ID A0A2K5LTQ3_CERAT Unreviewed; 1674 AA.
AC A0A2K5LTQ3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Kinesin family member 21A {ECO:0000313|Ensembl:ENSCATP00000016321.1};
GN Name=KIF21A {ECO:0000313|Ensembl:ENSCATP00000016321.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000016321.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000016321.1}
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 RefSeq; XP_011885000.1; XM_012029610.1.
DR STRING; 9531.ENSCATP00000016321; -.
DR Ensembl; ENSCATT00000040481.1; ENSCATP00000016321.1; ENSCATG00000031474.1.
DR GeneID; 105571722; -.
DR CTD; 55605; -.
DR GeneTree; ENSGT00940000155323; -.
DR OMA; GECTPIG; -.
DR OrthoDB; 1131899at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000031474; Expressed in frontal cortex and 11 other cell types or tissues.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0071532; F:ankyrin repeat binding; IEA:Ensembl.
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 CDD; cd01372; KISc_KIF4; 1.
DR CDD; cd00890; Prefoldin; 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; 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; 4.
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:UP000233060};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 9..371
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REPEAT 1343..1382
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1539..1578
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1580..1615
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1622..1655
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 554..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 379..513
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 940..974
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 558..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..635
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1237..1263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1305
FT /note="Polar 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 1674 AA; 187337 MW; 588B163108FE7A08 CRC64;
MLGAPDESSV RVAVRIRPQL AKEKIEGCHI CTSVTPGEPQ VFLGKDKAFT FDYVFDIDSQ
QEQIYIQCIE KLIEGCFEGY NATVFAYGQT GAGKTYTMGT GFDVNIVEEE QGIISRAVKH
LFKSIEEKKH IAIKNGLPPP DFKVNAQFLE LYNEEVLDLF DTTRDIDAKN KKSNIRIHED
STGGIYTVGV TTRTVNTESE MMQCLKLGAL SRTTASTQMN VQSSRSHAIF TIHVCQTRVC
PQIDADSATD NKIISESAQM NEFETLTAKF HFVDLAGSER LKRTGATGER AKEGISINCG
LLALGNVISA LGDKSKRATH VPYRDSKLTR LLQDSLGGNS QTIMIACVSP SDRDFMETLN
TLKYANRARN IKNKVMVNQD RASQQINALR SEITRLQMEL MEYKTGKRII DEEGVESIND
MFHENAMLQT ENNNLRVRIK AMQETVDALR SRITQLVSDQ ANHVLARAGE GNEEISNMIH
SYIKEIEDLR AKLLESEAVN ENLRKNLTRA TARAPYFSGS STFSPTILSS DKETIEIIDL
AKKDLEKLKR KEKRKKKRLQ KLEESNREER SVAGKEDNTD TDQEKKEEKG ASERENNELE
VEESQEMSDH EDEEEEEEEE EDDIEGGESS DESDSESDEK ANYQADLANI TCEIAIKQKL
IDELENSQKR LQTLKKQYEE KLMMLQHKIR DTQLERDQVL QNLGSVESYS EEKAKKVRSE
YEKKLQAMNK ELQRLQAAQK EHARLLKNQS QYEKQLKKLQ QDVMEMKKTK VRLMKQMKEE
QEKARLTESR RNREIAQLKK DQRKRDHQLR LLEAQKRNQE VVLRRKTEEV TALRRQVRPM
SDKVAGKVTR KLSSSDAPAQ DTSSSAAALE TDASRTGVQQ KMRIPVARVQ ALPTPTTNGT
RKKYQRKGLT GRVFISKTAR MKWQLLERRV TDIIMQKMTI SNMEADMNRL LKQREELTKR
REKLSKRREK IVKENGEGDK NVANINEEME SLIANIDYIN DSISDCQANI MQMEEAKEEG
ETLDVTAVIN ACTLTEARYL LDHFLSMGIN KGLQAAQKEA QIKVLEGRLK QTEITSATQN
QLLFHMLKEK AELNPELDAL LGHALQDLDS VPLENVEDST DEDAPLNSPG SEGSTLSSDL
MKLCGEVKPK SKARRRTTTQ MELLYADSSE LASDTSTGDA SLPGPLTPVA EGQEIGMNTE
TSGTSAREKE LSPPPGLPSK IGSISRQSSL PEKKIPEPSP VTRRKAYEKA EKSKAKEQKH
SDSGTSEASL SPPSSPPSRP RNELNVFNRL TVSQGNTSVQ QDKSDESDSS LSEVHRSSRR
GIINPFPASK GIRAFPLQCI HIAEGHTKAV LCVDSTDDLL FTGSKDRTCK VWNLVTGQEI
MSLGGHPNNV VSVKYCNYTS LVFTVSTSYI KVWDIRDSAK CIRTLTSSGQ VTLGDACSAS
TSRTVAIPSG ENQINQIALN PTGTFLYAAS GNAVRMWDLK RFQSTGKLTG HLGPVMCLTV
DQISNGQDLI ITGSKDHYIK MFDVTEGALG TVSPTHNFEP PHYDGIEALT IQGDNLFSGS
RDNGIKKWDL TQKDLLQQVP NAHKDWVCAL GVVPDHPVLL SGCRGGILKV WNMDTFMPVG
EMKGHDSPIN AICVNSTHIF TAADDRTVRI WKARNLQDGQ ISDTGDLGED TASN
//
