Isoform 4 [UniParc].

Checksum: 9EBF5FC45637645C
Show »

FASTA1,668184,054

References

« Hide 'large scale' references
[1]"An unusual N-terminal deletion of the laminin alpha3a isoform leads to the chronic granulation tissue disorder laryngo-onycho-cutaneous syndrome."
McLean W.H.I., Irvine A.D., Hamill K.J., Whittock N.V., Coleman-Campbell C.M., Mellerio J.E., Ashton G.S., Dopping-Hepenstal P.J.H., Eady R.A.J., Jamil T., Phillips R.J., Shabbir S.G., Haroon T.S., Khurshid K., Moore J.E., Page B., Darling J., Atherton D.J. expand/collapse author list , Van Steensel M.A.M., Munro C.S., Smith F.J.D., McGrath J.A.
Hum. Mol. Genet. 12:2395-2409(2003) [PubMed] [Europe PMC] [Abstract]
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]"DNA sequence and analysis of human chromosome 18."
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. expand/collapse author list , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.
Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS42419.1. [Q16787-2]
CCDS45838.1. [Q16787-3]
CCDS59307.1. [Q16787-4]
PIRA55347.
RefSeqNP_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]
UniGeneHs.436367.

3D structure databases

ProteinModelPortalQ16787.
SMRQ16787. Positions 44-427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110103. 4 interactions.
IntActQ16787. 3 interactions.
MINTMINT-1431248.
STRING9606.ENSP00000324532.

Chemistry

ChEMBLCHEMBL2364187.
DrugBankDB00009. Alteplase.
DB00029. Anistreplase.
DB00015. Reteplase.
DB00031. Tenecteplase.

PTM databases

PhosphoSiteQ16787.

Polymorphism databases

DMDM215274012.

Proteomic databases

MaxQBQ16787.
PaxDbQ16787.
PRIDEQ16787.

Protocols and materials databases

DNASU3909.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000269217; ENSP00000269217; ENSG00000053747.
ENST00000313654; ENSP00000324532; ENSG00000053747. [Q16787-2]
ENST00000399516; ENSP00000382432; ENSG00000053747. [Q16787-3]
ENST00000587184; ENSP00000466557; ENSG00000053747. [Q16787-4]
GeneID3909.
KEGGhsa:3909.
UCSCuc002kuq.3. human. [Q16787-2]
uc002kur.3. human. [Q16787-3]

Organism-specific databases

CTD3909.
GeneCardsGC18P021269.
GeneReviewsLAMA3.
HGNCHGNC:6483. LAMA3.
HPACAB010757.
HPA009309.
MIM226700. phenotype.
245660. phenotype.
600805. gene.
neXtProtNX_Q16787.
Orphanet79402. Generalized junctional epidermolysis bullosa, non-Herlitz type.
79404. Junctional epidermolysis bullosa, Herlitz type.
2407. LOC syndrome.
PharmGKBPA30272.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG292643.
HOGENOMHOG000231235.
HOVERGENHBG052300.
KOK06240.
OMARGLYFTE.
OrthoDBEOG7DFXB9.
PhylomeDBQ16787.
TreeFamTF335359.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ16787.
BgeeQ16787.
CleanExHS_LAMA3.
GenevestigatorQ16787.

Family and domain databases

Gene3D2.60.120.200. 5 hits.
InterProIPR008985. 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]
PfamPF00052. 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]
SMARTSM00180. EGF_Lam. 14 hits.
SM00281. LamB. 1 hit.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 5 hits.
PROSITEPS00022. 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]
ProtoNetSearch...

Other

ChiTaRSLAMA3. human.
GeneWikiLaminin,_alpha_3.
GenomeRNAi3909.
NextBio15345.
PMAP-CutDBQ6VU68.
PROQ16787.
SOURCESearch...

Entry information

Entry nameLAMA3_HUMAN
AccessionPrimary (citable) accession number: Q16787
Secondary accession number(s): B0YJ33 expand/collapse secondary AC list , Q13679, Q13680, Q6VU67, Q6VU68, Q6VU69, Q76E14, Q96TG0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM