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Database: UniProt
Entry: A0A195FT11_9HYME
LinkDB: A0A195FT11_9HYME
Original site: A0A195FT11_9HYME 
ID   A0A195FT11_9HYME        Unreviewed;      1590 AA.
AC   A0A195FT11;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Laminin subunit gamma-1 {ECO:0000313|EMBL:KYN43588.1};
GN   ORFNames=ALC56_01850 {ECO:0000313|EMBL:KYN43588.1};
OS   Trachymyrmex septentrionalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=34720 {ECO:0000313|EMBL:KYN43588.1, ECO:0000313|Proteomes:UP000078541};
RN   [1] {ECO:0000313|EMBL:KYN43588.1, ECO:0000313|Proteomes:UP000078541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN43588.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN43588.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex septentrionalis WGS genome.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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; KQ981276; KYN43588.1; -; Genomic_DNA.
DR   STRING; 34720.A0A195FT11; -.
DR   Proteomes; UP000078541; 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; 2.
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; 2.
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; 10.
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:UP000078541};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1590
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008271590"
FT   DOMAIN          51..325
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51117"
FT   DOMAIN          360..406
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          407..459
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          486..655
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          690..738
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          790..845
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          846..900
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          901..948
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          949..994
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   COILED          1054..1081
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1197..1231
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1261..1393
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1517..1574
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   DISULFID        360..372
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        380..389
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        430..439
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        708..717
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        814..823
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        873..882
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        901..913
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        903..920
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        922..931
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        949..961
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        969..978
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   1590 AA;  177239 MW;  C2658EB8787D1840 CRC64;
     MRGIGIWGLL SFVGSCVVLA DPEADPSEEL FSRLQLPKNR NEDKCYDENG KPQRCIPPFE
     NAAFNVLIEA TNTCGEDRPI EFCKQTGVQK KSCEICRRGD HSASFLTDHD NNDNATWWQS
     DTMYEEYPNQ VNLTLPLGKT FDITYVRVLF ESPRPESWGI YKRKNEKSPW EAYQFYSATC
     RDTYDLPESK ETIRGDDTRE WVQASDLKIT LDRLNTFGDE VFGDAQVLKS YYYAIADIAV
     GARCACNGHA GECVNSTSVD GKTRRVCRCE HNTAGPDCNE CLPFYNNAPW GRATTTDAHE
     CKPCNCNGYS DRCYFDKELY KLTGHGGHCL DCRANRDGAN CERCRENYYQ RSEDNYCVAC
     NCNEIGSRSL QCNSEGKCQC KPGVTGDKCN RCAANFYNFG SQGCTSCECS LAGSANNVPN
     CDTITGVCVC KENVEGKRCR ECRPGFFNLA VDNEFGCTPC FCYGHSSVCR PATGYSKLFI
     ESMFVRGNER WSASVAGNPI PLHYDALTQT ISATALDRDN VYFLAPDKFL GDQRASYNQH
     ISFILRIGEA GPAPTARDVI LEGGNGEQIT QPIFGQNNRL PTVTSQEYKF KLHEHVNYGW
     QPRLSSRAFM SILSNLTAIK IRGTYTHQGR GFLDDVKLET AHRGAAGESA DWVEHCQCPH
     GYVGQFCESC APGFHHDPPN GGPFALCVPC NCNGHADICE AETGQCICQH NTAGSNCELC
     SRGYYGYPLK GTPDDCKPCP CPDNGPCILL GNNPDPICSE CPIGRTGPRC ETCSDGYYGN
     PEKGLACRLC DCNNNIDLNA VRNCNHETGE CLKCVNNTAG FHCEECLAGY YGDALSDRKE
     DGCKLCQCYP PGTLELDDGR VAPCDQLTGY CACKPHVIGR NCNKCEEGYY HIASGEGCIP
     CNCDLEGSYN RTCDPITGQC QCRLGVTGQR CDACEPYQYG FSREGCKPCD CDSIGSQDLQ
     CDANGQCPCL TNVEGRRCDR CKENKHNRQH GCVDCPDCYN LVQSAVNDHR RRLAELEDTL
     YKINSSPTVI KDSDFEKELK NVQDRVKTLL TTAKQGSGSE NKTLVEQLDE LREQLNKIDK
     IYQTVDVTAN DARDITEEGL ISIDEAEKVL DKIYEQLTFR ILTIHRKEAE DYLGTDGASA
     LSSAKLRAEQ VGQQNQQMTS IAQEARVLAE INTNEGKKLH MLAEQARNTT MEAYNLAKQT
     ISKYSNITDE LRNLENKLAQ LDDRMDEVKN LTAIAATKSS TVSQEALDLL ILDLTLPAVD
     IEQLRQQIES VSSESLQIKE QAQLLLEQNE NFIKEMTEKI KKSEELLERA QDQQAATAEL
     LAELDEANET ANDAVKRGDQ TLKEAQETLK KLGEFDAEVQ RERVKAQSAL KDIQKIEELI
     NNANMQAIET ERVLNGSEGN AKSAREIAQN AQTYADRAST NANEIRVEAN KTKIEALRLG
     NEAEKLHLRV DTTDSMIRQY EIQMAKDANI TAEANYKVGQ AKTNVTLASQ QVDKALSEVA
     AIIRELENLP EIDDADLNRL EERLVAAEKE IKAANLDQRI RALTDAKNLQ TQWVKNYEDE
     ISRLRIEVEN IDDIRKALPT DCYQRVRLEP
//
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