ID A0A3Q3ADR0_KRYMA Unreviewed; 1039 AA.
AC A0A3Q3ADR0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Ankyrin repeat and sterile alpha motif domain containing 1A {ECO:0000313|Ensembl:ENSKMAP00000014733.1};
GN Name=ANKS1A {ECO:0000313|Ensembl:ENSKMAP00000014733.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000014733.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000014733.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR AlphaFoldDB; A0A3Q3ADR0; -.
DR Ensembl; ENSKMAT00000014948.1; ENSKMAP00000014733.1; ENSKMAG00000010858.1.
DR GeneTree; ENSGT00940000155806; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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; 2.
DR Pfam; PF00640; PID; 1.
DR Pfam; PF00536; SAM_1; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 5.
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; 4.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 2.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 89..121
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 125..157
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 158..190
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 191..223
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 223..255
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 607..668
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 674..733
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 833..962
FT /note="PID"
FT /evidence="ECO:0000259|PROSITE:PS01179"
FT REGION 25..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..305
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1039 AA; 113494 MW; A3226440E1B04D5E CRC64;
MGKEQELLDA ARTGNLAAVE KLLSGKRQSA GGSSGTAGSG NSGGHGGHGA SSHPLSSLVW
SLFTPSCAAS DVVEALLRNE ALTNIADNKG CYPLHLAAWK GDEHIVRLLI HQGPSHPKLN
EQNNDNETPL HCAAQYGHSR VVRLLLEELT DPTMRNTKFE TPLDLAALYG RLEVVKLLLS
AHPNLLSCNT KKHTPLHLAS RNGHLPVVDV LLDAGMDINY ETEKGSALHE AALFGKRDIV
QKLLRAGIDV NIVDQKGLTA LDTVKDMPSK KSREIAALIY GHMSGKTPII DLPPPPIPPP
QESPSPRKQG DLERVTELIS GMAPGPEEES PYEALFEATS CHSLDSLTSG KSSDRDSGRP
DSEVGKVSRT SSASIDERGE PAEDEEDHTY ELLLTAQTKV PPPSQESKSN KDNSQLSQDQ
GAGVPEQFTG LLHGSSPVID CREDAFRLPG VPPPNQGQQE ARKSTKAKKE VPAASPPPNR
PSMAAILTDC DPKAIYATVN KEPRDLGAGA GVRMRPPGDL KLARSLSKSD SDLLVSPPGE
EEGGLGNRSE SVSNCSTSKK RLEKSPSFTS EWDEIEKIMT LIGAGFSLLK RFPLSAGAAG
RLLDQPVGDW LEHVGVPQYE SKLLLNGFDD LHYMGSNVME DQDLREIGIT DPSHRKKILH
AARSFPKVKA LGCDGSNSLS SWLENLGLHD YLHNFLASGY RTLDCVKNLW ELEIVNVLKI
TLLGHRKRII ASLAERPYEE PPVKPPRLSQ IRDLPGSQTS SPLSQMDYPG RSMDPLLPAG
EPSRKKVPDT EYDERYEEVH QEPRLTLRPP SLAAPYAPVQ NWHHQPEKLI FESCAYEASY
LGSMLIKDLR GTESTQDACA KMRRSTEQMK KVPTIVLSIT YKGVKFIDAA NKNIIAEHEI
RNISCAAQDP EDLCTFAYIT KDLQTSHHYC HVFSTVDVNL TYEIILTLGQ AFEVAYQLAL
QAQRTKQQQQ QNLPGGTGSE VIETRSSRPV PKPRGSVRKS GGDMVDQEGG SQSQASAAWL
MDPKESKRTI STKYETTIF
//