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   27-MAR-2024, entry version 145.
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.
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.ENSMUSP00000153598; -.
DR   iPTMnet; Q7M6Z4; -.
DR   PhosphoSitePlus; Q7M6Z4; -.
DR   EPD; Q7M6Z4; -.
DR   MaxQB; Q7M6Z4; -.
DR   PaxDb; 10090-ENSMUSP00000043304; -.
DR   PeptideAtlas; Q7M6Z4; -.
DR   ProteomicsDB; 269302; -. [Q7M6Z4-1]
DR   ProteomicsDB; 269303; -. [Q7M6Z4-2]
DR   Antibodypedia; 13061; 71 antibodies from 15 providers.
DR   DNASU; 75050; -.
DR   Ensembl; ENSMUST00000043605.6; ENSMUSP00000043304.6; ENSMUSG00000060176.5. [Q7M6Z4-1]
DR   Ensembl; ENSMUST00000225388.2; ENSMUSP00000153598.2; ENSMUSG00000060176.5. [Q7M6Z4-1]
DR   GeneID; 75050; -.
DR   KEGG; mmu:75050; -.
DR   UCSC; uc007qtq.1; mouse. [Q7M6Z4-1]
DR   UCSC; uc011zao.1; mouse. [Q7M6Z4-2]
DR   AGR; MGI:1922300; -.
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; YVIMNTF; -.
DR   OrthoDB; 5395177at2759; -.
DR   PhylomeDB; Q7M6Z4; -.
DR   TreeFam; TF325946; -.
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 77 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 61 other cell types or tissues.
DR   ExpressionAtlas; Q7M6Z4; baseline and differential.
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   CDD; cd01372; KISc_KIF4; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
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   PANTHER; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR   PANTHER; PTHR47969:SF22; KINESIN FAMILY MEMBER 27; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   Genevisible; Q7M6Z4; MM.
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
//