ID A0A3Q1FMV7_9TELE Unreviewed; 1568 AA.
AC A0A3Q1FMV7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Kinesin family member 21A {ECO:0000313|Ensembl:ENSAPOP00000017012.1};
GN Name=KIF21A {ECO:0000313|Ensembl:ENSAPOP00000017012.1};
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:ENSAPOP00000017012.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000017012.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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}.
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; ENSAPOT00000026169.1; ENSAPOP00000017012.1; ENSAPOG00000020340.1.
DR GeneTree; ENSGT00940000155323; -.
DR Proteomes; UP000257200; Unplaced.
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; cd01372; KISc_KIF4; 1.
DR CDD; cd22263; Rcc_KIF21A; 1.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR027640; Kinesin-like_fam.
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; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR PANTHER; PTHR47969:SF30; KINESIN MOTOR DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46579; Prefoldin; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 9..368
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REPEAT 1240..1279
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1280..1311
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1517..1556
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 510..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1122..1206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 376..403
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 897..931
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 555..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..622
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1091
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 88..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1568 AA; 175079 MW; 87AC79FAA05F57D7 CRC64;
MTTGQDESSV RVALRIRPQL AREKIEGCHI CTYVMPGEPQ VILGKDKAFT YDYLFDMDSQ
QDAIYSTCTE KLIEGCFEGY NATVFAYGQT GSGKTYTMGT GFDVNIVDEE LGIIPRAVHH
LFKGIEERRQ AAQEQGRPVP EFKINAQFLE LYNEEVLDLF DSTRDMKQKS HIKIHEDATG
GIYTVGVTTR TVSSEAEMMQ CLKLGALSRT TASTQMNVQS SRSHAIFTIH LCQVRVCASD
NQEDETDNRV SNGNSEMDEY ETLTAKFHFV DLAGSERLKR TGATGDRAKE GISINCGLLA
LGNVISALGD RSKRSSHVPY RDSKLTRLLQ DSLGGNSQTV MIACISPSDR DFMETLNTLK
YANRARNIKN KVMVNQDKAS QQISALRTEI ARLQMELMEY KTGKRMVGED GIESFSDMFH
ENSMLQTENS NLRVRVKAMQ ETIDAQRVRL TQLISDQANQ ALARAGEGGT EEIGNMIQGY
IKEIEDLRAK LLESEAVNEN LRKNLSRASN RQSFYGGSGS FSSSLLAPEK ETSDIIELAK
KDLEKLKKRE KKKKKSANKE EVPDNDQEKG TEKEMTERAN EDTEMEVQDG SDHEEAEEEE
EEEEEEMDVE ESSDDSDSES DEKENFQADL ANITCEIAIK QKLIDELENS QRRLHTLKQQ
YEQKLMMLQC KIRDTQLERD RVLQNMTSVE SGTEDKARKI KAEYEKKLSV MNKELQKLQS
AQKEHARLLK NQSQYEKQLK KLQMDVTEMK KTKVRLMKQM KEQQEKNRMN ESRRNREIAS
LKKDQRKQEH QLKLLEAQKR QQELILRRKT EEVTALRRQV RPTSGKVIRK VNLPEPVQDS
PHRPPSGRLY SSSNAAPNGT RSSYRRTAGI YSTRIARNKW QSLERRITDV IMQRMTISNM
EADMNRLLKQ REELTKRKEK VIRKRDRLIK EGPETEKTVL PLNEEVDALT ANIDYINDSI
ADCQANIMQM EETKEEGDTV DVSAVIGSCT LAEARFLLDH FMSMAINKGL QAAQRESQVK
VMEGRLKQTE ITSATQNQLL FHMLKEKAEF NPELDALLGN ALQELGNLPA ENGDDSSSDE
SAQSPSAEGN TLASDLMKLC GETKTRNKAR RRTTTQMELL YANSDSAPDA PTADFSSPML
PLTETPDGGG DMDLSGSSVR DYTALSPGFS SKMGSISGSR TPGVEKRAPE PSPLSRRKTY
DKAQAAADRA KVKEIKQGVI NPVPSTKSSR SATLQCVHVA EGHSKAVLCV DSTDDLLFTG
SKDRTCKVWN LVTGQEIMSL AGHPNNVVSV RYSSSLVFTV STSYIKVWDI RDSAKCIRTL
TSSGQVNVGD ACASNTSRTV TIPAGENQIN QIALNPNGTV LYAAAGNSVR VWDLRRFAST
GKLTGHLGPV MCLTVDQSGN NQDLVITGSK DHYIKLFDVT EGSLGSISPT HNFEPPHYDG
IESLVVQGDI FFSGSRDNGI KKWDLDRKDL LQQVPNAHRD WVCALGVVPG SPALLSGCRG
GVLKLWHTDT LGTLGELKGH ESPINGISTN SSHLFTASDD RTVKIWRARG GLDSTSEVVD
NADEVASN
//
