KIF27_RAT
ID KIF27_RAT Reviewed; 1394 AA.
AC Q7M6Z5;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Kinesin-like protein KIF27;
GN Name=Kif27;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
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]
RP IDENTIFICATION.
RX PubMed=12783626; DOI=10.1186/1471-2164-4-22;
RA Oduru S., Campbell J.L., Karri S., Hendry W.J., Khan S.A., Williams S.C.;
RT "Gene discovery in the hamster: a comparative genomics approach for gene
RT annotation by sequencing of hamster testis cDNAs.";
RL BMC Genomics 4:22-22(2003).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672; SER-675; SER-704;
RP SER-999; SER-1365 AND SER-1387, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
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).
CC -!- FUNCTION: Plays an essential role in motile ciliogenesis.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with STK36. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell
CC projection, cilium {ECO:0000250}. Note=Localizes to centrioles and
CC basal bodies. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIF27 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; AABR03104681; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03107397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03106101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03107556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK001053; DAA01311.1; -; mRNA.
DR RefSeq; NP_932167.1; NM_198050.1.
DR RefSeq; XP_006253618.1; XM_006253556.3.
DR RefSeq; XP_008769646.1; XM_008771424.2.
DR AlphaFoldDB; Q7M6Z5; -.
DR SMR; Q7M6Z5; -.
DR STRING; 10116.ENSRNOP00000026054; -.
DR iPTMnet; Q7M6Z5; -.
DR PhosphoSitePlus; Q7M6Z5; -.
DR jPOST; Q7M6Z5; -.
DR PaxDb; Q7M6Z5; -.
DR PRIDE; Q7M6Z5; -.
DR Ensembl; ENSRNOT00000026054; ENSRNOP00000026054; ENSRNOG00000019257.
DR GeneID; 246209; -.
DR KEGG; rno:246209; -.
DR UCSC; RGD:621071; rat.
DR CTD; 55582; -.
DR RGD; 621071; Kif27.
DR eggNOG; KOG0244; Eukaryota.
DR GeneTree; ENSGT00940000157487; -.
DR HOGENOM; CLU_005591_0_0_1; -.
DR InParanoid; Q7M6Z5; -.
DR OMA; SDLCGTE; -.
DR OrthoDB; 369179at2759; -.
DR PhylomeDB; Q7M6Z5; -.
DR TreeFam; TF325946; -.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-983189; Kinesins.
DR PRO; PR:Q7M6Z5; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000019257; Expressed in testis and 6 other tissues.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; ISO:RGD.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0021591; P:ventricular system development; ISO:RGD.
DR Gene3D; 3.40.850.10; -; 1.
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 Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Motor protein;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..1394
FT /note="Kinesin-like protein KIF27"
FT /id="PRO_0000307145"
FT DOMAIN 5..341
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 551..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1267..1340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1375..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 352..418
FT /evidence="ECO:0000255"
FT COILED 493..554
FT /evidence="ECO:0000255"
FT COILED 709..980
FT /evidence="ECO:0000255"
FT COILED 1010..1078
FT /evidence="ECO:0000255"
FT COILED 1118..1152
FT /evidence="ECO:0000255"
FT COILED 1187..1226
FT /evidence="ECO:0000255"
FT COMPBIAS 551..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 84..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7M6Z4"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7M6Z4"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 704
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 999
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 1394 AA; 158880 MW; 78E6AA7FF01C7987 CRC64;
MEEIPIKVAV RIRPLLCKEV LHNHQVCVRD IPKTQQIIIG RDRVFTFDFV FGKNSTQDEV
YSTCIKPLVL SLIEGYNATV FAYGQTGSGK TYTIGGGHVA SVVDGQKGII PRAIQEIFQS
ISGNPNIDFK IKVSYIEVYK EDLRDLLELE TSMKDLHIRE DEKGNTVIVG AKECQVDSVE
DVMGLLQVGN AARHTGTTQM NEHSSRSHAI FTISVCQVGK SAEATEDGEW CSHRHIVSKF
HFVDLAGSER VTKTGNTGER FKESIQINSG LLALGNVISA LGDPRRKSSH VPYRDAKITR
LLKDSLGGSA KTVMITCVSP SSSDFDESLN SLKYANRARN IRNKPTLNFS PQADRMDEME
FEIKLLREAL QSHQASISQT SQTASENVPD QNRIHSLEEQ IAQLQEECLG YQDCIEQAFA
FLVDLKDAVR LNQKQQHKLQ QWFSRTQEVR KAVLTPLPGN QSIGNLEEGP QHVTVLQLKR
ELKKYQCALA ADQVVFTQKE LELEELRRQM QLMAQESKGH AVSLKEAQKV NRLQNEKIIE
QQLLVDQLSE ELAKRSSSMP TSTKESCGDG PDARAPEKRP HTAPFDSHWG HYVYIPSRQD
FKKVCSSSPV YSLDQVFAGF RTRSQMLMGH LEDQDEVLHC QFSDNSDDED SEGQEKPRVR
SRSHSWVKKP GSVCSLVEMS DTQAECQRSY LGNGDLKMES LQESQELNLQ KLRTSELILN
KAKQKMRELT INIRMKEDLI KELIKTGDNA KSVSRQYSLK VTKLEHEAEQ AKVELTETRK
QLQELEGKDL SDVALKVKLQ KEFRKKMDAA KLRVQVLQKK QQDSKKLASL SIQNEKRASE
LEQNVDHLKY QKVQLQRRLR EESEKKKQLD AEVKRDQQKL KELQLNAGQG EGLHPKAEDT
DAFNLNRRKG PFRSVDQLQK LDEQRKWLDE EVEKVLSQRQ ELEMLEEELK KREAIVSKKE
ALLQEKSHLE NKKLRSSQAL STDSLKISAR LNLLDQELSE KSLLLENSPT EEKVKISEQV
QALQREREQL QRQRNSVDEK LRHGRVLSPK EEHLLFQLEE GIEALEAAIE FKNESIQNRQ
SSLKSSFQNL SQSESNVLEK LVCLNIAEIR AILFKYFNKV INLREAERKQ QLQNKEMKMK
VLERDNMVHE LESALEYLRL QCDRRLTLQQ KEHEQKMQLL LHHFKDQDGE GIIETLNKYE
DKIQQLEKDL YFYKKTSRDL KKRLKDPVQG AVQWQRTLTE HHDAGDGVLN PEEAAVLSEE
LKWASRTENT KLNGREKEVD NSSSSLKTPP LTQQILEDGP DSLPVCGSLA PSSGQLQSSA
DKTEAHAFTQ SQSPPPPQLQ PVRSIAQLQG VKPVKVCRRE LRQISALELT LRRSSLGAGV
RSVTADSLEE PEES
