ID F4WFN5_ACREC Unreviewed; 2910 AA.
AC F4WFN5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Talin-1 {ECO:0000313|EMBL:EGI67012.1};
GN ORFNames=G5I_04444 {ECO:0000313|EMBL:EGI67012.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI67012.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GL888120; EGI67012.1; -; Genomic_DNA.
DR STRING; 103372.F4WFN5; -.
DR eggNOG; KOG4261; Eukaryota.
DR InParanoid; F4WFN5; -.
DR Proteomes; UP000007755; 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:UniProtKB-SubCell.
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; 2.
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:UP000007755}.
FT DOMAIN 89..414
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 2357..2595
FT /note="I/LWEQ"
FT /evidence="ECO:0000259|PROSITE:PS50945"
FT REGION 2740..2798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2838..2881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2891..2910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1812..1839
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2520..2555
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2751..2765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2780..2798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2838..2869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2910 AA; 314504 MW; 9FC6E585E4F61AFF CRC64;
MATLSLRISI PEKNATKMMQ FDPSTSVYDA CRIIREKLAE ASNMGQPKDY GLFLADEDVK
KGVWLEPGRN LDYYILRNGD 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 RAATTAAAIP ALRRKLITRL EACAKQAAST ATQCIAASSG
AGHHNTNPAS QEELNMECRM MAQQIPYLVS GVKGTQAQPD NSTAQLNLIN ASEQFLQPGT
AVVKAARAVL PTVTDQASAI QLNNTSQQLG SSLADLRSAV TRAREACGGL ELDAAEELIN
SLKDELGEFY RAVEAASLRP LPEETTESTA LRLGTTSKNV GFAMAQLLSA AKQGNENYTG
SAARETASAL KDLTYAVRGV AATSNQPETQ KKVLMTADDV ILRSLRLVKE ARRVLKNPDD
PENEVNLAAV AKDVSNSLNK CVSCLPGQRD VDEAICNIDD MTQVLNLNEF PQTSKSYGQL
QSDLNNAAAN LNDASSNVVS SVRSPIQLAN SSKQFTNAFG DLLGVGMEMA SQTTVETRSQ
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 NLCTFASSPE FASQPAKISI AARAAQEPIT
SAGKSIIDGS CAMVLAAKSL AVSPKDPPTW QLLANHSKSV SDSIKSLVAS IRDKAPGQKE
CDAAIEKVSA RIRELDAASL SAVSQALMPR RENTVQGFTD QMESSANELR 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 KVLEQQLQQQ FVHLSDIGGS
ESEWFVSDQE EELIRLLSTS ESSQPVMVTN VTSLLKTVKA VEDEHTRGTR ALESTIEAIA
QEIRALSSSE TQRSNVTPED LVRCTKSITI STAKAVAAGN SCKQDDIIAA ANMGRKSISD
MLTICKGAAH NCAETTELCE RTLQAGHDVA INYRELLQAI LQISSRSGDK HTLPAISRKI
AQSVTELVAV AELLKGNDWV DPDDPTVIAE NELLGAAASI DAAAKKLASL RPRRSIQEAN
EDMNFDEMIL EAAKSIAAAT SALIKAASAA QRELIATGKV SRTPLTSSDD GQWSEGLISA
ARMVAAATHS LVESANALVQ GVSSEEKLIS SAKQVASSTA QLLVACKVKA DPDSESTKRL
QAAGNAVKRA TDNLVRAAQQ AIQQEEDRSL VLNRRMVGGI AQEIDARSEV LRIERELEEA
RGRLTAIRLA KYKNRPDLAD GDGDVVGDQS GYQSYTTRYE TRAYEPQTSP IQTMNHTLDQ
LQSTTQHISH QFADQQNLVS PEKVHSTQST LERKMKDSQY RSTVDHYGSL DRKYTVDSYQ
DRSPYIVTER KIITDNSPGQ YSSIERRINQ ESYVTDRKHT DGIVSYPPPQ HISYATKSPT
PKIVQEQTAE DRKSPQDQLK YPTDRFSGVS PMSTFRSEKQ VDTQRFSSGI PQHQTFKNVE
SKTIPGHRVE TITTKVYTST PGKSTSSSNY ETTEETKQYT SGNELSTFKG SDNVEERTMK
HKVTEKKTVT MTMSSRQESN TKTFRYEDKQ
//