ID A0A3B5A3M1_9TELE Unreviewed; 1642 AA.
AC A0A3B5A3M1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Kinesin family member 21B {ECO:0000313|Ensembl:ENSSPAP00000015848.1};
GN Name=KIF21B {ECO:0000313|Ensembl:ENSSPAP00000015848.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000015848.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000015848.1}
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; ENSSPAT00000016103.1; ENSSPAP00000015848.1; ENSSPAG00000011855.1.
DR GeneTree; ENSGT00940000159650; -.
DR Proteomes; UP000261400; 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; cd00200; WD40; 1.
DR Gene3D; 6.10.250.2730; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
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:SF34; KINESIN-LIKE PROTEIN KIF21B; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF00400; WD40; 6.
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; 5.
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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 8..375
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REPEAT 1326..1365
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1366..1399
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1522..1561
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1563..1604
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1605..1634
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 501..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 665..847
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 978..1043
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 504..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..652
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..899
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1642 AA; 183584 MW; 1ADFE5DF444E5641 CRC64;
MASQGDCCVK VALRIRPQMA KEKIEGCHVC TLVTPGEPQV LLGKDKAFTY DFVFDIDSEQ
QHIYQACVYK LIEGCFEGYN ATVFAYGQTG SGKTYTMGTG FDVSLTQQEQ GIIPRAVHQL
FEGIQNRRLR AQETGSQPPE FKVSAQFLEL YNEEILDLFD GARDPESRSR KSNIKIHEDA
SGSIYTTGVT SRLVHTEEEL LQCLKLGALS RTTASTQMNA QSSRSHAIFT IHLCQMRVCQ
QLQMQNGGGE NGELNGVDSN PIAQPEYETL MAKFHFVDLA GSERLKRTGA TGERAREGIS
INCGLLALGN VISALGDQTK KGGHVPYRDS KLTRLLQDSL GGNSRTVMIA CVSPSDRDFM
ETLNTLKYAN RARNIKNKVV VNQDKTSQQI SALRAEIARL QMELMEYKAG KRVACEDGSE
GYSDLYQENA MLQRENDTLR LRVKAMQETI DHLNTRVTHL LANEVSTLLT KSSEGNEEIG
TLIQNYIREV EELRTKLLES ESMNESLRRQ AARLSARSPF PASSLSPAPG HPPGSSPAPM
SMEAEMTDVL RRAKLDIERL KKKERRQRRM SPELEKGLKK RVKLHTHENG ENGQSGENGQ
NGEIDSDDNY TEDIMSPLQE ESGCDEDEGE DEEECREEED EFDSDESLVD SDSDSDEKAN
FQADLADLTC EIEIKQKLID ELENSQRRLL MLKLQYEEKL ILLQNKIRDT QLERDRVLQN
LMSMENYTEE KANKIKQEYE KRLKEMNRDL LKLQAAQKEH ARLLKNQGRY ERELKKLQAE
VNEMKKAKVT LMKQMKEEQQ RRRMVEAKRN REIAQLKKEQ RRQEYQIRAL ESQKRQQEMV
LRRKTQEVTA LRRLAKPMSD RVAGRVARWN QTPPVTDSGA ELSASTTASS SEPETARTVS
GLVRQWNNKN SVYGYLGESE GSMDGTRVIG RKKLQRKPLG IGNIGAAGRA SSFSKSARQK
WQALERRIMD IVMQRMTISN VEADMDRLIK KREELTVQQE ALSHKREVLM AEGEGPEAED
RLLQEINEDI EVLNANIDYI NDSLSDCQAT IVQIEETKDE LDSVDTSVVI SSCSLAEARH
LLDHFLKASI DKSLQVAQKE TQIRLLEGQL RQTDVIGSSH NHIILDALRE KAEYIPELQA
LIHNVQQENG YASTDEEPSE FSQASDSSVS QMKESNSQED FKLKIEPRLS AQMKAVSAEY
LGPILDPTSG SKPQHITKSL ASLTDIQEDG LSLVTGSLGL SLALRDPYHR DRASRTISLP
VRGHTLPTDG YTPPSSPPLR TRNDRNVFSR LTSNQTQGSA LDKGVINPIG GVKGGRTAPL
QCVSVAEGHS KPVLCVDATD ELLFTGSKDR TCKMWNLVTG QEIVTLKGHP NNVVSVKYCP
SSCLVFSVST SYIKVWDIRD SAKCIRTLTS SGQVVSGDAC AGTTTRTITF AQGECQINQI
AINPSGSVLY AAAGNTVRMW DLNRMQAMGK LTGHIGSVMC LTVGQSLLGK DQVITGSKDH
YVKVFDVAEG TMGNVGPAHN FEPPHYDGIE CLAVQGDVLF SGSRDNGIKK WELEQQELTQ
QIPNAHKDWV CALAYVPGRP MLLSGCRGGM LKVWNVENFT PIGEVRGHES PINAICTNSR
QIFTASSDKT VKIWLSKVWR KR
//