ID M3XMC6_MUSPF Unreviewed; 1662 AA.
AC M3XMC6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Kinesin family member 21A {ECO:0000313|Ensembl:ENSMPUP00000000226.1};
DE SubName: Full=Kinesin-like protein KIF21A isoform X5 {ECO:0000313|RefSeq:XP_004771890.1};
GN Name=KIF21A {ECO:0000313|Ensembl:ENSMPUP00000000226.1,
GN ECO:0000313|RefSeq:XP_004771890.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000000226.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000000226.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004771890.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004771890.1};
RG RefSeq;
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}.
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DR EMBL; AEYP01077616; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01077617; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01077618; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01077619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01077620; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004771890.1; XM_004771833.3.
DR STRING; 9669.ENSMPUP00000000226; -.
DR Ensembl; ENSMPUT00000000230.1; ENSMPUP00000000226.1; ENSMPUG00000000229.1.
DR GeneID; 101681689; -.
DR CTD; 55605; -.
DR eggNOG; KOG0244; Eukaryota.
DR GeneTree; ENSGT00940000155323; -.
DR HOGENOM; CLU_001485_4_5_1; -.
DR OMA; GECTPIG; -.
DR OrthoDB; 1131899at2759; -.
DR Proteomes; UP000000715; Unplaced.
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; 2.
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:UP000000715};
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 1331..1370
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1610..1643
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 553..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 379..513
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 927..961
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 557..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..622
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1181..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1224..1250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1292
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 1662 AA; 185844 MW; 1E74D19B4FB12E30 CRC64;
MWGAPDESSV RVAVRIRPQL AKEKIEGCHI CTSVTPGEPQ VFLGKDKAFT FDYVFDIESQ
QEQIYTQCIE KLIEGCFEGY NATVFAYGQT GAGKTYTMGT GFDVNIIEEE QGIISRAVKH
LFKSIEEKKH TAIKNGLPPP DFKVNAQFLE LYNEEVLDLF DTTRDIDAKN KKSNIRIHED
STGGIYTVGV TTRTVNTESE MMQCLKLGAL SRTTASTQMN VQSSRSHAIF TIHLCQTRMC
PQIDAENATD NKVISESSQL NEFETLTAKF HFVDLAGSER LKRTGATGER AKEGISINCG
LLALGNVISA LGDKSKRATH VPYRDSKLTR LLQDSLGGNS QTIMIACVSP SDRDFMETLN
TLKYANRARN IKNKVMVNQD RASQQINALR SEITRLQMEL MEYKTGKRII DEEGVESIND
MFHENAMLQT ENNNLRVRIK AMQETVDALR TRITQLVSDQ ANQVLARAGE GNEEISNMIH
SYIKEIEDLR AKLLESEAVN ENLRKNLTRA TARSPYFSGS SAFSPTILSS DKETIEIIDL
AKKDLEKLKR KEKKKKKSVA GKEDNTDTDQ EKKEEKGITE RENNELEVEE SQEVSDHEEE
EEEEEEEEDD IEGGESSDES DSESDEKANY QADLANITCE IAIKQKLIDE LENSQKRLQT
LKKQYEEKLM MLQHKIRDTQ LERDQVLQNL GSVESYSEEK AKKVRSEYEK KLQAMNKELQ
RLQTAQKEHA RLLKNQSQYE KQLKKLQQDV MEMKKTKVRL MKQMKEEQEK ARLTESRRNR
EIAQLKKDQR KRDHQLRLLE AQKRNQEVVL RRKTEEVTAL RRQVRPMSDR VAGKVTRKLS
SSDTPVQDAG SSAVAVEADV SRAGAQQKMR IPVARVQALP TPTTNGTRKK YQRKGLTGRV
FTSKTARMKW QLLERRVTDI IMQKMTISNM EADMNRLLKQ REELTKRREK LSKRREKIVK
ESGEGDKNVV NINEEMESLT ANIDYINDSI SDCQANIMQM EEAKEEGETL DVSAVINACT
LTEARYLLDH FLSMGINKGL QAAQKEAQIK VLEGRLKQTE ITSATQNQLL FHMLKEKAEL
NPELDALLGH ALQDLDSVPL ENVEDSTDEE APLNSPGSEG STLSSDLMKL CGEVKPKSKA
RRRTTTQMEL LYADSSELAS DTSTGDASLP GPLTPVAEGQ EIGMNTETSG TSAREKELPP
PSGFPSKIGS ISRQSSLSEK KLPEPSPITR RKAYEKTEKS KSKEQKHSDS GTSEASLSPP
SSPPSRPRNE LNVFNRLTVS QGNTSVQQDK SDESDSSLSE VHSRSSRRGI INPFPASKGI
RTNPLQCLHI AEGHTKAVLC VDSTDDLLFT GSKDRTCKVW NLVTGQEIMS LGGHPNNVVS
VKYCNYTSLV FTVSTSYIKV WDIRDSAKCI RTLTSSGQVT LGDACSASTS RTVAIPSGEN
QINQIALNPT GTFLYAASGN AVRMWDLKRF QSTGKLTGHL GPVMCLTVDQ ISNGQDLIVT
GSKDHYIKMF DVTEGALGTV SPTHNFEPPH YDGIEALTIQ GDNLFSGSRD NGIKKWDLAQ
KDLLQQVPNA HKDWVCALGV VPGHPVLLSG CRGGILKLWN VDTFVPVGEM KGHDSPINAI
CVNSTHIFTA ADDRTVRIWK ARSLQDGQIS DLGDLGEDIA IN
//
