ID A0A3P8QU81_ASTCA Unreviewed; 1429 AA.
AC A0A3P8QU81;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Cytoplasmic linker associated protein 1a {ECO:0000313|Ensembl:ENSACLP00000033093.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000033093.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000033093.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000033093.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000256|ARBA:ARBA00004629}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Golgi
CC apparatus, trans-Golgi network {ECO:0000256|ARBA:ARBA00004601}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR Ensembl; ENSACLT00000033874.1; ENSACLP00000033093.1; ENSACLG00000022095.1.
DR GeneTree; ENSGT00940000154817; -.
DR Proteomes; UP000265100; Chromosome 16.
DR Bgee; ENSACLG00000022095; Expressed in brain and 6 other cell types or tissues.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
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:SF28; CLIP-ASSOCIATING PROTEIN 1; 1.
DR Pfam; PF21040; CEP104-like_TOG; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Kinetochore {ECO:0000256|ARBA:ARBA00022838};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..216
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REPEAT 168..206
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 297..529
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 777..1014
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 1182..1418
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REGION 231..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1101..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1429 AA; 158275 MW; A41F0C96BFBF4BDB CRC64;
MEPSMENCLA LVLQKDMGRR LQVGQEIIDY ILDKEKSHDL EQDQTALDKM VDGIASSWVN
SSNFKVALLG LDLLSALVTR LQERFRAQVG TVLPSLIDRL GDAKDQVRET DQTLLLKIME
QTANPQYVWD RMLGGFKHKN NRTREGVCLC LIATLNTYGA QGLTLNKIVP HICNLLGDPT
SQVRDGAMSS LVEIYRHVGE RVRLDLSKKV TYTLSHFFFF FFADKNFEDE DSVDGGRSSS
SSSKAPPSGR RTVVSSVRRP SSATTPKPTA AAGAVDEEDF IKAFEDVPSV QIYSNRELED
QLTKIREVLS DDKHDWEHRV VALKKVRSLM LAGATDYEGF PQQLRLLEAS FKLSAKDLRS
QVVREACITL GYLSSILGNK FDHAAESVMP TLLNLVPNSA KVMATSGMAV IRLILRHTHY
PRLIPIITSN CTSKSVAVRR RCYEFLDLML QEWHTNTLER HVAVLTETIK KGIHDADSEA
RSIARKCYWG FHGHYSREAE HLFQALEATY QKALQSHLKS SDSIVSLPQS DRSSSSSQES
LNRPLSVKSV IGGSMTRSKV PSTPGSLQRS RSDIDVNAAS SAKSRLSTVP ASSPFSSAAA
LPPGSYASLG RVRTRRQSSG SVGGASSSSV VDSRGRSRAK VVSQSQPGSR SSSPGKLLSH
SSYGRIPRAT ASASTTPADK RSRIPRSQGC SRETSPSRLG LDRYGLVHQA RISASVNAMR
VLNTGTEVEA AVADALRKTL RRRYESPGMY SDDDANSDAS SACSERSYGS RNGGIPHYLR
QTEDVAEVLN HCASSNWSER KEGLLGLQNL LKSQRILSRV ELKRLCEIFT RMFADPHSKV
FSMFLETLVD FVTVHREDLQ DWLFVLLTQL LKKMGADLLG SVQAKVQKAL DVTRESFPFD
QQFNILMRFI VDQTQTPNLK VKVAILKYIE SLARQMDPTD FVNSSETRLA VSRIITWTTE
PKSSDVRKAA QVVLIALFEL NTPEFTMLLG ALPKTFQDGA TKLLHNHLKN TSNTSSNVGS
PSNTIGRMPA RHTPSRTSPL TSPTNCSHGG LSPSMMEYDT ENMNSDEIYS SLRGVTEAIQ
SFSYRSQEDL NEPIRREAKR DDAVRREGVA SSPGSDARLG LDVVEGGRTA LDNKTSLLNT
PSPRSFSGPR TREFAPYGYG ETICTYDKSA LKEAVFDDDV EQFRDSVGQD HSDLVADLLK
ELSNHNERSE ERKGALVELL KITREDSRAV WDEHFKTILL LLLETLGDKD HTIRALALRV
LKEILRNQPA RFKNYAELTI MKTLEAHKDS HKEVVRAAEE AAATLAGSIH PEQCIKVLCP
IVQTADYPIN LAAIKMQTKV IERIAKESLL QLLPDIIPGL LQGYDNTESS VRKASVFCLV
AIYSVIGEEL KPHLAQLTGS KMKLLNLYIK RAQTTNSNSS SSSDVSSHS
//
