PIFO_MOUSE
ID PIFO_MOUSE Reviewed; 207 AA.
AC Q9D9W1; D9J0A0; D9J0A1; Q810M7;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein pitchfork;
GN Name=Pifo;
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 [MRNA] (ISOFORMS 1 AND 2), FUNCTION, ALTERNATIVE
RP PROMOTER USAGE, INTERACTION WITH ARL13B; AURKA; CETN1; KIF3A; RAB6A; RAB8A;
RP TUBB1 AND TUBG1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=20643351; DOI=10.1016/j.devcel.2010.06.005;
RA Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B.,
RA Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.;
RT "Pitchfork regulates primary cilia disassembly and left-right asymmetry.";
RL Dev. Cell 19:66-77(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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).
CC -!- FUNCTION: During primary cilia disassembly, involved in cilia
CC disassembly. Required specifically to control cilia retraction as well
CC as the liberation and duplication of the basal body/centrosome. May act
CC by stimulating AURKA activity at the basal body in a cell cycle-
CC dependent manner. {ECO:0000269|PubMed:20643351}.
CC -!- SUBUNIT: Interacts with proteins involved in ciliary transport,
CC including ARL13B, CETN1, KIF3A, RAB6A, RAB8A, TUBB1 and TUBG1.
CC Interacts with AURKA. {ECO:0000269|PubMed:20643351}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Golgi apparatus, Golgi stack. Golgi
CC apparatus, trans-Golgi network.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20643351}.
CC Cytoplasmic vesicle {ECO:0000269|PubMed:20643351}. Note=Accumulates
CC specifically at the basal body and ciliary necklace during the early
CC steps of cilia assembly and disassembly, when structural, functional
CC and regulatory proteins are delivered to cilia. At S phase, accumulates
CC in vesicles and declines during mitosis. In node pit cells, found close
CC to the ciliary membrane along the axoneme. In spermatocytes, localizes
CC to particles along the stabilized microtubules of tails.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D9W1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D9W1-2; Sequence=VSP_024558;
CC -!- TISSUE SPECIFICITY: Expressed in tissues rich in ciliated cells, such
CC as lung, kidney, vas deferens and testis. Both isoforms 1 and 2 are
CC expressed in testis. {ECO:0000269|PubMed:20643351}.
CC -!- DEVELOPMENTAL STAGE: At 7.75 dpc, expression restricted to the ventral
CC node monociliated pit cells. Not expressed in other tissues at
CC detectable levels until 9.5 dpc. At 10.5 dpc, expressed in motor
CC neurons in the ventral neural tube and in the apical ectodermal ridge
CC of lim buds. {ECO:0000269|PubMed:20643351}.
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DR EMBL; HM237137; ADI86274.1; -; mRNA.
DR EMBL; HM237138; ADI86275.1; -; mRNA.
DR EMBL; AK006407; BAB24572.1; -; mRNA.
DR EMBL; CH466608; EDL07534.1; -; Genomic_DNA.
DR EMBL; BC049757; AAH49757.1; -; mRNA.
DR CCDS; CCDS51037.1; -. [Q9D9W1-1]
DR CCDS; CCDS51038.1; -. [Q9D9W1-2]
DR RefSeq; NP_001186957.1; NM_001200028.1. [Q9D9W1-2]
DR RefSeq; NP_083880.2; NM_029604.3. [Q9D9W1-1]
DR AlphaFoldDB; Q9D9W1; -.
DR STRING; 10090.ENSMUSP00000010280; -.
DR iPTMnet; Q9D9W1; -.
DR PhosphoSitePlus; Q9D9W1; -.
DR PaxDb; Q9D9W1; -.
DR PRIDE; Q9D9W1; -.
DR ProteomicsDB; 289572; -. [Q9D9W1-1]
DR ProteomicsDB; 289573; -. [Q9D9W1-2]
DR Antibodypedia; 53752; 4 antibodies from 4 providers.
DR Ensembl; ENSMUST00000010280; ENSMUSP00000010280; ENSMUSG00000010136. [Q9D9W1-2]
DR Ensembl; ENSMUST00000066319; ENSMUSP00000069454; ENSMUSG00000010136. [Q9D9W1-1]
DR GeneID; 100503311; -.
DR KEGG; mmu:100503311; -.
DR UCSC; uc008qvr.1; mouse. [Q9D9W1-1]
DR UCSC; uc008qvs.1; mouse. [Q9D9W1-2]
DR CTD; 128344; -.
DR MGI; MGI:1923670; Pifo.
DR VEuPathDB; HostDB:ENSMUSG00000010136; -.
DR eggNOG; ENOG502RZWF; Eukaryota.
DR GeneTree; ENSGT00390000001017; -.
DR HOGENOM; CLU_098763_0_0_1; -.
DR InParanoid; Q9D9W1; -.
DR OMA; QKEMTPH; -.
DR OrthoDB; 1094638at2759; -.
DR TreeFam; TF328853; -.
DR BioGRID-ORCS; 100503311; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Pifo; mouse.
DR PRO; PR:Q9D9W1; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9D9W1; protein.
DR Bgee; ENSMUSG00000010136; Expressed in olfactory epithelium and 54 other tissues.
DR Genevisible; Q9D9W1; MM.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
DR GO; GO:0008092; F:cytoskeletal protein binding; IBA:GO_Central.
DR GO; GO:0043015; F:gamma-tubulin binding; IDA:UniProtKB.
DR GO; GO:0019894; F:kinesin binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0044782; P:cilium organization; IMP:MGI.
DR GO; GO:0060971; P:embryonic heart tube left/right pattern formation; IMP:MGI.
DR GO; GO:0033674; P:positive regulation of kinase activity; ISS:UniProtKB.
DR GO; GO:0031344; P:regulation of cell projection organization; IMP:UniProtKB.
DR InterPro; IPR033602; Pitchfork.
DR InterPro; IPR010736; SHIPPO-rpt.
DR PANTHER; PTHR31508; PTHR31508; 1.
DR Pfam; PF07004; SHIPPO-rpt; 1.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoplasmic vesicle; Golgi apparatus; Nucleus; Reference proteome.
FT CHAIN 1..207
FT /note="Protein pitchfork"
FT /id="PRO_0000284527"
FT VAR_SEQ 1..21
FT /note="MNTEEIPVAPPLRGVTPALQW -> MKTENEEDVKPPESCHAMQLLFKSLEA
FT SERAKVEEELKKTKENEFTQRNEHHALRDITHG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:20643351"
FT /id="VSP_024558"
SQ SEQUENCE 207 AA; 23434 MW; D564D3A08833DCA7 CRC64;
MNTEEIPVAP PLRGVTPALQ WKVNNYSFGT RQARKLFPHY HPPTWLGNLY LPLRGMPHTG
PGCYAAATDW NGLAYNLSKV PTSTKGYAIG ARTAVRFKPI SKDVTPYPGM YQKVDTLSEK
HKKSFAPFNI LMPRFRSAAK GDSYPGPGTY NPEMKSVPKV TWPMKFGSPD WSQVPCLEKR
TLKAELSADK DFRKHRSRVA YFSLYYQ
