ID A0A3Q1FT09_9TELE Unreviewed; 1502 AA.
AC A0A3Q1FT09;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Cytoplasmic linker associated protein 2 {ECO:0000313|Ensembl:ENSAPOP00000018757.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000018757.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000018757.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000256|ARBA:ARBA00004629}. Golgi apparatus, trans-Golgi network
CC {ECO:0000256|ARBA:ARBA00004601}.
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DR Ensembl; ENSAPOT00000028425.1; ENSAPOP00000018757.1; ENSAPOG00000022260.1.
DR GeneTree; ENSGT00940000155574; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0015631; F:tubulin binding; IEA:InterPro.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IEA:UniProt.
DR GO; GO:1902903; P:regulation of supramolecular fiber organization; IEA:UniProt.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 4.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024395; CLASP_N_dom.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR034085; TOG.
DR InterPro; IPR048491; XMAP215_CLASP_TOG.
DR PANTHER; PTHR21567; CLASP; 1.
DR PANTHER; PTHR21567:SF30; CLIP-ASSOCIATING PROTEIN 2; 1.
DR Pfam; PF12348; CLASP_N; 1.
DR Pfam; PF21041; XMAP215_CLASP_TOG; 1.
DR SMART; SM01349; TOG; 4.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 4: Predicted;
KW Centromere {ECO:0000256|ARBA:ARBA00023328};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Kinetochore {ECO:0000256|ARBA:ARBA00022838};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 8..233
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REPEAT 169..207
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 317..547
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 853..1111
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 1254..1498
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REGION 233..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1271..1302
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 543..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1502 AA; 165120 MW; 226BB54D675E928C CRC64;
MEEHDNMDYF YQQVLQKDVS RRLQVGQDLI DYLNDPQRSP DVEQDKPRLD KTIDELTGWV
NSSNFKVALL GIDICGAFVD RMGERFKGYL GTVLPALVDR LGDGKDQVRE NSQALILRCM
EQTASPMYVW ERLLPGFKHK NFRSREGICL CLSATLSTCG AQPLSLSKIV PHLCSLTGDQ
NPQVREASIT TLVDVYRHVG ERVRADLGKR GLPAARLQTI FARFDEALNS GNMALSPSHD
RSFEDDDSVD GNRSSSAQAA FKVPKVPKKP ADSSATRRPS ATGGKLVSKE SAGAVDEEDF
IKAFTDVPTV QIYSTRDLED NLNKIREVCS DDKHDWDQRA NALKKIRSLL VAGAATYDCF
YQHLRLLDGA FKLSAKDLRS QVVREACITV AHLSSVLGNK FDHGAEAIVP VLFNLIPNCA
KVMATSGVSA IRIIIRHTHV PRLIPLITSN CTSKSVAVRR RCYDFLDLLL QEWQTHSLER
HTAVLVESIK KGIRDADSEA RVEARKAYWG LRNHFPGEAD ALYNSLESSY QRTLQSCLRS
SGSVASLPQS DRSSSSSQES LNRPLSSKWS AAPGRVPAGS KGGVSSASLQ RSRSDVDVNA
AAVAKSRHVG TAGRAGRLPP GSYSSLGTRS DNGRVRTKQP LSTASSVSSQ VDSRGRSRTK
MVSQSQPGSR SGSPGRVLTT TALSTMSTGA HRVLAGAAGD GHRRSRIPRS QGCSRDSSPT
RLSVAPSSIS SIYNGASRGA RGSRIPRPSM SQGCSREASR ESSRDTSPVR SFTPLGSGFG
ISQSSRLSSS VSAMRVLNTG SDVEEALADA LKKPARRRYE NYGMYSDDDA NSDASSACSE
RSYSSRNGGA IPTYMRQTED VAEVLNRCAS ANWSERKEGL LGLQALLKNQ RTLSRVELKR
LCEIFTRMFA DPHSKRDSGR VYGTAESGIS SASFKVVFSM FLETLVDFIQ VHKDDLQDWL
FVLLTQLLKK MGADLLGSVQ AKVQRALDVT RESFPNDLQF TILMRFTVDQ TQTPNLKVKV
AILKYIETLT LQMEPPDFVN SSETRLAVSR IITWTTEPKS SDVRKAAQSV LIALFQLNTP
EFTMLLAALP KTFQDGATKL LQNHLKNTGN AAQAPMGSPL TRHTPRSPAS WSSPVTSPTN
TSQNTPSPSA FDYDTENMNS EDIYSSLKGV TEAIQNFSVR SQEDMNEPVQ RREGEEGGSG
TDGRGSDLVD GGRMALDNKT SLLNTPLLSS SPRGAREHFS DSPFKHSRKD TSLDDSEQLA
DDSSLDQSEL VAELLKELSN HNERIEERKA ALCELLKLIR ENTLQVWDEH FKTILLLLLE
TMGDREHVIR TLALRVLREI LSKQPWRFKN YAELTIMKAL ESHKDPHKEV VRAAEETAAM
LALSISPDQC IKVLCPIIQS ADYPINLAAI KMQTKVVERV PREGLISMLP EIVPGLIQGY
DNSESSVRKA CVFCLVAIYA VIGEDLKPHL SQLSSSKLKL LNLYIKRAQS GSTGSEPSSE
GL
//
