ID A0A158NYZ5_ATTCE Unreviewed; 1620 AA.
AC A0A158NYZ5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Laminin subunit gamma-1 {ECO:0008006|Google:ProtNLM};
GN Name=105626050 {ECO:0000313|EnsemblMetazoa:XP_012062753.1};
OS Atta cephalotes (Leafcutter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012062753.1, ECO:0000313|Proteomes:UP000005205};
RN [1] {ECO:0000313|Proteomes:UP000005205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA Weinstock G.M., Gerardo N.M., Currie C.R.;
RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT insights into its obligate symbiotic lifestyle.";
RL PLoS Genet. 7:e1002007-e1002007(2011).
RN [2] {ECO:0000313|EnsemblMetazoa:XP_012062753.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) to UniProtKB.
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; ADTU01004413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012062753.1; XM_012207363.1.
DR STRING; 12957.A0A158NYZ5; -.
DR EnsemblMetazoa; XM_012207363.1; XP_012062753.1; LOC105626050.
DR GeneID; 105626050; -.
DR KEGG; acep:105626050; -.
DR eggNOG; KOG1836; Eukaryota.
DR InParanoid; A0A158NYZ5; -.
DR OrthoDB; 90222at2759; -.
DR Proteomes; UP000005205; Unassembled WGS sequence.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd00055; EGF_Lam; 10.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 10.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF435; LAMININ SUBUNIT GAMMA-1; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 10.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00180; EGF_Lam; 11.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 9.
DR PROSITE; PS01248; EGF_LAM_1; 4.
DR PROSITE; PS50027; EGF_LAM_2; 7.
DR PROSITE; PS51115; LAMININ_IVA; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000005205};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1620
FT /note="Laminin subunit gamma-1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007629832"
FT DOMAIN 51..282
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 399..445
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 446..498
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 525..694
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 729..777
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 829..884
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 885..939
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 940..987
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 988..1033
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT COILED 1038..1162
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1227..1261
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1291..1423
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1547..1604
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 399..411
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 419..428
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 469..478
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 747..756
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 853..862
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 912..921
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 940..952
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 942..959
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 961..970
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 988..1000
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1008..1017
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1620 AA; 180280 MW; FDBC4EAE228CD8A4 CRC64;
MKGIGIWSLL SLVGSCVVLA DPEADPSEEL FSRLQLPKNR NEDKCYDENG RPQRCIPPFE
NAAFNVLIEA TNTCGEDRPI EFCKQTGVQK KSCEICRRGD HSASFLTDHD NNDNATWWQS
DTMYEEYPNQ VNLTLPLGKT FDITYVRVLF ESPRPESWGI YKRKNEKSPW EAYQFYSATC
RDTYDLPESK ETIRGDDTRV LCTSEFSDIS PLTKGTVAFS TLEGRPSAYY FETNTELQEW
VQASDLKITL DRLNTFGDEV FGDAQVLKSY YYAIADIAVG ARCACNGHAG ECVNSTSVDG
KTRRVCRCEH NTAGPDCNEC LPFYNNAPWG RATTTDAHEC KPCNCNGYSD RCYFDKELYK
LTGHGGHCLD CRANRDGANC ERCRENYYQR PEDNYCVACN CNEIGSRSLQ CNSEGKCQCK
PGVTGDKCNR CAANFYNFGS QGCTSCECSL AGSANNVPNC DTITGVCVCK ENVEGKRCRE
CRPGFFNLAV DNEFGCTPCF CYGHSSVCRP ATGYSKLFIE SMFVRGNERW SASVAGNPIP
LHYDALTQTI SATALDRDNV YFLAPDKFLG DQRASYNQHI SFILRIGEAG PAPTARDVIL
EGGNGEQITQ PIFGQNNRLP TVTPQEYKFK LHEHVNYGWQ PRLSSRAFMS ILSNLTAIKI
RGTYTHQGRG FLDDVKLETA HRGAAGESAD WVEHCQCPHG YVGQFCESCA PGFHHDPPNG
GPFALCVPCN CNGHADICEA ETGQCICQHN TAGSNCELCS RGYYGYPLKG TPDDCKPCPC
PDNGPCILLG NNPDPICSEC PIGRTGPRCE TCSDGYYGNP EKGLACRPCD CNNNIDLNAV
RNCNHETGEC LKCVNNTAGF HCEECLAGYY GDALSDRKED GCKLCQCYPP GTLELDDGRV
APCDQLTGHC ACKPHVIGRN CDKCEEGYYH IASGEGCIPC NCDLEGSYNR TCDPITGQCQ
CRLGVTGQRC DACESYQYGF SREGCKHCDC DSIGSQDLQC DANGQCPCLT NVEGRRCDRC
KENKHNRQHG CVDCPDCYNL VQSAVNDHRQ RLAELEDTLY KINSSPTVIK NSDFEKELKN
VQDRVKTLLT TAKQGSGSEN KTLVEQLDEL REQLNKIDKI YQTVDVTAND ARDITEEGLI
SIDEAEKVLD KIYEQLTEAE DYLGTDGASA LSSAKLRAEQ VGQQNQQMTS IAQEARVVAE
INTNEAKKLY MLAEQARNTT MDAYNLAKQT ISKYSNITDE LRNLENKLAQ LDDRMDEVKN
LTAIAATKSS TVSQEALDLL ILDLTLPAVD IEQLRQQIES ISSESLQIKE QAQLSLEQNE
NFIKEMTEKI KKSEELLERA QDQQAATAEL LAELDEANET ANDAVKRGDQ TLKEAQETLK
KLGEFDAEVQ RERIKAQSAL KDIQKIEELI NNANMQAIET ERVLNGSEGN AKSAREIAQN
AQTYADRAST NANEIRVEAN KTKIEALRLG NEAEKLHLRV DTTDSMIRLH EIQMANDANI
TAEANYKVGQ AKTNVTLASQ QVDKALSEVA AIIRELENLP EIDDADLNRL EERLVAAEKE
IKAANLDQRI RALTDAKNLQ TQWVKNYEDE VSRLRIEVEN IDDIRKALPT DCYQRVRLEP
//
