ID D6WGM6_TRICA Unreviewed; 2330 AA.
AC D6WGM6;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Laminin A {ECO:0000313|EMBL:EFA01328.2};
GN Name=AUGUSTUS-3.0.2_03460 {ECO:0000313|EMBL:EFA01328.2};
GN ORFNames=TcasGA2_TC003460 {ECO:0000313|EMBL:EFA01328.2};
OS Tribolium castaneum (Red flour beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX NCBI_TaxID=7070 {ECO:0000313|EMBL:EFA01328.2, ECO:0000313|Proteomes:UP000007266};
RN [1] {ECO:0000313|EMBL:EFA01328.2, ECO:0000313|Proteomes:UP000007266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA01328.2,
RC ECO:0000313|Proteomes:UP000007266};
RX PubMed=18362917; DOI=10.1038/nature06784;
RG Tribolium Genome Sequencing Consortium;
RA Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT "The genome of the model beetle and pest Tribolium castaneum.";
RL Nature 452:949-955(2008).
RN [2] {ECO:0000313|EMBL:EFA01328.2, ECO:0000313|Proteomes:UP000007266}
RP GENOME REANNOTATION.
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA01328.2,
RC ECO:0000313|Proteomes:UP000007266};
RX PubMed=19820115; DOI=10.1093/nar/gkp807;
RA Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT for Tribolium castaneum.";
RL Nucleic Acids Res. 38:D437-D442(2010).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR EMBL; KQ971321; EFA01328.2; -; Genomic_DNA.
DR STRING; 7070.D6WGM6; -.
DR EnsemblMetazoa; TC003460_001; TC003460_001; TC003460.
DR eggNOG; KOG1836; Eukaryota.
DR HOGENOM; CLU_001729_1_0_1; -.
DR InParanoid; D6WGM6; -.
DR OMA; ECKERVT; -.
DR Proteomes; UP000007266; Linkage group 3.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
DR GO; GO:0030334; P:regulation of cell migration; IEA:InterPro.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:InterPro.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 21.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 19.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009254; Laminin_aI.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF365; NETRIN-A-RELATED; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 21.
DR Pfam; PF06008; Laminin_I; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00180; EGF_Lam; 22.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 21.
DR PROSITE; PS01248; EGF_LAM_1; 8.
DR PROSITE; PS50027; EGF_LAM_2; 15.
DR PROSITE; PS51115; LAMININ_IVA; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..2330
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007310615"
FT DOMAIN 22..273
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 403..447
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 448..493
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 494..539
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 540..585
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 586..630
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 631..675
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 731..783
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1362..1407
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1408..1452
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1453..1499
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1500..1550
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1571..1760
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1794..1843
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1902..1954
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1955..2001
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2002..2048
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT COILED 2159..2214
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 423..432
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 448..460
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 450..467
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 469..478
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 494..506
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 496..513
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 515..524
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 540..552
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 542..559
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 561..570
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 586..598
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 606..615
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 631..643
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 651..660
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 754..763
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1362..1374
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1364..1381
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1383..1392
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1425..1434
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1475..1484
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1500..1512
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1502..1519
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1521..1530
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1813..1822
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1926..1935
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1938..1952
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1974..1983
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2022..2031
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 2330 AA; 258770 MW; 524FF44D90D89AC2 CRC64;
MFVVRAWTGL LAVLVLRLET VQGEILTPPY FNLAEGRKIT ATATCGVDTE GPELYCKLVG
ANAENDLNVN VIQGQFCDVC DPTRPDKMHP PEFAVDGMET WWQSPPLSRG MKYNEVNLTI
DLGQEFHVAY VFIRMGNSPR PGLWVLEKSA DYGKTYTPWQ YFSDSPGDCE TYFGKESLQP
ITKDDSVICT TEYSKIVPLE GGEIAISLLN NRPSAKNYFN STILQEWTRA TNVRLKLLRT
KNFLGHLMSV ARQDPTVTRR YFYSIKDISI GGRCMCNGHA DTCDIQDSQD PSVLLCRCQH
NTCGAKCDTC CPGFEQKKWQ QSKINHPFVC EPCNCFQHSN ECVYDEEVDR KGLSLDIHGR
YAGGGVCLNC QHNTDGINCN KCKPTFYRPF GKFENDTDAC QPCNCNHFYS TGNCAEGSGQ
CECKKQFQPP NCDSCSFGYF GYPNCRPCEC FLNGTKDLQC EARNGQCPCL YNYGGQFCGE
CAPGYYSFPD CKHCECNPEG SVTNACEQES GNCTCKNNFG GKRCDECQHG YYNYPTCDYC
NCDIKGTKEG ICDKTTGQCM CKEGYTGDRC DSCLAGYYGY PDCKPCNCSK VGSVGFSCSA
TGKCSCSTNY GGKTCDQCNP GYFKYPECLP CECDSHGSIG VSCDGEGKCE CHHNFAGLRC
DSCREGFYNF PACEDCNCHP AGVVAGFAGC GSVPAGELCQ CKERVEGRIC NKCRPLYWNL
SPNNPQGCEE CKCNISGVLG GIAVCDSESG ECVCKSLVMG RGCTECVDGT YNLQEENLFG
CTDCDCDVGG SVNNICDKAT GQCLCHSRVK GRTCKEPLET HYFPTLYQYQ YEVEDGRTPA
NTLVRYANDE RTFPGYSWKG YAVFGPLQKQ ILQDVIILKP SLYRMVLRFV NKNPETVIGK
IRITPDNPSD NEQEIQVQFR NSTVPAFVTV SGPVGNTPQP FVINPGRWQI SIEVTKDLLL
DYFVLLPEDF YLATILNKKV ETPCTIDGPG LCHDYTYLNL TQFSTTYGVG GYVPEGRRST
KLREYFQDNE HLAKIGVGNR VPVLNLAQPN VSFNITVPKP GQYVIIINYV TPKEDQRTHK
IDVTLQSGRH TNDGRIVLYS CQYTTLCRQV ITTPEGIVAV QQVDGNEIKV DLHSSNADVG
IHSIVAIPYE EWSLDYIKPK SVCIRKDGKC LAASFRYPPE TKKIQFEENN ADLATTLWNN
TYMWLDPSYD TLDLKGKVPT PGYYTFIVHY YQPNFQDFDV TVLMQNGQFY EATLPVHYCP
SRSGCRSVIT QVDGNTKFSL TENFMLTLKE PGNKNVYLDY LLVIPTDFYS DRYLEEEDVD
RTGEFISTCG SNHFNINTTT EGFCKDSVFS ITAGHNSGAL PCGCDFAGSL SFECDKFGGQ
CRCKPNIIGR KCEACKTGYF GFPDCKPCNC PSIAFCEPTT GQCICPPHVV GERCDQCEPL
TYGYDPIIGC EECKCNILGI EGTEQCDLNN GSCHCKPNVV GRQCDKCLAG HYAFPYCEFC
SCDYRGTTSE ICDQATAECF CKKNVVGPTC EICREGTFNL QEENEHGCTE CFCFGKTTRC
TSSKLIRTSV LQMDDWELVG LNFSTRLEIY PLNLTVHNAE ENSIGVAFNS VDFKNTTVYF
TAPSDYTGKK LTAYGGFLNY TLYYTITPGE GSAVSEPDVI LEGRKTYLTY SSYEQPTAAV
EYHASVQLVE ENFELPTGLP ARRDHIMEVL EDVRGVYIRA TYWTASVTTR LSHVIQDDAI
SYQYYSGDNR NLAFALTVEE CRCPENYQGL SCEECAPGYY RVEGGPHGGY CVPCQCHGHA
TECDVNTGIC LNCTHNTRGD HCELCEVGYH GNALAGTPMD CLICACPLPV GSNNFATACD
VSADGEKISC ECKEGYFGAR CQSCAAGFYG RPESLGDFCK PCQCSGNINP DDPSSCDTVS
GECLRCLNNT YGKACALCAP GYFGDAVNLK DCQSCICDEL GTDHCNSFTG ECVCKPNVIG
EKCDRCEVKH YGFQTGAGCV PCDCAEASDS SQCDDVTGQC RCKPGVSGRS CNRCSAGFWN
YTTDGCVSCG CKSEYSLGFG CNALTGQCEC LQGVVGEKCD QCPHRWVFVP DYGCHQCDSC
THALLDDTDA LRHLIDPIIV EFDSANSGYF TRRKLDNMRD LLNELKPKFD EVDPKQINLD
LYIDELQTLE QDSKNLNRKT NYSLENSDSL RVSSIDLKER AELLLDDVQN AEDDSFRVID
EINKITFQLN KDENPEIDSA LEEGQELLDA IKRYNLTGRE EMADDELDKV SNLLLNVSNF
KIPVDYLEEK TDKVKESLKN FNDKLDDLYN QTQYSLSKAN EAQRIIEKSG
//
