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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
  • central nervous system development Source: FlyBase
  • dorsal trunk growth, open tracheal system Source: FlyBase
  • embryonic morphogenesis 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
  • organ morphogenesis Source: FlyBase
  • peripheral nervous system development 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
  • tissue development 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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Chaini23 – 37123690Laminin subunit alphaPRO_0000017064Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence analysis
Glycosylationi219 – 2191N-linked (GlcNAc...)Sequence analysis
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
Glycosylationi395 – 3951N-linked (GlcNAc...)Sequence analysis
Disulfide bondi403 ↔ 414By similarity
Disulfide bondi405 ↔ 421By similarity
Disulfide bondi423 ↔ 432By similarity
Disulfide bondi435 ↔ 445By similarity
Disulfide bondi448 ↔ 460By similarity
Disulfide bondi450 ↔ 468By similarity
Glycosylationi453 – 4531N-linked (GlcNAc...)Sequence analysis
Disulfide bondi470 ↔ 479By similarity
Disulfide bondi482 ↔ 492By similarity
Disulfide bondi495 ↔ 507By similarity
Disulfide bondi497 ↔ 514By similarity
Glycosylationi508 – 5081N-linked (GlcNAc...)Sequence analysis
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
Glycosylationi588 – 5881N-linked (GlcNAc...)Sequence analysis
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
Glycosylationi722 – 7221N-linked (GlcNAc...)Sequence analysis
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
Glycosylationi897 – 8971N-linked (GlcNAc...)Sequence analysis
Glycosylationi1352 – 13521N-linked (GlcNAc...)Sequence analysis
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
Glycosylationi1484 – 14841N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1489 ↔ 1498By similarity
Disulfide bondi1501 ↔ 1511By similarity
Disulfide bondi1514 ↔ 1526By similarity
Disulfide bondi1516 ↔ 1533By similarity
Disulfide bondi1535 ↔ 1544By similarity
Disulfide bondi1547 ↔ 1562By similarity
Glycosylationi1583 – 15831N-linked (GlcNAc...)Sequence analysis
Glycosylationi1617 – 16171N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1778 ↔ 1787By similarity
Disulfide bondi1790 ↔ 1806By similarity
Disulfide bondi1809 ↔ 1818By similarity
Disulfide bondi1811 ↔ 1825By similarity
Disulfide bondi1828 ↔ 1837By similarity
Disulfide bondi1840 ↔ 1856By similarity
Glycosylationi1847 – 18471N-linked (GlcNAc...)Sequence analysis
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
Glycosylationi1943 – 19431N-linked (GlcNAc...)Sequence analysis
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
Glycosylationi2024 – 20241N-linked (GlcNAc...)Sequence analysis
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 bondi2112 – 2112InterchainCurated
Disulfide bondi2115 – 2115InterchainCurated
Glycosylationi2196 – 21961N-linked (GlcNAc...)1 Publication
Glycosylationi2215 – 22151N-linked (GlcNAc...)Sequence analysis
Glycosylationi2267 – 22671N-linked (GlcNAc...)Sequence analysis
Glycosylationi2301 – 23011N-linked (GlcNAc...)Sequence analysis
Glycosylationi2323 – 23231N-linked (GlcNAc...)Sequence analysis
Glycosylationi2482 – 24821N-linked (GlcNAc...)Sequence analysis
Glycosylationi2524 – 25241N-linked (GlcNAc...)Sequence analysis
Glycosylationi2538 – 25381N-linked (GlcNAc...)1 Publication
Glycosylationi2569 – 25691N-linked (GlcNAc...)Sequence analysis
Glycosylationi2699 – 26991N-linked (GlcNAc...)Sequence analysis
Glycosylationi2720 – 27201N-linked (GlcNAc...)Sequence analysis
Glycosylationi2890 – 28901N-linked (GlcNAc...)Sequence analysis
Glycosylationi2938 – 29381N-linked (GlcNAc...)Sequence analysis
Glycosylationi3010 – 30101N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3022 ↔ 3048By similarity
Glycosylationi3070 – 30701N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3196 ↔ 3223By similarity
Glycosylationi3491 – 34911N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3505 ↔ 3528By similarity
Glycosylationi3612 – 36121N-linked (GlcNAc...)Sequence analysis
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

BgeeiQ00174.
ExpressionAtlasiQ00174. differential.
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 interactions.
IntActiQ00174. 9 interactions.
MINTiMINT-754541.
STRINGi7227.FBpp0076722.

Structurei

3D structure databases

ProteinModelPortaliQ00174.
SMRiQ00174. Positions 24-817, 1376-1555, 1775-2110, 2683-3214, 3327-3690.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 272250Laminin N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini273 – 33260Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini333 – 40270Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini403 – 44745Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini448 – 49447Laminin EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini495 – 54046Laminin EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini541 – 58646Laminin EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini587 – 63145Laminin EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini632 – 67645Laminin EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini677 – 73155Laminin EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini732 – 78453Laminin EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini785 – 81531Laminin EGF-like 11; truncatedPROSITE-ProRule annotationAdd
BLAST
Domaini1375 – 142046Laminin EGF-like 12PROSITE-ProRule annotationAdd
BLAST
Domaini1421 – 146545Laminin EGF-like 13PROSITE-ProRule annotationAdd
BLAST
Domaini1466 – 151348Laminin EGF-like 14PROSITE-ProRule annotationAdd
BLAST
Domaini1514 – 156451Laminin EGF-like 15PROSITE-ProRule annotationAdd
BLAST
Domaini1565 – 157410Laminin EGF-like 16; first partPROSITE-ProRule annotation
Domaini1585 – 1775191Laminin IV type APROSITE-ProRule annotationAdd
BLAST
Domaini1776 – 180833Laminin EGF-like 16; second partPROSITE-ProRule annotationAdd
BLAST
Domaini1809 – 185850Laminin EGF-like 17PROSITE-ProRule annotationAdd
BLAST
Domaini1859 – 191658Laminin EGF-like 18PROSITE-ProRule annotationAdd
BLAST
Domaini1917 – 196953Laminin EGF-like 19PROSITE-ProRule annotationAdd
BLAST
Domaini1970 – 201647Laminin EGF-like 20PROSITE-ProRule annotationAdd
BLAST
Domaini2017 – 206347Laminin EGF-like 21PROSITE-ProRule annotationAdd
BLAST
Domaini2064 – 211148Laminin EGF-like 22PROSITE-ProRule annotationAdd
BLAST
Domaini2672 – 2868197Laminin G-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini2876 – 3048173Laminin G-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini3055 – 3223169Laminin G-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini3349 – 3528180Laminin G-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini3534 – 3709176Laminin G-like 5PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni816 – 1374559Domain IV''Add
BLAST
Regioni2112 – 2671560Domain II and IAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili2178 – 224972Sequence analysisAdd
BLAST
Coiled coili2301 – 232121Sequence analysisAdd
BLAST
Coiled coili2376 – 245075Sequence analysisAdd
BLAST
Coiled coili2541 – 2676136Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3270 – 329627Poly-ThrAdd
BLAST

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.
OrthoDBiEOG7DFXB9.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451Q → P in AAA28662 (PubMed:1425586).Curated
Sequence conflicti1032 – 10321L → R in AAC37178 (PubMed:8223265).Curated
Sequence conflicti1407 – 14071A → R in AAA28662 (PubMed:1425586).Curated
Sequence conflicti1559 – 15591P → Q in AAC37178 (PubMed:8223265).Curated
Sequence conflicti1598 – 15981H → Q in AAC37178 (PubMed:8223265).Curated
Sequence conflicti1912 – 19121Q → E in AAC37178 (PubMed:8223265).Curated
Sequence conflicti2630 – 26301N → S in AAF50672 (PubMed:10731132).Curated

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.
SMRiQ00174. Positions 24-817, 1376-1555, 1775-2110, 2683-3214, 3327-3690.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi64176. 12 interactions.
IntActiQ00174. 9 interactions.
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.
OrthoDBiEOG7DFXB9.
PhylomeDBiQ00174.

Enzyme and pathway databases

ReactomeiR-DME-446107. Type I hemidesmosome assembly.

Miscellaneous databases

ChiTaRSiLanA. fly.
GenomeRNAii38723.
PROiQ00174.

Gene expression databases

BgeeiQ00174.
ExpressionAtlasiQ00174. differential.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Laminin A chain: expression during Drosophila development and genomic sequence."
    Kusche-Gullberg M., Garrison K., Mackrell A.J., Fessler L.I., Fessler J.H.
    EMBO J. 11:4519-4527(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  2. "Genetic analysis of laminin A reveals diverse functions during morphogenesis in Drosophila."
    Henchcliffe C., Garcia-Alonso L., Tang J., Goodman C.S.
    Development 118:325-337(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE.
    Tissue: Embryo.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. "Drosophila laminin A chain sequence, interspecies comparison, and domain structure of a major carboxyl portion."
    Garrison K., Mackrell A.J., Fessler J.H.
    J. Biol. Chem. 266:22899-22904(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1762-3712.
  6. "Identification of N-glycosylated proteins from the central nervous system of Drosophila melanogaster."
    Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L., Panin V.
    Glycobiology 17:1388-1403(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2196 AND ASN-2538, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Oregon-R.
    Tissue: Head.
  7. "Activity-dependent retrograde laminin A signaling regulates synapse growth at Drosophila neuromuscular junctions."
    Tsai P.I., Wang M., Kao H.H., Cheng Y.J., Lin Y.J., Chen R.H., Chien C.T.
    Proc. Natl. Acad. Sci. U.S.A. 109:17699-17704(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

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: June 8, 2016
This is version 138 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.