ID D4A1V5_RAT Unreviewed; 1603 AA.
AC D4A1V5;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Kinesin family member 21A {ECO:0000313|Ensembl:ENSRNOP00000040915.4};
GN Name=Kif21a {ECO:0000313|Ensembl:ENSRNOP00000040915.4,
GN ECO:0000313|RGD:1305126};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000040915.4, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000040915.4, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000040915.4,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0007829|PubMed:16641100}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [3] {ECO:0007829|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4] {ECO:0000313|Ensembl:ENSRNOP00000040915.4}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000040915.4};
RG Ensembl;
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}.
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_008764054.1; XM_008765832.2.
DR RefSeq; XP_008774790.1; XM_008776568.2.
DR jPOST; D4A1V5; -.
DR Ensembl; ENSRNOT00000046744.6; ENSRNOP00000040915.4; ENSRNOG00000014844.9.
DR AGR; RGD:1305126; -.
DR RGD; 1305126; Kif21a.
DR VEuPathDB; HostDB:ENSRNOG00000014844; -.
DR GeneTree; ENSGT00940000155323; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000014844; Expressed in cerebellum and 17 other cell types or tissues.
DR ExpressionAtlas; D4A1V5; baseline and differential.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0071532; F:ankyrin repeat binding; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR CDD; cd01372; KISc_KIF4; 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; 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:SF30; KINESIN MOTOR DOMAIN-CONTAINING PROTEIN; 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; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, 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};
KW Proteomics identification {ECO:0007829|PeptideAtlas:D4A1V5};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494};
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 1272..1311
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1551..1581
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 553..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 379..506
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 636..684
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 929..963
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 558..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..624
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1245
FT /note="Basic and acidic 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 1603 AA; 179079 MW; 832392F9065F3C03 CRC64;
MLGAADESSV RVAVRIRPQL AKEKIEGCHI CTSVTPGEPQ VFLGKDKAFT FDYVFDIDSQ
QEQIYTQCIE KLIEGCFEGY NATVFAYGQT GAGKTYTMGT GFDVNIMEEE QGIISRAVKH
LFKSIEEKKT SAIKNGVPPP EFKVNAQFLE LYNEEVLDLF DTTRDIDAKN KKSNIRIHED
STGGIYTVGV TTRTVNTEPE MMQCLKLGAL SRTTASTQMN VQSSRSHAIF TIHVCQTRVC
PQTDAENVTD NKMVSESPQM NEFETLTAKF HFVDLAGSER LKRTGATGER AKEGISINCG
LLALGNVISA LGDKSKRATH VPYRDSKLTR LLQDSLGGNS QTIMIACVSP SDRDFMETLN
TLKYANRARN IKNKVMVNQD RASQQINALR SEITRLQMEL MEYKTGKRII DEEGVESIND
MFHENAMLQT ENNNLRVRIK AMQETVDALR ARITQLVSEQ ANQVLARAGE GNEEISNMIH
SYIKEIEDLR AKLLESEAVN ENLRKSLTRA TARSPFFSAS SAFSSTILSS DKETIEIIDL
AKKDLEKLKR KEKRKKKSVA GKENNADPDQ EKKEEKGVSE KESSEVDVDE NQEASDHEDE
EDEEEEDEEE DDIEGEESSD ESDSESDEKA NYQADLANIT CEIAIKQKLI DELENSQKRL
QTLKKQYEEK LMMLQHKIRD TQLERDQVLQ NLGSVESYSE EKAKKVKCEY EKKLHAMNKE
LQRLQTAQKE HARLLKNQSQ YEKQLKKLQQ DVTEMKKTKV RLMKQMKEEQ EKARLTESRR
NREIAQLKKD QRKRDHQLRL LEAQKRNQEV VLRRKTEEVT ALRRQVRPMS DKVAGKVTRK
LSSSESPTPD AGSSVTSGEA DASRPGTQQK MRIPVARVQA LPTPTTNGTR KRYQRKGFTG
RVFTSKTARM KWQLLERRVT EIIMQKMTIS NMEADMNRLL RQREELTKRR EKLSKRREKI
AKESGEGDKN LVNISEEMES LTANIDYIND SIADCQANIM QMEEAKEEGE TLDVTAVINA
CTLTEARYLL DHFLSMGINK GLQAAQKEAQ IKVLEGRLKQ TEITSATQNQ LLFHMLKEKA
ELNPELDALL GNALQDLDSA PLEDEEDSSE EDGPLHSPGS EGSTLSSDLM KLCGEVKPKN
KARRRTTTQM ELLYADSSEV ASDTSAGDAS LPGPLTPVAE GQETGMNTET SVPSARDKEL
LPPSGLPPKI GSISRQPSVS EKKVPEPSPV TRRKAYEKAD KAKTKEQKQG IINPFPACRG
IRASFLQCVH VAEGHTKAVL CVDSTDDLLF TGSKDRTCKV WNLVTGQEIM SLGVHPNNVV
SVKYCNYTSL VFTVSTSYIK VWDIRESAKC IRTLTSSGQV TLGEACSAST SRTVAIPSGE
SQINQIALNP TGTFLYAASG NAVRMWDLKR FQSTGKLTGH LGPVMCLTVD QISNGQDLII
TGSKDHYIKM FDVTEGALGT VSPTHNFEPP HYDGIEALAI QGDNLFSGSR DNGIKKWDLA
QKGLLQQVPN AHKDWVCALG LVPGHPILLS GCRGGILKLW NVDTFVPVGE MRGHDSPINA
ISVNSTHVFT AADDRTVRIW KAHNLQDGQI SDTGDPGEDS TSN
//
