KIF27_MOUSE
ID KIF27_MOUSE Reviewed; 1394 AA.
AC Q7M6Z4; Q14AX5; Q8BMB9;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Kinesin-like protein KIF27;
GN Name=Kif27;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 726-1394 (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP IDENTIFICATION (ISOFORM 1).
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH STK36.
RX PubMed=19305393; DOI=10.1038/nature07883;
RA Wilson C.W., Nguyen C.T., Chen M.H., Yang J.H., Gacayan R., Huang J.,
RA Chen J.N., Chuang P.T.;
RT "Fused has evolved divergent roles in vertebrate Hedgehog signalling and
RT motile ciliogenesis.";
RL Nature 459:98-102(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-643 AND SER-646, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays an essential role in motile ciliogenesis.
CC {ECO:0000269|PubMed:19305393}.
CC -!- SUBUNIT: Interacts with STK36. {ECO:0000269|PubMed:19305393}.
CC -!- INTERACTION:
CC Q7M6Z4; Q69ZM6: Stk36; NbExp=2; IntAct=EBI-15765182, EBI-15765145;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000305|PubMed:19305393}. Cell projection, cilium
CC {ECO:0000269|PubMed:19305393}. Note=Localizes to centrioles and basal
CC bodies.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=KIF27A;
CC IsoId=Q7M6Z4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7M6Z4-2; Sequence=VSP_028607, VSP_028608;
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; BC116646; AAI16647.1; -; mRNA.
DR EMBL; AK032912; BAC28083.1; -; mRNA.
DR EMBL; BK001056; DAA01314.1; -; mRNA.
DR CCDS; CCDS26570.1; -. [Q7M6Z4-1]
DR RefSeq; NP_780423.2; NM_175214.3. [Q7M6Z4-1]
DR RefSeq; XP_006517489.1; XM_006517426.3. [Q7M6Z4-1]
DR RefSeq; XP_006517490.1; XM_006517427.2. [Q7M6Z4-1]
DR RefSeq; XP_006517492.1; XM_006517429.3. [Q7M6Z4-1]
DR RefSeq; XP_006517494.1; XM_006517431.2. [Q7M6Z4-1]
DR RefSeq; XP_006517495.1; XM_006517432.2. [Q7M6Z4-1]
DR RefSeq; XP_006517496.1; XM_006517433.3. [Q7M6Z4-1]
DR RefSeq; XP_006517497.1; XM_006517434.2. [Q7M6Z4-1]
DR RefSeq; XP_006517498.1; XM_006517435.3. [Q7M6Z4-1]
DR RefSeq; XP_006517499.1; XM_006517436.3. [Q7M6Z4-1]
DR RefSeq; XP_011242881.1; XM_011244579.2. [Q7M6Z4-1]
DR RefSeq; XP_011242882.1; XM_011244580.2. [Q7M6Z4-1]
DR RefSeq; XP_017171108.1; XM_017315619.1. [Q7M6Z4-1]
DR RefSeq; XP_017171109.1; XM_017315620.1. [Q7M6Z4-1]
DR AlphaFoldDB; Q7M6Z4; -.
DR SMR; Q7M6Z4; -.
DR BioGRID; 217179; 4.
DR DIP; DIP-59753N; -.
DR IntAct; Q7M6Z4; 1.
DR STRING; 10090.ENSMUSP00000043304; -.
DR iPTMnet; Q7M6Z4; -.
DR PhosphoSitePlus; Q7M6Z4; -.
DR EPD; Q7M6Z4; -.
DR MaxQB; Q7M6Z4; -.
DR PaxDb; Q7M6Z4; -.
DR PeptideAtlas; Q7M6Z4; -.
DR PRIDE; Q7M6Z4; -.
DR ProteomicsDB; 269302; -. [Q7M6Z4-1]
DR ProteomicsDB; 269303; -. [Q7M6Z4-2]
DR Antibodypedia; 13061; 68 antibodies from 15 providers.
DR DNASU; 75050; -.
DR Ensembl; ENSMUST00000043605; ENSMUSP00000043304; ENSMUSG00000060176. [Q7M6Z4-1]
DR Ensembl; ENSMUST00000225388; ENSMUSP00000153598; ENSMUSG00000060176. [Q7M6Z4-1]
DR GeneID; 75050; -.
DR KEGG; mmu:75050; -.
DR UCSC; uc007qtq.1; mouse. [Q7M6Z4-1]
DR UCSC; uc011zao.1; mouse. [Q7M6Z4-2]
DR CTD; 55582; -.
DR MGI; MGI:1922300; Kif27.
DR VEuPathDB; HostDB:ENSMUSG00000060176; -.
DR eggNOG; KOG0244; Eukaryota.
DR GeneTree; ENSGT00940000157487; -.
DR HOGENOM; CLU_005591_0_0_1; -.
DR InParanoid; Q7M6Z4; -.
DR OMA; SDLCGTE; -.
DR OrthoDB; 369179at2759; -.
DR PhylomeDB; Q7M6Z4; -.
DR TreeFam; TF325946; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 75050; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Kif27; mouse.
DR PRO; PR:Q7M6Z4; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q7M6Z4; protein.
DR Bgee; ENSMUSG00000060176; Expressed in spermatid and 59 other tissues.
DR ExpressionAtlas; Q7M6Z4; baseline and differential.
DR Genevisible; Q7M6Z4; MM.
DR GO; GO:0005929; C:cilium; IDA: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; IDA:UniProtKB.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0021591; P:ventricular system development; IMP:MGI.
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 Alternative splicing; ATP-binding; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Motor protein; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1394
FT /note="Kinesin-like protein KIF27"
FT /id="PRO_0000307144"
FT DOMAIN 5..341
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 559..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1267..1319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1325..1344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 352..418
FT /evidence="ECO:0000255"
FT COILED 498..554
FT /evidence="ECO:0000255"
FT COILED 709..891
FT /evidence="ECO:0000255"
FT COILED 921..1078
FT /evidence="ECO:0000255"
FT COILED 1118..1152
FT /evidence="ECO:0000255"
FT COILED 1186..1226
FT /evidence="ECO:0000255"
FT COMPBIAS 642..661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1325..1339
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:0007744|PubMed:21183079"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7M6Z5"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7M6Z5"
FT MOD_RES 704
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7M6Z5"
FT MOD_RES 999
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7M6Z5"
FT MOD_RES 1365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7M6Z5"
FT MOD_RES 1387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7M6Z5"
FT VAR_SEQ 1..484
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028607"
FT VAR_SEQ 485..486
FT /note="YQ -> ML (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028608"
FT CONFLICT 1377
FT /note="G -> E (in Ref. 2; BAC28083)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1394 AA; 158956 MW; AC5F7CCD2CA61D6B CRC64;
MEEIPIKVAV RIRPLLCKEV LHNHQVCVRD IPNTQQIIIG RDRVFTFDFV FGKNSTQDEV
YNTCIKPLVL SLIEGYNATV FAYGQTGSGK TYTIGGGHVA SVVEGQKGII PRAIQEIFQS
ISENPSIDFK IKVSYIEVYK EDLRDLLELE TSMKDLHIRE DEKGNTVIVG AKECQVESVE
DVMSLLQVGN AARHTGTTQM NEHSSRSHAI FTISVCQVEK NAEAAENGEW YSHRHIVSKF
HFVDLAGSER VTKTGNTGER FKESIQINSG LLALGNVISA LGDPRRKSSH IPYRDAKITR
LLKDSLGGSA KTVMITCVSP SSSDFDESLN SLKYANRARN IRNKPALNIS PQADRMDEME
FEIKLLREAL QSHQASISQA SQASSENVPD QNRIHSLEEQ VAQLQEECLG YQDCIEQAFA
FLVDLKDAVK LNQKQQHKLQ EWFSRTQEVR KAVLTPLPGN QGIGNLEEGP QHLTVLQLKR
ELKKYQCALA ADQVVFTQKD LELEELRTQV QLMMQESKGH AVSLKEAQKV NRLQNEKIIE
QQLLVDQLSA ELAKRSLSVP TSAKESCGDG PDARASEKRP HTAPFESHWG HYVYIPSRQD
FKKVCSSTPV YSLDQVFAGF RTRSQMLMGH LEDQDEVLHC QFSDNSDDED SEGQEKPRVR
SRSHSWAKKP GSVCSLVELS DTQAESQRSY LGNGDLKMES LQESQEINLQ KLRTSELILN
KAKQKMRELT INIRMKEDLI KELIKTGNNA KSVSRQYSLK VTKLEHEAEQ AKVELTETRK
QLQELESKDL SDVALKVKLQ KEFRKKMDAA KMRVQVLQKK QQDSKKLASL SIQNEKRASE
LEHNVDHLKY QKVQLQRRLR EEGEKKKQLD AEIKRDQQKI KELQLKAGQG EGLNPKAEDQ
DGFNLNRRKS PFRSGDQFQK LDEQRKWLDE EVEKVLSQRQ ELEMLEEDLK KREAIVSKKE
ALLQEKSLLE NKKLRSSQAL STDGLKISAR LNLLDQELSE KSLQLESSPT EEKMKISEQV
QALQRERDQL QRQRNSVDER LKHGRVLSPK EEHLLFQLEE GIEALEAAIE FKNESIQSRQ
NSLKASFQNL SQSEANVLEK LVCLNITEIR AILFKYFNKV INLRETERKQ QLQNKEMKMK
VLERDNVVHE LESALEHLRL QCDRRLTLQQ KEHEQKMQLL LQHFKDQDGD SIIETLKNYE
DKIQQLEKDL YFYKKTSRDL KKRLKDPAQG AAQWQRTLTE HHDAGDGVLN PEETTVLSEE
LKWASRTENT KLNGSEREVD NSSSSLKTQP LTQQIPEDGP DSLPARSSIA PSSGQLQSIA
DKTEARPFTH SQSPVPHQFQ PVRSIGPLQG VKPVKLCRRE LRQISAMELS LRRCSLGAGG
RSMTADSLED PEEN
