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Protein

Laminin subunit alpha

Gene

LanA

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: 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. Activates presynaptic signaling involving integrin alpha-PS3/beta-nu and Fak to suppress neuromuscular junction (NMJ) growth during larval development and during low crawling activity, but not during higher-crawling conditions. Mediates, together with integrin alpha-PS3/beta-nu, glutamate receptor-modulated NMJ growth.2 Publications

GO - Biological processi

  • axon guidance Source: FlyBase
  • brain morphogenesis Source: FlyBase
  • cell adhesion mediated by integrin Source: FlyBase
  • dorsal trunk growth, open tracheal system Source: FlyBase
  • female meiosis chromosome segregation Source: FlyBase
  • heart development Source: FlyBase
  • imaginal disc-derived wing morphogenesis Source: FlyBase
  • inter-male aggressive behavior Source: FlyBase
  • locomotion involved in locomotory behavior Source: FlyBase
  • melanotic encapsulation of foreign target Source: FlyBase
  • mesoderm development Source: FlyBase
  • negative regulation of synaptic growth at neuromuscular junction Source: FlyBase
  • regulation of cell adhesion Source: InterPro
  • regulation of cell migration Source: InterPro
  • regulation of embryonic development Source: InterPro
  • regulation of glucose metabolic process Source: FlyBase
  • startle response Source: FlyBase
  • substrate adhesion-dependent cell spreading Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-DME-446107. Type I hemidesmosome assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit alpha
Alternative name(s):
Laminin A chain
Gene namesi
Name:LanA
Synonyms:lamA
ORF Names:CG10236
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0002526. LanA.

Subcellular locationi

GO - Cellular componenti

  • axon Source: UniProtKB-SubCell
  • basal lamina Source: FlyBase
  • basement membrane Source: FlyBase
  • cell junction Source: UniProtKB-KW
  • presynaptic periactive zone Source: FlyBase
  • synaptic vesicle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Cell junction, Cell projection, Cytoplasmic vesicle, Extracellular matrix, Secreted, Synapse

Pathology & Biotechi

Disruption phenotypei

Flies show late embryonic lethality. Certain partial loss-of-function mutations give raise to escaper adults, which have rough eyes associated with changes in cell fate and pattern, misshappen legs and defects in wing structure.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000001706423 – 3712Laminin subunit alphaAdd BLAST3690

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi116N-linked (GlcNAc...)Sequence analysis1
Glycosylationi219N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi273 ↔ 282By similarity
Disulfide bondi275 ↔ 296By similarity
Disulfide bondi298 ↔ 307By similarity
Disulfide bondi310 ↔ 330By similarity
Disulfide bondi333 ↔ 342By similarity
Disulfide bondi335 ↔ 367By similarity
Disulfide bondi370 ↔ 379By similarity
Disulfide bondi382 ↔ 400By similarity
Glycosylationi395N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi403 ↔ 414By similarity
Disulfide bondi405 ↔ 421By similarity
Disulfide bondi423 ↔ 432By similarity
Disulfide bondi435 ↔ 445By similarity
Disulfide bondi448 ↔ 460By similarity
Disulfide bondi450 ↔ 468By similarity
Glycosylationi453N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi470 ↔ 479By similarity
Disulfide bondi482 ↔ 492By similarity
Disulfide bondi495 ↔ 507By similarity
Disulfide bondi497 ↔ 514By similarity
Glycosylationi508N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi516 ↔ 525By similarity
Disulfide bondi528 ↔ 538By similarity
Disulfide bondi541 ↔ 553By similarity
Disulfide bondi543 ↔ 560By similarity
Disulfide bondi562 ↔ 571By similarity
Disulfide bondi574 ↔ 584By similarity
Disulfide bondi587 ↔ 599By similarity
Glycosylationi588N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi589 ↔ 605By similarity
Disulfide bondi607 ↔ 616By similarity
Disulfide bondi619 ↔ 629By similarity
Disulfide bondi632 ↔ 644By similarity
Disulfide bondi634 ↔ 650By similarity
Disulfide bondi652 ↔ 661By similarity
Disulfide bondi664 ↔ 674By similarity
Disulfide bondi677 ↔ 691By similarity
Disulfide bondi679 ↔ 700By similarity
Disulfide bondi702 ↔ 711By similarity
Disulfide bondi714 ↔ 729By similarity
Glycosylationi722N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi732 ↔ 746By similarity
Disulfide bondi734 ↔ 753By similarity
Disulfide bondi755 ↔ 764By similarity
Disulfide bondi767 ↔ 782By similarity
Disulfide bondi785 ↔ 797By similarity
Disulfide bondi787 ↔ 804By similarity
Disulfide bondi806 ↔ 815By similarity
Glycosylationi897N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1352N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1375 ↔ 1387By similarity
Disulfide bondi1377 ↔ 1394By similarity
Disulfide bondi1396 ↔ 1405By similarity
Disulfide bondi1408 ↔ 1418By similarity
Disulfide bondi1421 ↔ 1429By similarity
Disulfide bondi1423 ↔ 1436By similarity
Disulfide bondi1438 ↔ 1447By similarity
Disulfide bondi1450 ↔ 1463By similarity
Disulfide bondi1466 ↔ 1480By similarity
Disulfide bondi1468 ↔ 1487By similarity
Glycosylationi1484N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1489 ↔ 1498By similarity
Disulfide bondi1501 ↔ 1511By similarity
Disulfide bondi1514 ↔ 1526By similarity
Disulfide bondi1516 ↔ 1533By similarity
Disulfide bondi1535 ↔ 1544By similarity
Disulfide bondi1547 ↔ 1562By similarity
Glycosylationi1583N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1617N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1778 ↔ 1787By similarity
Disulfide bondi1790 ↔ 1806By similarity
Disulfide bondi1809 ↔ 1818By similarity
Disulfide bondi1811 ↔ 1825By similarity
Disulfide bondi1828 ↔ 1837By similarity
Disulfide bondi1840 ↔ 1856By similarity
Glycosylationi1847N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1859 ↔ 1874By similarity
Disulfide bondi1861 ↔ 1885By similarity
Disulfide bondi1887 ↔ 1896By similarity
Disulfide bondi1899 ↔ 1914By similarity
Disulfide bondi1917 ↔ 1931By similarity
Disulfide bondi1919 ↔ 1938By similarity
Disulfide bondi1941 ↔ 1950By similarity
Glycosylationi1943N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1953 ↔ 1967By similarity
Disulfide bondi1970 ↔ 1980By similarity
Disulfide bondi1972 ↔ 1987By similarity
Disulfide bondi1989 ↔ 1998By similarity
Disulfide bondi2001 ↔ 2014By similarity
Disulfide bondi2017 ↔ 2028By similarity
Disulfide bondi2019 ↔ 2035By similarity
Glycosylationi2024N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2037 ↔ 2046By similarity
Disulfide bondi2049 ↔ 2061By similarity
Disulfide bondi2064 ↔ 2076By similarity
Disulfide bondi2066 ↔ 2083By similarity
Disulfide bondi2085 ↔ 2094By similarity
Disulfide bondi2097 ↔ 2109By similarity
Disulfide bondi2112InterchainCurated
Disulfide bondi2115InterchainCurated
Glycosylationi2196N-linked (GlcNAc...)1 Publication1
Glycosylationi2215N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2267N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2301N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2323N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2482N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2524N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2538N-linked (GlcNAc...)1 Publication1
Glycosylationi2569N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2699N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2720N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2890N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2938N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3010N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3022 ↔ 3048By similarity
Glycosylationi3070N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3196 ↔ 3223By similarity
Glycosylationi3491N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3505 ↔ 3528By similarity
Glycosylationi3612N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3682 ↔ 3709By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ00174.
PRIDEiQ00174.

Expressioni

Tissue specificityi

Newly formed mesoderm and later prominently expressed in hemocytes, which also synthesize collagen IV. Expressed in muscles.2 Publications

Developmental stagei

During morphogenesis, mostly in embryo development at 10-12 hours.1 Publication

Gene expression databases

BgeeiFBgn0002526.
ExpressionAtlasiQ00174. baseline.
GenevisibleiQ00174. DM.

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.

Protein-protein interaction databases

BioGridi64176. 12 interactors.
IntActiQ00174. 9 interactors.
MINTiMINT-754541.
STRINGi7227.FBpp0076722.

Structurei

3D structure databases

ProteinModelPortaliQ00174.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini23 – 272Laminin N-terminalPROSITE-ProRule annotationAdd BLAST250
Domaini273 – 332Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST60
Domaini333 – 402Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST70
Domaini403 – 447Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST45
Domaini448 – 494Laminin EGF-like 4PROSITE-ProRule annotationAdd BLAST47
Domaini495 – 540Laminin EGF-like 5PROSITE-ProRule annotationAdd BLAST46
Domaini541 – 586Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST46
Domaini587 – 631Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST45
Domaini632 – 676Laminin EGF-like 8PROSITE-ProRule annotationAdd BLAST45
Domaini677 – 731Laminin EGF-like 9PROSITE-ProRule annotationAdd BLAST55
Domaini732 – 784Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST53
Domaini785 – 815Laminin EGF-like 11; truncatedPROSITE-ProRule annotationAdd BLAST31
Domaini1375 – 1420Laminin EGF-like 12PROSITE-ProRule annotationAdd BLAST46
Domaini1421 – 1465Laminin EGF-like 13PROSITE-ProRule annotationAdd BLAST45
Domaini1466 – 1513Laminin EGF-like 14PROSITE-ProRule annotationAdd BLAST48
Domaini1514 – 1564Laminin EGF-like 15PROSITE-ProRule annotationAdd BLAST51
Domaini1565 – 1574Laminin EGF-like 16; first partPROSITE-ProRule annotation10
Domaini1585 – 1775Laminin IV type APROSITE-ProRule annotationAdd BLAST191
Domaini1776 – 1808Laminin EGF-like 16; second partPROSITE-ProRule annotationAdd BLAST33
Domaini1809 – 1858Laminin EGF-like 17PROSITE-ProRule annotationAdd BLAST50
Domaini1859 – 1916Laminin EGF-like 18PROSITE-ProRule annotationAdd BLAST58
Domaini1917 – 1969Laminin EGF-like 19PROSITE-ProRule annotationAdd BLAST53
Domaini1970 – 2016Laminin EGF-like 20PROSITE-ProRule annotationAdd BLAST47
Domaini2017 – 2063Laminin EGF-like 21PROSITE-ProRule annotationAdd BLAST47
Domaini2064 – 2111Laminin EGF-like 22PROSITE-ProRule annotationAdd BLAST48
Domaini2672 – 2868Laminin G-like 1PROSITE-ProRule annotationAdd BLAST197
Domaini2876 – 3048Laminin G-like 2PROSITE-ProRule annotationAdd BLAST173
Domaini3055 – 3223Laminin G-like 3PROSITE-ProRule annotationAdd BLAST169
Domaini3349 – 3528Laminin G-like 4PROSITE-ProRule annotationAdd BLAST180
Domaini3534 – 3709Laminin G-like 5PROSITE-ProRule annotationAdd BLAST176

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni816 – 1374Domain IV''Add BLAST559
Regioni2112 – 2671Domain II and IAdd BLAST560

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili2178 – 2249Sequence analysisAdd BLAST72
Coiled coili2301 – 2321Sequence analysisAdd BLAST21
Coiled coili2376 – 2450Sequence analysisAdd BLAST75
Coiled coili2541 – 2676Sequence analysisAdd BLAST136

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi3270 – 3296Poly-ThrAdd BLAST27

Domaini

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

Sequence similaritiesi

Contains 22 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

eggNOGiKOG1836. Eukaryota.
ENOG410XRDC. LUCA.
InParanoidiQ00174.
KOiK06240.
OrthoDBiEOG091G005L.
PhylomeDBiQ00174.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR013320. ConA-like_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR009254. Laminin_aI.
IPR010307. Laminin_domII.
IPR002049. Laminin_EGF.
IPR001791. Laminin_G.
IPR000034. Laminin_IV.
IPR008211. Laminin_N.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 20 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]
SMARTiSM00181. EGF. 14 hits.
SM00180. EGF_Lam. 21 hits.
SM01411. Ephrin_rec_like. 4 hits.
SM00281. LamB. 1 hit.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 5 hits.
PROSITEiPS00022. EGF_1. 17 hits.
PS01186. EGF_2. 5 hits.
PS01248. EGF_LAM_1. 19 hits.
PS50027. EGF_LAM_2. 22 hits.
PS50025. LAM_G_DOMAIN. 5 hits.
PS51115. LAMININ_IVA. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q00174-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGHGVASIGA LLVILAISYC QAELTPPYFN LATGRKIYAT ATCGQDTDGP
60 70 80 90 100
ELYCKLVGAN TEHDHIDYSV IQGQVCDYCD PTVPERNHPP ENAIDGTEAW
110 120 130 140 150
WQSPPLSRGM KFNEVNLTIN FEQEFHVAYL FIRMGNSPRP GLWTLEKSTD
160 170 180 190 200
YGKTWTPWQH FSDTPADCET YFGKDTYKPI TRDDDVICTT EYSKIVPLEN
210 220 230 240 250
GEIPVMLLNE RPSSTNYFNS TVLQEWTRAT NVRIRLLRTK NLLGHLMSVA
260 270 280 290 300
RQDPTVTRRY FYSIKDISIG GRCMCNGHAD TCDVKDPKSP VRILACRCQH
310 320 330 340 350
HTCGIQCNEC CPGFEQKKWR QNTNARPFNC EPCNCHGHSN ECKYDEEVNR
360 370 380 390 400
KGLSLDIHGH YDGGGVCQNC QHNTVGINCN KCKPKYYRPK GKHWNETDVC
410 420 430 440 450
SPCQCDYFFS TGHCEEETGN CECRAAFQPP SCDSCAYGYY GYPNCRECEC
460 470 480 490 500
NLNGTNGYHC EAESGQQCPC KINFAGAYCK QCAEGYYGFP ECKACECNKI
510 520 530 540 550
GSITNDCNVT TGECKCLTNF GGDNCERCKH GYFNYPTCSY CDCDNQGTES
560 570 580 590 600
EICNKQSGQC ICREGFGGPR CDQCLPGFYN YPDCKPCNCS STGSSAITCD
610 620 630 640 650
NTGKCNCLNN FAGKQCTLCT AGYYSYPDCL PCHCDSHGSQ GVSCNSDGQC
660 670 680 690 700
LCQPNFDGRQ CDSCKEGFYN FPSCEDCNCD PAGVIDKFAG CGSVPVGELC
710 720 730 740 750
KCKERVTGRI CNECKPLYWN LNISNTEGCE ICDCWTDGTI SALDTCTSKS
760 770 780 790 800
GQCPCKPHTQ GRRCQECRDG TFDLDSASLF GCKDCSCDVG GSWQSVCDKI
810 820 830 840 850
SGQCKCHPRI TGLACTQPLT THFFPTLHQF QYEYEDGSLP SGTQVRYDYD
860 870 880 890 900
EAAFPGFSSK GYVVFNAIQN DVRNEVNVFK SSLYRIVLRY VNPNAENVTA
910 920 930 940 950
TISVTSDNPL EVDQHVKVLL QPTSEPQFVT VAGPLGVKPS AIVLDPGRYV
960 970 980 990 1000
FTTKANKNVM LDYFVLLPAA YYEAGILTRH ISNPCELGNM ELCRHYKYAS
1010 1020 1030 1040 1050
VEVFSPAATP FVIGENSKPT NPVETYTDPE HLQIVSHVGD IPVLSGSQNE
1060 1070 1080 1090 1100
LHYIVDVPRS GRYIFVIDYI SDRNFPDSYY INLKLKDNPD SETSVLLYPC
1110 1120 1130 1140 1150
LYSTICRTSV NEDGMEKSFY INKEDLQPVI ISADIEDGSR FPIISVTAIP
1160 1170 1180 1190 1200
VDQWSIDYIN PSPVCVIHDQ QCATPKFRSV PDSKKIEFET DHEDRIATNK
1210 1220 1230 1240 1250
PPYASLDERV KLVHLDSQNE ATIVIESKVD ATKPNLFVIL VKYYQPSHPK
1260 1270 1280 1290 1300
YQVYYTLTAG KNQYDGKFDI QHCPSSSGCR GVIRPAGEGS FEIDDEFKFT
1310 1320 1330 1340 1350
ITTDRSQSVW LDYLVVVPLK QYNDDLLVEE TFDQTKEFIQ NCGHDHFHIT
1360 1370 1380 1390 1400
HNASDFCKKS VFSLTADYNS GALPCNCDYA GSTSFECHPF GGQCQCKPNV
1410 1420 1430 1440 1450
IERTCGACRS RYYGFPDCKP CKCPNSAMCE PTTGECMCPP NVIGDLCEKC
1460 1470 1480 1490 1500
APNTYGFHQV IGCEECACNP MGIANGNSQC DLFNGTCECR QNIEGRACDV
1510 1520 1530 1540 1550
CSNGYFNFPH CEQCSCHKPG TELEVCDKID GACFCKKNVV GRDCDQCVDG
1560 1570 1580 1590 1600
TYNLQESNPD GCTTCFCFGK TSRCDSAYLR VYNVSLLKHV SITTPEFHEE
1610 1620 1630 1640 1650
SIKFDMWPVP ADEILLNETT LKADFTLREV NDERPAYFGV LDYLLNQNNH
1660 1670 1680 1690 1700
ISAYGGDLAY TLHFTSGFDG KYIVAPDVIL FSEHNALVHT SYEQPSRNEP
1710 1720 1730 1740 1750
FTNRVNIVES NFQTISGKPV SRADFMMVLR DLKVIFIRAN YWEQTLVTHL
1760 1770 1780 1790 1800
SDVYLTLADE DADGTGEYQF LAVERCSCPP GYSGHSCEDC APGYYRDPSG
1810 1820 1830 1840 1850
PYGGYCIPCE CNGHSETCDC ATGICSKCQH GTEGDHCERC VSGYYGNATN
1860 1870 1880 1890 1900
GTPGDCMICA CPLPFDSNNF ATSCEISESG DQIHCECKPG YTGPRCESCA
1910 1920 1930 1940 1950
NGFYGEPESI GQVCKPCECS GNINPEDQGS CDTRTGECLR CLNNTFGAAC
1960 1970 1980 1990 2000
NLCAPGFYGD AIKLKNCQSC DCDDLGTQTC DPFVGVCTCH ENVIGDRCDR
2010 2020 2030 2040 2050
CKPDHYGFES GVGCRACDCG AASNSTQCDP HTGHCACKSG VTGRQCDRCA
2060 2070 2080 2090 2100
VDHWKYEKDG CTPCNCNQGY SRGFGCNPNT GKCQCLPGVI GDRCDACPNR
2110 2120 2130 2140 2150
WVLIKDEGCQ ECNNCHHALL DVTDRMRYQI DSVLEDFNSV TLAFFTSQKL
2160 2170 2180 2190 2200
NYYDQLADEL EPKVKLLDPN SVDLSPSKKA NSELESDAKS YAKQVNQTLA
2210 2220 2230 2240 2250
NAFDIRERSS TTLGNITVAY DEAVKSADQA KEAIASVEAL SKNLEAAAST
2260 2270 2280 2290 2300
KIDAALEQAQ HILGQINGTS IELTPNEQVL EKARKLYEEV NTLVLPIKAQ
2310 2320 2330 2340 2350
NKSLNALKND IGEFSDHLED LFNWSEASQA KSADVERRNV ANQKAFDNSK
2360 2370 2380 2390 2400
FDTVSEQKLQ AEKNIKDAGN FLINGDLTLN QINQKLDNLR DALNELNSFN
2410 2420 2430 2440 2450
KNVDEELPVR EDQHKEADAL TDQAEQKAAE LAIKAQDLAA QYTDMTASAE
2460 2470 2480 2490 2500
PAIKAATAYS GIVEAVEAAQ KLSQDAISAA GNATDKTDGI EERAHLADTG
2510 2520 2530 2540 2550
STDLLQRARQ SLQKVQDDLE PRLNASAGKV QKISAVNNAT EHQLKDINKL
2560 2570 2580 2590 2600
IDQLPAESQR DMWKNSNANA SDALEILKNV LEILEPVSVQ TPKELEKAHG
2610 2620 2630 2640 2650
INRDLDLTNK DVSQANKQLD DVEGSVSKLN ELAEDIEEQQ HRVGSQSRQL
2660 2670 2680 2690 2700
GQEIENLKAQ VEAARQLANS IKVGVNFKPS TILELKTPEK TKLLATRTNL
2710 2720 2730 2740 2750
STYFRTTEPS GFLLYLGNDN KTAQKNNDFV AVEIVNGYPI LTIDLGNGPE
2760 2770 2780 2790 2800
RITSDKYVAD GRWYQAVVDR MGPNAKLTIR EELPNGDVVE HSKSGYLEGS
2810 2820 2830 2840 2850
QNILHVDKNS RLFVGGYPGI SDFNAPPDLT TNSFSGDIED LKIGDESVGL
2860 2870 2880 2890 2900
WNFVYGDDND QGARERDVLL EKKKPVTGLR FKGNGYVQLN ATSNLKSRSS
2910 2920 2930 2940 2950
IQFSFKADKD TSNGLLFFYG RDKHYMSIEM IDGAIFFNIS LGEGGGVQSG
2960 2970 2980 2990 3000
SQDRYNDNQW HKVQAERENR NGLLKVDDIV ISRTNAPLEA DLELPKLRRL
3010 3020 3030 3040 3050
YFGGHPRRLN TSISLQPNFD GCIDNVVINQ GVVDLTEYVT GGGVEEGCSA
3060 3070 3080 3090 3100
KFSTVVSYAP HEYGFLRMNN VSSDNNLHVV LHFKTTQPNG VLFYAANHDQ
3110 3120 3130 3140 3150
SSTIGLSLQD GLLKLNSMGS QLVIDDRILN DGEDHVVTVQ HTQGELRLTV
3160 3170 3180 3190 3200
DDVDNKRLGS PQPLILEGGD IFFAGLPDNY RTPRNALASL AYFVGCISDV
3210 3220 3230 3240 3250
TVNEEIINFA NSAEKKNGNI NGCPPHVLAY EPSLVPSYYP SGDNEVESPW
3260 3270 3280 3290 3300
SNADTLPPLK PDIESTLPPT TPTTTTTTTT TTTSTTTTST TTTTTTPSPI
3310 3320 3330 3340 3350
VIDEEKEIEA KTPQKILTTR PPAKLNLPSD ERCKLPEQPN FDVDFTEAGY
3360 3370 3380 3390 3400
RFYGLREQRL QINSLPVKVR RHHDIGISFR TERPNGLLIY AGSKQRDDFI
3410 3420 3430 3440 3450
AVYLLDGRVT YEIRVGAQLQ AKITTEAELN DGTWHTVEVV RTQRKVSLLI
3460 3470 3480 3490 3500
DKLEQPGSVD LNAERSAPVL AVELPIYLGG VNKFLESEVK NLTDFKTEVP
3510 3520 3530 3540 3550
YFNGCLKNIK FDAMDLETPP EEFGVVPCSE QVERGLFFNN QKAFVKIFDH
3560 3570 3580 3590 3600
FDVGTEMKIS FDFRPRDPNG LLFSVHGKNS YAILELVDNT LYFTVKTDLK
3610 3620 3630 3640 3650
NIVSTNYKLP NNESFCDGKT RNVQAIKSKF VINIAVDFIS SNPGVGNEGS
3660 3670 3680 3690 3700
VITRTNRPLF LGGHVAFQRA PGIKTKKSFK GCISKVEVNQ RMINITPNMV
3710
VGDIWQGYCP LN
Length:3,712
Mass (Da):411,157
Last modified:May 10, 2005 - v2
Checksum:iF8DB4D0CC88BBEC1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti45Q → P in AAA28662 (PubMed:1425586).Curated1
Sequence conflicti1032L → R in AAC37178 (PubMed:8223265).Curated1
Sequence conflicti1407A → R in AAA28662 (PubMed:1425586).Curated1
Sequence conflicti1559P → Q in AAC37178 (PubMed:8223265).Curated1
Sequence conflicti1598H → Q in AAC37178 (PubMed:8223265).Curated1
Sequence conflicti1912Q → E in AAC37178 (PubMed:8223265).Curated1
Sequence conflicti2630N → S in AAF50672 (PubMed:10731132).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96388 Genomic DNA. Translation: AAA28662.1.
L07288 mRNA. Translation: AAC37178.1.
AE014296 Genomic DNA. Translation: AAF50672.2.
M75882 mRNA. Translation: AAA28661.1.
PIRiS28399. S18253.
RefSeqiNP_476617.1. NM_057269.3.
UniGeneiDm.865.

Genome annotation databases

GeneIDi38723.
KEGGidme:Dmel_CG10236.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96388 Genomic DNA. Translation: AAA28662.1.
L07288 mRNA. Translation: AAC37178.1.
AE014296 Genomic DNA. Translation: AAF50672.2.
M75882 mRNA. Translation: AAA28661.1.
PIRiS28399. S18253.
RefSeqiNP_476617.1. NM_057269.3.
UniGeneiDm.865.

3D structure databases

ProteinModelPortaliQ00174.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi64176. 12 interactors.
IntActiQ00174. 9 interactors.
MINTiMINT-754541.
STRINGi7227.FBpp0076722.

Proteomic databases

PaxDbiQ00174.
PRIDEiQ00174.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi38723.
KEGGidme:Dmel_CG10236.

Organism-specific databases

CTDi38723.
FlyBaseiFBgn0002526. LanA.

Phylogenomic databases

eggNOGiKOG1836. Eukaryota.
ENOG410XRDC. LUCA.
InParanoidiQ00174.
KOiK06240.
OrthoDBiEOG091G005L.
PhylomeDBiQ00174.

Enzyme and pathway databases

ReactomeiR-DME-446107. Type I hemidesmosome assembly.

Miscellaneous databases

ChiTaRSiLanA. fly.
GenomeRNAii38723.
PROiQ00174.

Gene expression databases

BgeeiFBgn0002526.
ExpressionAtlasiQ00174. baseline.
GenevisibleiQ00174. DM.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR013320. ConA-like_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR009254. Laminin_aI.
IPR010307. Laminin_domII.
IPR002049. Laminin_EGF.
IPR001791. Laminin_G.
IPR000034. Laminin_IV.
IPR008211. Laminin_N.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 20 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]
SMARTiSM00181. EGF. 14 hits.
SM00180. EGF_Lam. 21 hits.
SM01411. Ephrin_rec_like. 4 hits.
SM00281. LamB. 1 hit.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 5 hits.
PROSITEiPS00022. EGF_1. 17 hits.
PS01186. EGF_2. 5 hits.
PS01248. EGF_LAM_1. 19 hits.
PS50027. EGF_LAM_2. 22 hits.
PS50025. LAM_G_DOMAIN. 5 hits.
PS51115. LAMININ_IVA. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLAMA_DROME
AccessioniPrimary (citable) accession number: Q00174
Secondary accession number(s): Q9VRW0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 10, 2005
Last modified: November 30, 2016
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.