ID A0A2U4BAE1_TURTR Unreviewed; 1660 AA.
AC A0A2U4BAE1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Kinesin-like protein KIF21A isoform X2 {ECO:0000313|RefSeq:XP_019790183.1};
GN Name=KIF21A {ECO:0000313|RefSeq:XP_019790183.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019790183.1};
RN [1] {ECO:0000313|RefSeq:XP_019790183.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019790183.1};
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 RefSeq; XP_019790183.1; XM_019934624.2.
DR STRING; 9739.ENSTTRP00000012175; -.
DR GeneID; 101332772; -.
DR OrthoDB; 1131899at2759; -.
DR Proteomes; UP000245320; Chromosome 11.
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:UP000245320};
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 1329..1368
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1608..1641
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..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 379..513
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 634..816
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 835..853
FT /note="Polar 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 1206..1221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1291
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 1660 AA; 185882 MW; 4CAC3380D0703BAD CRC64;
MWGAPDESSV RVAVRIRPQL AKERIEGCHI CTSVTPGEPQ VFLGKDKAFT FDYVFDIDSQ
QEQIYTQCIE KLIEGCFEGY NATVFAYGQT GAGKTYTMGT GFDVNIIEEE QGIISRAVKH
LFKSIEEKKH TSIKNGLPPP DFKVNAQFLE LYNEEVLDLF DTTRDIDAKN KKSNIKIHED
SAGGIYTVGV TTRTVITESE MMQCLKLGAL SRTTASTQMN VQSSRSHAIF TIHLCQTRMC
PQIDAESATD NKVISESSQM NEFETLTAKF HFVDLAGSER LKRTGATGER AKEGISINCG
LLALGNVISA LGDKSKRATH VPYRDSKLTR LLQDSLGGNS QTIMIACVSP SDRDFMETLN
TLKYANRARN IKNKVMVNQD RASQQINALR SEITRLQMEL MEYKTGKRII DEEGVESIND
MFHENAMLQT ENNNLRVRIK AMQETVDVLR TRITQLVSDQ ANQVLARAGE GNEEISNMIH
NYIKEIEDLR AKLLESEAVN ENLRKNLTRA TARSPYFSGS SAFSPTIVSS DKETIEIIDL
AKKDLEKLKR KEKKKKKSVA GKEDNTDTDQ EKKEEKGISE RESNELEVEE SQEVSDHEDE
EEEEEEEEDD IEGGESSDES DSESDEKANY QADLANITCE IAIKQKLIDE LENSQKRLQT
LKKQYEEKLM MLQHKIRDTQ LERDQVLQNL GSVESYSEEK AKKVRSEYEK KLQAMNKELQ
RLQTAQKEHA RLLKNQSQYE KQLKKLQQDV MEMKKTKVRL MKQMKEEQEK ARLTESRRNR
EIAQLKKDQR KRDHQLRLLE AQKRNQEVVL RRKTEEVTAL RRQVRPMSDK VAGKVTRKLS
STDTPVQDTG SSATTIETDA SRAGAQQKMR IPVARVQALP TPTTNGTRKK YQRKGLTGRV
FTSKTARMKW QLLERRVTDI IMQKMTISNM EADMNRLLKQ REELTKRREK LSKRREKIVK
ENGEGDKNVV TINEEMESLT ANIDYINDSI SDCQANIMQM EEAKEEGETL DVTAVINACT
LTEARYLLDH FLSMGINKGL QAAQKEAQIK VLEGRLKQTE ITSATQNQLL FHMLKEKAEL
NPELDALLGH ALQDLDSIPL ENVEDSTDED VPLNSPGSEG SSLSSDLMKL CGEVKPKNKA
RRRTTTQMEL LYADSSELAS DTSTGDASLP GPLTPVAEGQ EIGMNTETST SAREKELPPP
SGFPSKIGSI SRQSSVSEKK LPEPSPVTRR KAYEKGEKSK AKEQKHSDSG TSEASLSPPS
SPPSRPRNEL NVFNRLTVSQ GNTSVQQDKS DESDSSLSEV HRSSRRGIIN PFPALKGIRA
SPLQCIHIAE GHTKAVLCVD STDDLLFTGS KDRTCKVWNL VTGQEIMSLG GHHNNVVSVK
YCNYTSLVFT VSTSYIKVWD IRDSAKCIRT LTSSGQVTLG DACSATTSRT VTIPSGENQV
NQIALNPTGT FLYAASGNAV RMWDLKRFQS TGKLTGHLGP VMCLTVDQIS SGQDLIITGS
KDHYIRMFDV TEGALGAVSP THNFEPPHYD GIEALTIQGD NLFSGSRDNG IKKWDLAQKD
LLQQVPNAHK DWVCALGVMP GHPVLLSGCR GGILKLWNID TFVPVGEMKG HESPINAICV
NSTHIFTAAD DRTVRIWKTR NLQDGQLFDT GDPVEDIASN
//
