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IFT27_MOUSE
ID   IFT27_MOUSE             Reviewed;         186 AA.
AC   Q9D0P8;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Intraflagellar transport protein 27 homolog;
DE   AltName: Full=Putative GTP-binding protein RAY-like;
DE   AltName: Full=Rab-like protein 4;
GN   Name=Ift27; Synonyms=Rabl4, Rayl;
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].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Retina;
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   [3]
RP   IDENTIFICATION IN THE IFT COMPLEX B, SUBCELLULAR LOCATION, AND INTERACTION
RP   WITH ITF88.
RX   PubMed=19253336; DOI=10.1002/cm.20346;
RA   Follit J.A., Xu F., Keady B.T., Pazour G.J.;
RT   "Characterization of mouse IFT complex B.";
RL   Cell Motil. Cytoskeleton 66:457-468(2009).
RN   [4]
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).
RN   [5]
RP   INTERACTION WITH RABL2, AND TISSUE SPECIFICITY.
RX   PubMed=23055941; DOI=10.1371/journal.pgen.1002969;
RA   Lo J.C., Jamsai D., O'Connor A.E., Borg C., Clark B.J., Whisstock J.C.,
RA   Field M.C., Adams V., Ishikawa T., Aitken R.J., Whittle B., Goodnow C.C.,
RA   Ormandy C.J., O'Bryan M.K.;
RT   "RAB-like 2 has an essential role in male fertility, sperm intra-flagellar
RT   transport, and tail assembly.";
RL   PLoS Genet. 8:E1002969-E1002969(2012).
RN   [6]
RP   INTERACTION WITH TTC30B.
RX   PubMed=23810713; DOI=10.1016/j.yexcr.2013.06.010;
RA   Howard P.W., Jue S.F., Maurer R.A.;
RT   "Interaction of mouse TTC30/DYF-1 with multiple intraflagellar transport
RT   complex B proteins and KIF17.";
RL   Exp. Cell Res. 319:2275-2281(2013).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=25446516; DOI=10.1016/j.devcel.2014.09.011;
RA   Eguether T., San Agustin G.T., Keady B.T., Jonassen J.A., Liang Y.,
RA   Francis R., Tobita K., Johnson C.A., Abdelhamed Z.A., Lo C.W., Pazour G.J.;
RT   "IFT27 links the BBSome to IFT for maintenance of the ciliary signaling
RT   compartment.";
RL   Dev. Cell 31:279-290(2014).
RN   [8]
RP   INTERACTION WITH HSPB11.
RX   PubMed=28430876; DOI=10.1093/biolre/iox029;
RA   Liu H., Li W., Zhang Y., Zhang Z., Shang X., Zhang L., Zhang S., Li Y.,
RA   Somoza A.V., Delpi B., Gerton G.L., Foster J.A., Hess R.A., Pazour G.J.,
RA   Zhang Z.;
RT   "IFT25, an intraflagellar transporter protein dispensable for ciliogenesis
RT   in somatic cells, is essential for sperm flagella formation.";
RL   Biol. Reprod. 96:993-1006(2017).
RN   [9]
RP   FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=28964737; DOI=10.1016/j.ydbio.2017.09.023;
RA   Zhang Y., Liu H., Li W., Zhang Z., Shang X., Zhang D., Li Y., Zhang S.,
RA   Liu J., Hess R.A., Pazour G.J., Zhang Z.;
RT   "Intraflagellar transporter protein (IFT27), an IFT25 binding partner, is
RT   essential for male fertility and spermiogenesis in mice.";
RL   Dev. Biol. 432:125-139(2017).
RN   [10]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=29626631; DOI=10.1016/j.mod.2018.04.001;
RA   Desai P.B., San Agustin J.T., Stuck M.W., Jonassen J.A., Bates C.M.,
RA   Pazour G.J.;
RT   "Ift25 is not a cystic kidney disease gene but is required for early steps
RT   of kidney development.";
RL   Mech. Dev. 151:10-17(2018).
CC   -!- FUNCTION: Small GTPase-like component of the intraflagellar transport
CC       (IFT) complex B that promotes the exit of the BBSome complex from cilia
CC       via its interaction with ARL6 (PubMed:25446516). Not involved in entry
CC       of the BBSome complex into cilium. Prevents aggregation of GTP-free
CC       ARL6. Required for hedgehog signaling (PubMed:25446516). Forms a
CC       subcomplex within the IFT complex B with IFT25 (By similarity). Its
CC       role in intraflagellar transport is mainly seen in tissues rich in
CC       ciliated cells such as kidney and testis. Essential for male fertility,
CC       spermiogenesis and sperm flagella formation (PubMed:28964737). Plays a
CC       role in the early development of the kidney (PubMed:29626631). May be
CC       involved in the regulation of ureteric bud initiation
CC       (PubMed:29626631). {ECO:0000250|UniProtKB:A8HN58,
CC       ECO:0000269|PubMed:25446516, ECO:0000269|PubMed:28964737,
CC       ECO:0000269|PubMed:29626631}.
CC   -!- SUBUNIT: Component of the IFT complex B, at least composed of IFT20,
CC       IFT22, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74,
CC       IFT80, IFT81, and IFT88 (PubMed:19253336). Interacts with HSPB11/IFT25
CC       (PubMed:28430876). Interacts with TTC30B (PubMed:23810713). Interacts
CC       with RABL2/RABL2A; binding is equal in the presence of GTP or GDP
CC       (PubMed:23055941). Interacts with IFT88 (PubMed:19253336). Interacts
CC       with ARL6; recognizes and binds with the GTP-free form of ARL6 (By
CC       similarity). {ECO:0000250|UniProtKB:Q9BW83,
CC       ECO:0000269|PubMed:19253336, ECO:0000269|PubMed:23055941,
CC       ECO:0000269|PubMed:23810713, ECO:0000269|PubMed:28430876}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC       {ECO:0000269|PubMed:19253336}. Cytoplasm {ECO:0000269|PubMed:28964737}.
CC       Cell projection, cilium, flagellum {ECO:0000269|PubMed:28964737}.
CC       Note=Localizes to the sperm flagellum. {ECO:0000269|PubMed:28964737}.
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in the testis (at protein
CC       level) (PubMed:28964737). Co-localizes with RABL2/RABL2A in the
CC       midpiece of elongated spermatids within the testis (at protein level).
CC       {ECO:0000269|PubMed:23055941, ECO:0000269|PubMed:28964737}.
CC   -!- DISRUPTION PHENOTYPE: Null mutants retain the ability to ciliate and
CC       survive through gestation. They die shortly after birth due to
CC       different phenotypes reminiscent of Shh signaling defects: polydactyly,
CC       lung isomerisms, and structural heart defects (PubMed:25446516).
CC       Conditional knockout in male germ cells results in infertility,
CC       abnormal sperm morphology, significantly reduced sperm count and sperm
CC       mobility (PubMed:28964737). Mutant mice with germline deletion of IFT27
CC       die shortly after birth with structural defects in most organs
CC       including the kidneys, where duplicated collecting duct system and/or
CC       duplex kidney is often observed. Conditional deletion in the collecting
CC       duct results in smaller kidneys that develop only mild tubule dilation
CC       with age whereas conditional deletion from the peri-Wolffian duct
CC       stroma results in duplex kidneys (PubMed:29626631).
CC       {ECO:0000269|PubMed:25446516, ECO:0000269|PubMed:28964737,
CC       ECO:0000269|PubMed:29626631}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; AK011196; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC017514; AAH17514.1; -; mRNA.
DR   CCDS; CCDS37131.1; -.
DR   RefSeq; NP_080207.1; NM_025931.2.
DR   AlphaFoldDB; Q9D0P8; -.
DR   SMR; Q9D0P8; -.
DR   BioGRID; 211896; 3.
DR   ComplexPortal; CPX-5028; IFT-B complex.
DR   IntAct; Q9D0P8; 7.
DR   STRING; 10090.ENSMUSP00000016781; -.
DR   iPTMnet; Q9D0P8; -.
DR   PhosphoSitePlus; Q9D0P8; -.
DR   EPD; Q9D0P8; -.
DR   MaxQB; Q9D0P8; -.
DR   PaxDb; Q9D0P8; -.
DR   PeptideAtlas; Q9D0P8; -.
DR   PRIDE; Q9D0P8; -.
DR   ProteomicsDB; 266956; -.
DR   Antibodypedia; 11783; 125 antibodies from 23 providers.
DR   DNASU; 67042; -.
DR   Ensembl; ENSMUST00000016781; ENSMUSP00000016781; ENSMUSG00000016637.
DR   GeneID; 67042; -.
DR   KEGG; mmu:67042; -.
DR   UCSC; uc007wor.1; mouse.
DR   CTD; 11020; -.
DR   MGI; MGI:1914292; Ift27.
DR   VEuPathDB; HostDB:ENSMUSG00000016637; -.
DR   eggNOG; KOG0079; Eukaryota.
DR   GeneTree; ENSGT00870000136549; -.
DR   HOGENOM; CLU_041217_10_6_1; -.
DR   InParanoid; Q9D0P8; -.
DR   OMA; EMSVKEM; -.
DR   OrthoDB; 1585129at2759; -.
DR   PhylomeDB; Q9D0P8; -.
DR   TreeFam; TF329292; -.
DR   Reactome; R-MMU-5620924; Intraflagellar transport.
DR   BioGRID-ORCS; 67042; 4 hits in 73 CRISPR screens.
DR   ChiTaRS; Ift27; mouse.
DR   PRO; PR:Q9D0P8; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q9D0P8; protein.
DR   Bgee; ENSMUSG00000016637; Expressed in urogenital fold and 251 other tissues.
DR   ExpressionAtlas; Q9D0P8; baseline and differential.
DR   Genevisible; Q9D0P8; MM.
DR   GO; GO:0005813; C:centrosome; IDA:MGI.
DR   GO; GO:0005929; C:cilium; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR   GO; GO:0030992; C:intraciliary transport particle B; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
DR   GO; GO:0097225; C:sperm midpiece; IDA:MGI.
DR   GO; GO:0097228; C:sperm principal piece; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0060271; P:cilium assembly; IC:ComplexPortal.
DR   GO; GO:0090102; P:cochlea development; IMP:MGI.
DR   GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IMP:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
DR   GO; GO:0035720; P:intraciliary anterograde transport; IC:ComplexPortal.
DR   GO; GO:0042073; P:intraciliary transport; IMP:UniProtKB.
DR   GO; GO:0001822; P:kidney development; IMP:UniProtKB.
DR   GO; GO:0007224; P:smoothened signaling pathway; IMP:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cilium; Cytoplasm; Differentiation; Flagellum;
KW   GTP-binding; Nucleotide-binding; Protein transport; Reference proteome;
KW   Spermatogenesis; Transport.
FT   CHAIN           1..186
FT                   /note="Intraflagellar transport protein 27 homolog"
FT                   /id="PRO_0000082716"
FT   BINDING         12..19
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         64..68
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         123..126
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   186 AA;  20814 MW;  1CFC788EF5592C51 CRC64;
     MVKLAAKCIL AGDPAVGKTA LVQMFRSDGT HFQKNYTLTT GVDLVVKTVP VLDTNDSVEL
     FIFDSAGKEL FSEMLDKLWE NPNVLCLVYD VTNEQSFISC TKWLEKVRSQ TSGISLPGVL
     VGTKTDLAGR QTVDSAQAQV WALSQGLEFF ETSVKEMDNY EAPFHCLAKQ FYQLYREKVD
     IFHTLV
 
 
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