ID A0A195FSV9_9HYME Unreviewed; 2867 AA.
AC A0A195FSV9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Talin-1 {ECO:0000313|EMBL:KYN43533.1};
GN ORFNames=ALC56_01794 {ECO:0000313|EMBL:KYN43533.1};
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:KYN43533.1, ECO:0000313|Proteomes:UP000078541};
RN [1] {ECO:0000313|EMBL:KYN43533.1, ECO:0000313|Proteomes:UP000078541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN43533.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN43533.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex septentrionalis WGS genome.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KQ981276; KYN43533.1; -; Genomic_DNA.
DR STRING; 34720.A0A195FSV9; -.
DR Proteomes; UP000078541; Unassembled WGS sequence.
DR GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005925; C:focal adhesion; IEA:InterPro.
DR GO; GO:0001726; C:ruffle; IEA:InterPro.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0030182; P:neuron differentiation; IEA:UniProt.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd10569; FERM_C_Talin; 1.
DR CDD; cd17089; FERM_F0_TLN; 1.
DR CDD; cd17090; FERM_F1_TLN; 1.
DR CDD; cd12150; talin-RS; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 1.20.120.230; Alpha-catenin/vinculin-like; 5.
DR Gene3D; 1.20.1410.10; I/LWEQ domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.20.1420.10; Talin, central domain; 7.
DR InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR032425; FERM_f0.
DR InterPro; IPR035964; I/LWEQ_dom_sf.
DR InterPro; IPR002558; ILWEQ_dom.
DR InterPro; IPR002404; IRS_PTB.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR037438; Talin1/2-RS.
DR InterPro; IPR015224; Talin_cent.
DR InterPro; IPR036476; Talin_cent_sf.
DR InterPro; IPR049108; Talin_R4.
DR InterPro; IPR015009; Vinculin-bd_dom.
DR PANTHER; PTHR19981:SF1; RHEA, ISOFORM B; 1.
DR PANTHER; PTHR19981; TALIN; 1.
DR Pfam; PF16511; FERM_f0; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF01608; I_LWEQ; 1.
DR Pfam; PF02174; IRS; 1.
DR Pfam; PF09141; Talin_middle; 1.
DR Pfam; PF21692; Talin_R4; 2.
DR Pfam; PF08913; VBS; 1.
DR SMART; SM00295; B41; 1.
DR SMART; SM00307; ILWEQ; 1.
DR SMART; SM01244; IRS; 1.
DR SUPFAM; SSF109880; A middle domain of Talin 1; 1.
DR SUPFAM; SSF47220; alpha-catenin/vinculin-like; 5.
DR SUPFAM; SSF109885; I/LWEQ domain; 4.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS50945; I_LWEQ; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000078541}.
FT DOMAIN 89..414
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 2313..2551
FT /note="I/LWEQ"
FT /evidence="ECO:0000259|PROSITE:PS50945"
FT REGION 2611..2636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2696..2747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2794..2825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2847..2867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1812..1839
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2476..2511
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2707..2721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2794..2823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2867 AA; 309600 MW; 9A571F75239E1BE5 CRC64;
MATLSLRISI PEKNATKMMQ FDPSTSVYDA CRIIREKLAE ASNMGQPKDY GLFLADEDVK
KGIWLEPGRN LDYYMLRNGD LLEYRRKLRT LRVRMLDGTL KTMLVDDSQP VANLMVVICT
KIGITNHDEY SLVRELVEDE NENQKPGNFG TLTLKRKKEE KGERDTKMEQ LRKKLKTDDE
VNWIDPSKTL REQGIDESET VLLRRKFFFS DQNIDSRDPV QLSLLYVQAR DAILDGTHPI
TQEKACVFAG IQCQIQFGDH KEEKHKPGFL DLKEFLPQSY VKVKGIEKKV FAEHKKHIGL
SELDAKVLYT KTARSLNTYG VTFFLVKEKM KGKNKLVPRL LGVTKDSVLR LDEKTKEILK
TWPLTTVRRW GASPNTFTLD FGDYSDQYYS VQTTEAEQIL QLIAGYIDII LKKQKAKDHF
GIEGDEGSTM VEDSVSPLKA TIMQHETSNV GKGNVEAVSV AIPAVMRAGG DGARPYGTGH
IGGAQYTTVS GQVNIAHAPP MVQQTKVTSV LSEPQRALLS TITAGHEVIH IAETELITKA
QLPELGTDPA SLRWIEQTID THKQNVGSQI AAMNAATAQV VTLTSGPADD VDHTAVGAAI
TTIATNLPEM TKGVRMIAAL MDDESSGERL LDAARKLCSA FSDLLKATEP ETKEPRQNLL
NAASRVGEAS HQVLTTIGEE DDSNRELQDM LLALAKAVAN TTAALVLKAK NIAATCEDSA
TQNRVISAAT QCALATSQLV ACAKVVAPTL HSPACQTQLM NAVREVTKAV ERLVQVCNET
CSDENLLKEL SIAAAEVSRT LNDLLNHIKT ATRERAKESI QEGAVETILV ATDKLFASTG
DAGEMVRQAR VVGQATAQLI QSIKGEAERQ TDSEQQQRLL AAAKLLADAT AKMVEAARQC
ASSPHDAKMQ DQLRQAAEEL RAATTAAATP ALRRKLITRL EACAKQAAST ATQCIAASSG
AGHHNTNPAS QEELNMECRM MAQQIPYLVS GVKGTQAQPD NSTAQLNLIN ASEQFLQPGT
AVVKAARAVL PTVTDQASAI QLNNTSQQLG SSLADLRSAV TRAREACGGL ELDAAEELIN
SLKDELGEFY RAVEAASLRP LPEETTESTA LRLGATSKNV GFAMAQLLSA AKQGNENYTG
SAARETASAL KDLTYAVRGV AATSNQSETQ KKVLMTADDV ILRSLRLVKE ARRVLKNPDD
PENEANLAAV AKDVSNSLNK CVSCLPGQRD VDEAICNIDD MTQVLNLNEF PQTSKSYGQL
QSDLNNAAAN LNDASSNVVS SVRSPVQLAN SSKQFTNAFG DLLGVGMEMA SQTTIETRSQ
VVVSLKNVSM TSSKLLMTAK SIAADPTAPN AKNQLSAAAR AVTDSINYLV DVCTSAAPGQ
NECDNAIRNI QSMRSLLDNP SEPISDASYF ECLETVMEKS KSLGDGMTGI ANHAKKSEHE
QFSIAVRGVS SSICGLIEAA AQAAYLAGVS DPTSVAGKPG LVDQAQFLRA AQAIHSGCQS
LGSPTSTQQQ VLSAATMIAK HTSALCNACR LASSKTSNPV AKRHFVQSAK DVANSTACLV
KEIKALDQNY SDINREKCAE ATKPLLEAVD NLCTFAGSPE FASQPAKISI AARAAQEPIT
SAGKSIIDGS CAMVLAAKSL AVSPKDPPTW QLLANHSKSV SDSIKSLVAS IRDKAPGQKE
CDAAIEKLSA RIRELDAASL SAVSQALMPR RENTVQGFTD QMESSASELR EKLEPLRTAA
KYEAENVGHA VNQIALYSEP LVSGAIGAAS NMVHSKQQMV LLDQTKTVAE SALQLIYITK
ESGGNPKAVA LHTEVDETVE STKDALQELQ NTLETISTSA GIVTGLIDTI SRAMVRLEDH
RMSTIDTVDS YVDYQTRMVE AAKEIARLAQ EISTKSSTDV ARLGPLAVDI SHKYTQLARD
TSGASAAASN ADVSARLRTG VQELGRACAD IVRAAGTCQM SPGDAYAQRE VAEHSKIVTE
KVSQVLAALQ AGSRGTQACI NAASTVSGII GDLDTTIMFA TAGTLHAENE GDTFADHREN
ILQTAKALVE DTKTLVAGAA SSQEQLAVAA QNAVSTIVQL AEVVKYGAAS LGSQNPEAQV
MLINAVKDVA SALGDLIHAT KAASGKPIND PSMAHLKDSA KVMVTNVTSL LKTVKAVEDE
HTRGTRALES TIEAIAQEIR ALSSSETQRS NVTPEDLVRC TKSITISTAK AVAAGNSCKQ
DDIIAAANMG RKSISDMLTI CKGAAHNCAE TTELCERTLQ AGHDVAINYR ELLQAILQIS
SRSGDKHTLP AISRKIAQSV TELVAVAELL KGNDWVDPDD PTVIAENELL GAAASIDAAA
KKLASLRPRR SIQEANEDMN FDEMILEAAK SIAAATSALI KAASAAQREL IATGKVSRTP
LTSSDDGQWS EGLISAARMV AAATHSLVES ANALVQGVSS EEKLISSAKQ VASSTAQLLV
ACKVKADPDS ESTKRLQAAG NAVKRATDNL VRAAQQAIQQ EEDRSLVLNR RMVGGIAQEI
DARSEVLRIE RELEEARGRL TAIRLAKYKN RPDLADGDGD VTGDQSGYQS YTTRYETRAY
EPQTSPIQTM NHTLDQLQST TQHISHQFAD QQNLVSPEKV HSTQSTLERK MKDSQYRSTM
DHYGSLDRKY TVDSFQDRSP YIVTERKIIT DNSPGQYSSI ERRINQESYV ADRKHTDGIV
SYPPPQHISY ATKSPTPKVV QEQTAEDRKS PQDQLKYPTD RFSGISPMST FRSEKQVDTQ
RFSSGIPQHQ TFKNVESKTI PGHRIETVTT KVYTSTPSKS SSNYETTEET KQYTSGNELS
TFKGNDNVEE RTMKQSMHKV TEKKTVTMTM SSRQESNTKT FRYEDKQ
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