ID A0A3P9N270_POERE Unreviewed; 1677 AA.
AC A0A3P9N270;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Kinesin family member 21B {ECO:0000313|Ensembl:ENSPREP00000003645.1};
GN Name=KIF21B {ECO:0000313|Ensembl:ENSPREP00000003645.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000003645.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000003645.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000003645.1};
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}.
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 RefSeq; XP_017160374.1; XM_017304885.1.
DR Ensembl; ENSPRET00000003700.1; ENSPREP00000003645.1; ENSPREG00000002626.1.
DR GeneID; 103464904; -.
DR CTD; 23046; -.
DR GeneTree; ENSGT00940000159650; -.
DR OrthoDB; 1131899at2759; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
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; 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:SF34; KINESIN-LIKE PROTEIN KIF21B; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF00400; WD40; 5.
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}; Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 8..374
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REPEAT 1361..1400
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1401..1434
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1557..1596
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1598..1639
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1640..1669
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 517..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1148..1179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1254..1306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 382..516
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 664..846
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 560..591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..651
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1175
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 1677 AA; 187979 MW; 14347E83D41827C0 CRC64;
MASQSDCCVK VALRIRPQMA KEKIEGCHVC TLVTPGEPQV LLGKDKAFTY DFVFDIDSEQ
QRIYQTCVYK LIEGCFEGYN ATVFAYGQTG SGKTYTMGTG FDVSLSLQEQ GIIPRAVHQL
FEGIQSRRDR AQETGIQPPE FKVSAQFLEL YNEEILDLFD GSRDPESRSR KSNIKIHEDA
NGSIYTTGVT SRLVQSEDEL LQCLKLGALS RTTASTQMNA QSSRSHAIFT IYLCQMRVFQ
QQQMNGGEEN GEVNGVDSSP IAQPEYETLM AKFHFVDLAG SERLKRTGAT GERAREGISI
NCGLLALGNV ISALGDQTKK AGHVPYRDSK LTRLLQDSLG GNSRTVMIAC VSPSDRDFME
TLNTLKYANR ARNIKNKVVV NQDKTSQQIN ALRAEVARLQ MELMEYKAGK RVAGEDGAEG
YSDLYQENAM LQRENDSLRL RVKAMQETID HLNTRVTHLL ANEVSTLLTK SSEGNEEIGT
LIQNYIREVE ELRSKLLESE AMNESLRRQV ARLSSRSSFP ASSLSPAPGH PPGSSPISMS
MEAEMTDVLR RAKLDIERLK KKERRQRRLS PELEKGLKKR VKLHTQENGE NRRSGENGQN
GEIDSDDNYT EDIMSPLQEE SGCEEDEGED EEEGREEEDD FDSDESLVDS DSDSDEKANF
QADLADLTCE IEIKQKLIDE LENSQRRLLM LKLQYEEKLI LLQNKIRDTQ LERDRVLQNL
MSMENYTEEK ASKIRQEYEK RLKEMNRDLL KLQVAQKEHA RLLKNQGRYE RELKKLQTEV
NEMKKAKVVL MKQMKEEQQR RRMVEAKRNR EIAQLKKEQR RQEYQIRALE SQKRQQELVL
RRKTQEVTAL RRMAKPMSDR VAGRVARWNQ TPPVTDSGAD LSASTMASGS EAETARTVSG
LVRQWNNKNN VYGYMAESEG SMDGTRVISR KKLQKKPAGL GSTAPAGRAN SFSKSARLKW
QTLERRIMDI VMQRMTISNV EADMDRLIKK REELTMQQEA FSHKREVLMA DGEGPEAEDR
LLQEVNEEIE VLNANIDYIN DSLSDCQATI VQIEETKDEL DSVDTSVVIS SCSLAEARHL
LDHFLKASID KSLQVAQREA QIRLLEGQLR QTDVIGSSHN HMILDALREK AECIPELQAL
IHNVQQENGY ASTDEEPSEF SQASDSSVSQ MKESNSQDDF KIKMEPRLSA QMKAVSAEYL
GPILDPSSSS KQQHITKSLA SLTDIQEDGL GLVPGSLALS VPLRDPFHRE RASRTISLPV
RGHTFPRQSR GYDTSPITRR KSYDRSYRPT DVYTPPSSPP LRTRNDRNVF SRLTSNQAQG
SALDKSDDSD SSLSEVLRGV INPIGGVKGG RTAPLQCVSV AEGHSKPVLC VDATDELLFT
GSKDRTCKMW NLVTGQEIAT LKGHPNNVVS VKYCPSSGLA FSVSTSYIKV WDIRDSAKCI
RTLTSSGQVV TGDACAGTTT RTITFAQGEC QINQIALNPS GSVLYAATGN IVRMWDLNRM
QATGKLSGHI GSVMCLTVGQ SLLGKDQVIT GSKDHYVKIF DVAEGTLGNV GPAHNFEPPH
YDGIECLAVQ GDVLFSGSRD NGIKKWELEQ QELTQQIPNA HKDWVCALAY VPGRPMLLSA
CRGGMLKVWN VENFTPIGEV RGHDSPINAI CTNSRHIFTA SSDKTVKIWL SKVWRKR
//
