ID A0A3P8R7X3_ASTCA Unreviewed; 1783 AA.
AC A0A3P8R7X3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Kinesin-like protein KIF1A {ECO:0000313|Ensembl:ENSACLP00000038038.1};
GN Name=KIF1A {ECO:0000313|Ensembl:ENSACLP00000038038.1};
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:ENSACLP00000038038.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000038038.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000038038.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR Ensembl; ENSACLT00000038926.1; ENSACLP00000038038.1; ENSACLG00000025416.1.
DR GeneTree; ENSGT00940000156474; -.
DR Proteomes; UP000265100; Chromosome 23.
DR Bgee; ENSACLG00000025416; Expressed in brain and 1 other cell type or tissue.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR CDD; cd01233; PH_KIFIA_KIFIB; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 6.10.250.2520; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR InterPro; IPR032405; Kinesin_assoc.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR PANTHER; PTHR47117:SF1; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF12473; DUF3694; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF12423; KIF1B; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}.
FT DOMAIN 5..355
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 517..572
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 1668..1766
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 860..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1622..1651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 431..458
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 628..677
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 860..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..929
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 96..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1783 AA; 201724 MW; 1E4633F9570E55F7 CRC64;
MAGASVKVAV RVRPFNSREI EKDSKLIIQM SGNTTTIINP KQAKDNKSFN FDYSYWSHTS
PEDVNYASQK QVYKDIGEEM LLHAFEGYNV CIFAYGQTGA GKSYTMMGKQ DVKDQQGIIP
LLCEDLFTKI NDNTDNSMSY SVEVSYMEIY CERVRDLLNP KNKGHLRVRE HPLMGPYVED
LSKLAVTSYN DIQDLMDSGN KARTVAATNM NETSSRSHAV FNIIFTQKRH DTEMDNTTEK
VSKISLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEMGS GPNKNKKKKK
AESFIPYRDS VLTWLLRENL GGNSRTAMVA ALSPADINYD ETLSTLRYAD RAKQIRCNAV
INEDPNNRLV RELKEEVSRL KELLFAQGLG DIIEMTNAMT GMSPSPSLSA LSSRAGSIAS
LHDRIMFSPG SEEAIERLKE TEKIIAELNE TWEEKLRRTE AIRMEREALL AEMGVAMRED
GGTVGVFSPK KTPHLVNLNE DPLMSECLLY YIKDGITRVG RLDASSRQDI VLSGHFIKDE
HCTFTSSTGP MGETVILEPC EGAETYVNGK RVTEPTVLKS GNRIILGKSH VFRFNHPVQA
RADRDKNPCA ETPVEPVDWA FAQRELLEKQ GIDMKQEMEQ RLQELEDQYR KEREEASNLL
EQQRLDYESK LEALQKQVDR YNPEAPEEEE EPEEEVQWTE RERELAVWSF RKWRCYQFTS
LRDLLWGNAI FLKEANAISV ELKKKVQFQF VLLTDTLYSP LPPDLLPPEA TKDREKRQFP
RTIVAVEVQD QKNGATHYWT LEKLRQRLDL MREMYDRAAD VPNSTVEDCE NVMTGGDPFY
DRFPWFRLVG RNPIFNTCMS ERMSDPTPSP TLSTSEITEL ADSQREGRGE EEELEDLDDL
DDDIFLDDPS SELGVEDDDD DDDDDDEREL CRGSSEGLDP FYDRSPLFSV VGRAFVYLSN
LLYPVPLVHR VAIVSEKGEV KGFLRVAVQA ISADEEAPDY GSGVRQSGTA KISFEDQQYE
KFQSESCSVG LSHTGISQEE LRIVEGEGQN AEMGPSADEV NNNTSGSDEV ENPLKPGLDG
ALDTTLEHLR IGNIFTFRVT VLQASSISAE YADIFCQFNF IHRHDEAFST EPLKNTGRGP
PLGFYHVQNI AVEVTRSFVD YIKTQPIVFE VFGHYQKQPF LPLCKDVMSP LRPCRRQFPR
VMPLSKPVPA TKLTAMTRPQ AGPCHCKYDL MVFFEICELE ANGDYIPAVV DHRGGMPCHG
TFLLHQGLQR RITVTIVHES GNDIEWKEVR ELVVGRLRNT PESDETIIDP NILSLNILSV
GYVRPLHDDR QFLDSDMPRT FFRFEAAWDS SMHNSLLLNR VTPYGEKIYM TLSAYLEMEN
CTQPAVITKD ICMVFYSRDT KLSASRSIRN LFGTGSLRAA DGNRVTGVYE VSLCHQADAG
SPGMQRRRRR VLDTSVAYVR GEENLAGWRP RSDSLILDHQ WELEKLSLLQ DVEKTKHYLL
LREKLESTLL MGQETLQSCV TDELNESPQP TEMDPEVSCN EITTERQREL AAKCLRLLTH
SFNREYSHVC VSASESKISE MSITTLREST SISALNTITP SSTCPSLVEG CYSNAGLRPP
VPRSRVVSSG PDAQQDAEAK KSINGASETK PQTRKFVPDI QEIRVSPIVS KKGYLHFLEP
LTNGWVKRYV VVRRPYVYIY NTERDAVERA ILNLSSAQVE YSEDQQAMLK TPNTFAVCTE
HRGILLQATN DKDMHDWLYA FNPLLAGTIR SKLSRRRAGQ MRM
//