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Database: UniProt
Entry: A0A195FDY4_9HYME
LinkDB: A0A195FDY4_9HYME
Original site: A0A195FDY4_9HYME 
ID   A0A195FDY4_9HYME        Unreviewed;      3668 AA.
AC   A0A195FDY4;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Laminin subunit alpha {ECO:0000313|EMBL:KYN38880.1};
GN   ORFNames=ALC56_06879 {ECO:0000313|EMBL:KYN38880.1};
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:KYN38880.1, ECO:0000313|Proteomes:UP000078541};
RN   [1] {ECO:0000313|EMBL:KYN38880.1, ECO:0000313|Proteomes:UP000078541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN38880.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN38880.1};
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC       Secreted, extracellular space, extracellular matrix, basement membrane
CC       {ECO:0000256|ARBA:ARBA00004302}.
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; KQ981636; KYN38880.1; -; Genomic_DNA.
DR   STRING; 34720.A0A195FDY4; -.
DR   Proteomes; UP000078541; Unassembled WGS sequence.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
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:0048731; P:system development; IEA:UniProt.
DR   CDD; cd02795; CBM6-CBM35-CBM36_like; 1.
DR   CDD; cd00055; EGF_Lam; 22.
DR   CDD; cd00110; LamG; 5.
DR   Gene3D; 2.60.120.200; -; 5.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.10.25.10; Laminin; 21.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR009254; Laminin_aI.
DR   InterPro; IPR010307; Laminin_dom_II.
DR   InterPro; IPR001791; Laminin_G.
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; PF02210; Laminin_G_2; 5.
DR   Pfam; PF06008; Laminin_I; 1.
DR   Pfam; PF06009; Laminin_II; 1.
DR   Pfam; PF00055; Laminin_N; 1.
DR   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00181; EGF; 10.
DR   SMART; SM00180; EGF_Lam; 22.
DR   SMART; SM00281; LamB; 1.
DR   SMART; SM00282; LamG; 5.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5.
DR   SUPFAM; SSF57196; EGF/Laminin; 22.
DR   PROSITE; PS01248; EGF_LAM_1; 7.
DR   PROSITE; PS50027; EGF_LAM_2; 15.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR   PROSITE; PS51115; LAMININ_IVA; 1.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
PE   4: Predicted;
KW   Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00460}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   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:UP000078541};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..3668
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008271373"
FT   DOMAIN          18..269
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51117"
FT   DOMAIN          444..489
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          490..535
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          536..581
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          582..626
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          627..676
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          727..779
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1361..1406
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1407..1449
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1450..1497
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1498..1548
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1568..1750
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          1784..1833
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1892..1944
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1945..1991
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1992..2038
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          2039..2086
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          2646..2838
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          2849..3023
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          3030..3200
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          3311..3482
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          3488..3665
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   COILED          2619..2646
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   DISULFID        444..456
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        446..463
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        465..474
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        490..502
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        492..509
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        511..520
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        536..548
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        538..555
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        557..566
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        582..594
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        602..611
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        627..639
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        647..656
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        750..759
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1361..1373
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1363..1380
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1382..1391
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1422..1431
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1473..1482
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1498..1510
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1500..1517
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1519..1528
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1803..1812
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1916..1925
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1928..1942
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1964..1973
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        2012..2021
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        2039..2051
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        2041..2058
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        2060..2069
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        3638..3665
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ   SEQUENCE   3668 AA;  406828 MW;  19F16FDE2BB898C5 CRC64;
     MQLPAIFAGL LLIIRLSRSE ILTPPYFNLA EGKEIVASAT CGVDTTGPEL YCKLVGANAD
     QDEDINLIQG QVCDYCDPEN PEKSHPPEYA VDGMETWWQS PPLSRGMKYN EVNLTINLGQ
     EFHVAYVYIR MGNSPRPGLW VLEKSKDYGK TWSPWQYFSD SASDCLTYFG VDSHKPITRD
     DSVICTTEYS KVVPLEGGEI PISILNNRPS AKHYFNSTLL QEWTRATNVR FRFLRTKNLL
     GHLMSVVRQD PTVTRRYFYS IKDISIGGRC MCNGHADTCD IQDPNMPKKL VCRCQHNTCG
     PQCATCCKGF EQKKWRQSTA SQKFICEPCN CFGHSDECIY DPNIDEKHLS LDIHGNYEGG
     GICQNCKHNT EGINCNRCKP KFYRPWDKPL NATDVCQPCN CDYFYSTGNC SDSTGKCECR
     KEFTPPNCDT CNYGYFGYPN CLPCQCDLRG TDGYHCEATD GYCPCKLNYA GHYCNLCAEG
     YYNFPDCLPC DCNPLSALDN VCDVISGNCT CKNNYGGRTC DICEDGYFNY PFCTYCNCDA
     RGTEPGICDK TNGSCSCKEG YGGIRCDQCT PGYYGYPNCV PCNCSSVGSS SISCDSTGKC
     SCLANFAGRT CSQCSPGYYK YPECVACSCD SHGSIGVSCD GEGKCQCREN FDGIRCEQCK
     EGYYNFPTCE GCNCDPAGIV ATFQGCGSLP PGELCQCKER VEGRICNQCK PLYWNLQPYN
     PDGCEECHCN IPGVIGSIGE CDTKTGQCIC KPGVTDRGCS RCIDGTYNLQ EDNLFGCSDC
     SCDVGGSVNP ICDKQTGQCP CQPRITGLTC KEPLKAHYFP TLHQYQYEAE VGKTPSGSGV
     PYGFAEDIFP GFSWKGYAEF TNQQKEIILG VGIGKSSLYR MVLRYVNPNN DPILGTITII
     PDSPSEIEQQ FIVNFKPTTR PSFVTVAGAH GNHPLPMVMN PGHWSIKIST KRSMFLDYFV
     LLPSEYYEGG ILTQDVNVPC EVGYKGLCRH YGYPNLTWFD SVHGAGGFLS ENNVRIPLTE
     YFTDHETLQE INEDEVPLIN NQQEEIHFEL RISKPGPHVL VVTYVTPRDE QDTSVLLIEA
     NTVGKGKVIL NPCRYTSTCR QVVTDTYGKV AVMNFPSNYV SLVLTGESTS NVAIDSIVAI
     PYHQWSLDYI KPKSVCVRKN GKCIQGLFPD AADAKKIEFE TSNNILEAET RPPGIYDNAT
     KLIYLSDGDM VDIHAKVSQP GDYIFVVQYY QPDHPQFELD VLVQNGKFYE AKVPVPHCPS
     NSGCRSIIRQ IDNNDTRFQL IENFVLTLKE PGHGIWLDYI LVIPADQYNE KILSKLQFDE
     TNEFIKRCGS NHFHINVTED GFCRDSTFSL TANYNNGALP CNCDGEGSTS FECEKFGGQC
     PCRPNIIGRR CEICKSGFYG FPRCRPCNCP ALCERDTGRC ICPSRVTGQR CDQCEPGTYG
     FHPIIGCEEC NCSPLGVLDG DLQCDLFDGS CRCKENVVGR QCDRCRAGYS QFPHCERCDC
     DSRGTTADIC DQYTAECFCK ANVQGQACDV CREGTFNIQA ENTDGCTKCF CFGKTTRCAS
     ANLYWTHLMD MAWELITPID KSGNFTTLST YPVENATAIT VSLIANDTFE NVIYFSAPDT
     YLDKKLTSYG GYLNYSVYYS TGPFGKAVSA ADVILQGANI TLFYYSDEQP PSFVNFRASV
     RLIEANFVTS NRLSATREQI MVVLEDLRGI YVRATYWNPS IMASLSYVTW DITTEQYSAQ
     YSIPAGSVEQ CQCPPNYQGL SCEECAPGYY RIKSGPYGGY CAPCQCNGHA TACDVNTGIC
     QNCKNGTTGD HCEFCEQGYY GNATVGTPTD CLICACPLPV ASNNFATGCE VNEEGNKISC
     DCLPGYYGAR CEACAAGYYG NPEVYGDYCK PCECSGNIDT NQIGSCDSIT GQCLQCLNNT
     YGEACNLCAP GYFGDAVERK DCRSCVCDDC GMEHCDSYSG QCFCRENVIG ERCDHCAPNH
     YGFGTCNGCR PCDCDLASES SQCDGETGQC KCMPGVTGRR CDQCIQGYWN YGRDGCTSCE
     CNTGYSVGVS CDTTTGQCTC LPGVIGEKCD HCPYRHVLIP SQGCFSCGSC TGNLLDVTDE
     LADLVEPVSR EYSTVAEGYF TNQRLKFIND TVNELYPEVK LLDPNRVNLL PLQEKLKQLE
     NEVYYQKQQI DFTAEDSGKW KDNAENTLQD MNTLEEDVVH KIDLVNQIVS EVQSLALNIE
     LGTGAKVDNA LNEAKEILKK IKDVSFIEFR DNAVDQANQA NILISEMQQY SFPASNLSFA
     VTDLNVRIKN ISVKMDDLLD TVKIAQDTAS IADKLNRENR IAAQSGNLDV VKNSTAEARE
     DLEAGEQLKN NASDFLNHAK TNIDLLRINT DSDVIDQLNN TIALNDEMLI DLAEPVQKAQ
     VHAAYLHNRS LELDSLLTDT RNTNAVRAVS AYRDIETAIQ AAKDAADNAI IAAENATSLT
     DGIEQKMLDS RNECFKLLAA AQVALTKTTG QPENDLRDAR NNATLIDTQN KRNKELLDSI
     DKTLGNIPSQ SSSVAHDAMN QAMNVESNIE IAIDDMNGIV NQIPEDLRET KQLSKNTSET
     IREISQANKQ LDGVDKVMPS INSLLNSLNG NQKSIDATGN DLQSKIEALR NKIANARELA
     NRFKTGLTFY RNTTLELKNP ESLPLLSTST KISLYFRTNK TNGFLLYLGN EEKSKLPRSK
     AHDFTALLIE SGYPVLIVDL GSGPERINHN KFVSDNVWRQ IIIDRTGKNV KLIVREDIGE
     GKDTLYEKER VLSGPYYIFN VDQEHSKLFV GGYPSSFHIQ DAVTASSFEG EMEELMIGDI
     PVSFWNFVDG ENNQKSALER DKLINFAPSR GYRFDRHGYA ILSKKSSQIT PDTRKFIIKL
     SFKTFVEDGL IYLMGKGRQF LSIEIRNGQL LYQYDLGEGT IVLRSLNKYN DGNWHTLEAI
     RQDTMGALKI DDHTVASSQE RGTTKPLASS DHIYFGGYPP NAKRPYDSVT NNGFEGCIDD
     VVILDTSVDL TRNVQAFGVM PGCPVRFASL VSFEKNTPGY VRWRNLASDG LQVNLKFKTL
     ASNGLIFYAT NDELQNAATS YLSLVDGQLV FTSQGEELRT SPSDVKFNDN EWHVVTATHD
     QSALSLDIDD MENYSTDSAP PPLHFLYGNL YIGGLPSNFD FGERKVVPFV GCIGDATLNS
     EIIINFANTT ERPYAFLGKC KGSDQTLSPP VVKPEFLPPL LPSEGPEDTV ELSTQISKTE
     TNYFLLDIIE VDVDKEDEKE EEEEEPELEG RNNVDKYDFT TTTQRPTEQP ETVDKCHLPY
     YPATDPDLEN AWRFGTARNS RLEYRSLNGR YKDDYDFQID IKTMADDGII FYTSDLSKQN
     LIAVYVLGGK VHYKFDCGSG PALLVSKKMI NNNQWHIIIF KRNGNYGHLT VDEEDVIGYS
     LGNTTAINVN PPFFVGGILP EISSIAYTNI GLNKTFSGCL GNFMTNGQPV GEPSEKVGVI
     PCSKRVEPGI FFYPGNGSNL FKAVDRFNVD RTVDIQMDIK PRSTSGHLLS VHGKRDYLVL
     EMINGTVKFL IKTQRGSIET AFEPTKPNSL CDGHWHNIRA VKQKNAVLLS VDHKPAPPGI
     GGKNVARVLS KHPIFIGGHP MLGKRLRGST SQAQYVGCIN NILINMKPVS IRPERAYGQV
     ITGVCPTI
//
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