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Database: UniProt
Entry: G1K9W0_ANOCA
LinkDB: G1K9W0_ANOCA
Original site: G1K9W0_ANOCA 
ID   G1K9W0_ANOCA            Unreviewed;      1199 AA.
AC   G1K9W0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 3.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Ankyrin repeat and sterile alpha motif domain containing 1A {ECO:0000313|Ensembl:ENSACAP00000001718.4};
GN   Name=ANKS1A {ECO:0000313|Ensembl:ENSACAP00000001718.4};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000001718.4, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000001718.4, ECO:0000313|Proteomes:UP000001646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000001718.4,
RC   ECO:0000313|Proteomes:UP000001646};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000001718.4}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; G1K9W0; -.
DR   STRING; 28377.ENSACAP00000001718; -.
DR   Ensembl; ENSACAT00000001758.4; ENSACAP00000001718.4; ENSACAG00000001592.4.
DR   eggNOG; KOG0507; Eukaryota.
DR   GeneTree; ENSGT00940000155806; -.
DR   HOGENOM; CLU_010379_0_0_1; -.
DR   TreeFam; TF320582; -.
DR   Proteomes; UP000001646; Chromosome 4.
DR   Bgee; ENSACAG00000001592; Expressed in hemipenis and 13 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0046875; F:ephrin receptor binding; IBA:GO_Central.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; IBA:GO_Central.
DR   CDD; cd01274; PTB_Anks; 1.
DR   CDD; cd09499; SAM_AIDA1AB-like_repeat1; 1.
DR   CDD; cd09500; SAM_AIDA1AB-like_repeat2; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 2.
DR   InterPro; IPR033635; ANKS1/Caskin.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR006020; PTB/PI_dom.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR041880; SAM_ANKS1_repeat1.
DR   InterPro; IPR041882; SAM_ANKS1_repeat2.
DR   PANTHER; PTHR24174:SF4; ANKYRIN REPEAT AND SAM DOMAIN-CONTAINING PROTEIN 1A; 1.
DR   PANTHER; PTHR24174; ANKYRIN REPEAT AND STERILE ALPHA MOTIF DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF12796; Ank_2; 3.
DR   Pfam; PF00640; PID; 1.
DR   Pfam; PF00536; SAM_1; 2.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM00462; PTB; 1.
DR   SMART; SM00454; SAM; 2.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 2.
DR   PROSITE; PS50297; ANK_REP_REGION; 5.
DR   PROSITE; PS50088; ANK_REPEAT; 6.
DR   PROSITE; PS01179; PID; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 2.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   REPEAT          79..111
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          112..144
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          148..180
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          181..213
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          214..246
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          246..278
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          734..797
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   DOMAIN          804..863
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   DOMAIN          974..1106
FT                   /note="PID"
FT                   /evidence="ECO:0000259|PROSITE:PS01179"
FT   REGION          33..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          303..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          369..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          620..691
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1105..1133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1162..1199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..331
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..420
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..463
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        481..514
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        659..691
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1199 AA;  130903 MW;  AAC8D346E84F4559 CRC64;
     MGKEQELLEA SRTGNLPAVE KLLSGKRLSS GFGSGGGGSG GGGGSSGGGG GGGSGGGGHP
     LSSLLSIWRG PNVNCVDSTG YTPLHHAALN GHKDVVEVLL RNDALTNVAD CKGCYPLHLA
     AWKGDAEIVK LLIHQGPSHT KVNEQNNDNE TALHCAAQYG HTEVVKVLLE ELTDPTMRNN
     KFETPLDLAA LYGRLEVVKM LLNAHPNLLS CNTKKHTPLH LAARNGHKAV VHVLLDAGMD
     NNYQTEKGSA LHEAALFGKT DVVQILLAAG IDVNIKDNRG LTALEIVREL PSQKSQQIAS
     LIEESTTGKK ANKVEEKSTS GSSTSTETLV QLSQGNVEKA VTELIIDFDG KPEECPYEVL
     YNATSCHSLD SLASGRSSDR DSVNREAEMT NVRVRPRERP PPPAKPPPDE EEEHTEKKQS
     ASSKGMITKR KSRGSTADEE EEHPYELLLT AETKKHTVVD KKTKGESSSG VAAGVQPQAW
     PRKGPSSQDG QWPLSCQASS EFSSSHSEQY SSPDLQLVEI PKDQSRSSNN HSQTDEQDVP
     VLDQFSGLLH GSSPVCEINE DPFRLISAVG KGGTERTAMQ LEDVETSESV QTSTADQNKV
     VYSTIRHSCD NKLDPEILVH PHLSQHPGGT EDGDKSGVVG RVHVGGKSRA ELKLSRSLSK
     SDSDLLTTSP TEDDTMGSRS ESLSNCTAGK KRLEKSPSFA SEWDEIEKIM SSIGEGIDFS
     QEQQRMSGSR MLEQSVGEWL ESIGLQQYES KLLLNGFDDV RFLGCNVMED QDLREIGISD
     PQHRRKLLQA ARSLPKVKSL GCDGTQPSVP AWLDSLGLQD YIQSFLSSGY SSIDSVKNLW
     ELELVNVLKV NLLGHRKRII ASLADRPYEE PPQKPPRFSQ LRCQDLISQT SSPLSQSDSY
     TGRSADLLLP LGDAGKKRHE GSHDTVSYPR TERLKEERHE SKLMLRPPSL AAPYAPVQHW
     QHQPEKLIFE SCGYEANYLG SMLIKDLRGT ESTQDACAKM RKSTEHMKKI PTIILSITYK
     GVKFIDASNK NVIAEHEIRN ISCAAQDPED LCTFAYITKD LQTSHHYCHV FSTIDVNLTY
     EIILTLGQAF EVAYQLALQA QKSKPPGALT AETIETKSSK PVPKPRASMR KSAVPLPPDN
     RCCNCHTCTT HRPSYLPLQS VSQGAKLEPS EVDQDSQSHA SVSWVVEPKQ DSKRTLSTN
//
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