PIFO_HUMAN
ID PIFO_HUMAN Reviewed; 191 AA.
AC Q8TCI5; D9J0A2; D9J0A3; Q4G0K4; Q52LJ6; Q5T5D5; Q5T5D6; Q8N310;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein pitchfork;
GN Name=PIFO; Synonyms=C1orf88;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ARL13B;
RP AURKA; CETN1; KIF3A; RAB6A; RAB8A; TUBB1 AND TUBG1, AND VARIANTS LYS-80 AND
RP ASN-105.
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] (ISOFORMS 1 AND 3).
RC TISSUE=Lung;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ASN-105.
RC TISSUE=Brain, Lung, and 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: Cytoplasmic vesicle {ECO:0000250}. Golgi
CC apparatus, trans-Golgi network {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Accumulates specifically at the basal body and ciliary necklace
CC during the early steps of cilia assembly and disassembly, when
CC structural, functional and regulatory proteins are delivered to cilia.
CC At S phase, accumulates in vesicles and declines during mitosis.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8TCI5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TCI5-2; Sequence=VSP_024557;
CC Name=3;
CC IsoId=Q8TCI5-3; Sequence=VSP_042040;
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DR EMBL; HM237139; ADI86276.1; -; mRNA.
DR EMBL; HM237140; ADI86277.1; -; mRNA.
DR EMBL; AK074433; BAB85081.1; -; mRNA.
DR EMBL; AK303897; BAG64829.1; -; mRNA.
DR EMBL; AL356387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029237; AAH29237.1; -; mRNA.
DR EMBL; BC050319; AAH50319.1; -; mRNA.
DR EMBL; BC093891; AAH93891.1; -; mRNA.
DR EMBL; BC101501; AAI01502.1; -; mRNA.
DR CCDS; CCDS72836.1; -. [Q8TCI5-3]
DR CCDS; CCDS833.1; -. [Q8TCI5-1]
DR RefSeq; NP_001287760.1; NM_001300831.1. [Q8TCI5-3]
DR RefSeq; NP_857594.2; NM_181643.5. [Q8TCI5-1]
DR AlphaFoldDB; Q8TCI5; -.
DR BioGRID; 126109; 20.
DR IntAct; Q8TCI5; 7.
DR STRING; 9606.ENSP00000358753; -.
DR iPTMnet; Q8TCI5; -.
DR PhosphoSitePlus; Q8TCI5; -.
DR BioMuta; PIFO; -.
DR DMDM; 145558868; -.
DR jPOST; Q8TCI5; -.
DR MassIVE; Q8TCI5; -.
DR PaxDb; Q8TCI5; -.
DR PeptideAtlas; Q8TCI5; -.
DR PRIDE; Q8TCI5; -.
DR ProteomicsDB; 74140; -. [Q8TCI5-1]
DR ProteomicsDB; 74141; -. [Q8TCI5-2]
DR ProteomicsDB; 74142; -. [Q8TCI5-3]
DR Antibodypedia; 53752; 4 antibodies from 4 providers.
DR DNASU; 128344; -.
DR Ensembl; ENST00000369737.4; ENSP00000358752.4; ENSG00000173947.14. [Q8TCI5-3]
DR Ensembl; ENST00000369738.9; ENSP00000358753.4; ENSG00000173947.14. [Q8TCI5-1]
DR GeneID; 128344; -.
DR KEGG; hsa:128344; -.
DR MANE-Select; ENST00000369738.9; ENSP00000358753.4; NM_181643.6; NP_857594.2.
DR UCSC; uc001eaw.3; human. [Q8TCI5-1]
DR CTD; 128344; -.
DR DisGeNET; 128344; -.
DR GeneCards; PIFO; -.
DR HGNC; HGNC:27009; PIFO.
DR HPA; ENSG00000173947; Tissue enriched (fallopian).
DR MIM; 614234; gene.
DR neXtProt; NX_Q8TCI5; -.
DR OpenTargets; ENSG00000173947; -.
DR PharmGKB; PA142672472; -.
DR VEuPathDB; HostDB:ENSG00000173947; -.
DR eggNOG; ENOG502RZWF; Eukaryota.
DR GeneTree; ENSGT00390000001017; -.
DR HOGENOM; CLU_098763_0_0_1; -.
DR InParanoid; Q8TCI5; -.
DR OMA; QKEMTPH; -.
DR OrthoDB; 1094638at2759; -.
DR PhylomeDB; Q8TCI5; -.
DR TreeFam; TF328853; -.
DR PathwayCommons; Q8TCI5; -.
DR SignaLink; Q8TCI5; -.
DR BioGRID-ORCS; 128344; 45 hits in 1073 CRISPR screens.
DR GenomeRNAi; 128344; -.
DR Pharos; Q8TCI5; Tbio.
DR PRO; PR:Q8TCI5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8TCI5; protein.
DR Bgee; ENSG00000173947; Expressed in bronchial epithelial cell and 125 other tissues.
DR Genevisible; Q8TCI5; HS.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005802; C:trans-Golgi network; ISS: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; IEA:Ensembl.
DR GO; GO:0060971; P:embryonic heart tube left/right pattern formation; IEA:Ensembl.
DR GO; GO:0033674; P:positive regulation of kinase activity; IMP:UniProtKB.
DR GO; GO:0031344; P:regulation of cell projection organization; ISS:UniProtKB.
DR InterPro; IPR033602; Pitchfork.
DR PANTHER; PTHR31508; PTHR31508; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoplasmic vesicle; Golgi apparatus; Reference proteome.
FT CHAIN 1..191
FT /note="Protein pitchfork"
FT /id="PRO_0000284526"
FT VAR_SEQ 54..86
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042040"
FT VAR_SEQ 130..191
FT /note="SPGAYNPEKKPPPKIAWPMKFGSPDWAQVPCLQKRTLKAELSTDKDFRKHRN
FT RVAYLSLYYN -> RYVSSLLVHFNKKSNRRKRST (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024557"
FT VARIANT 80
FT /note="R -> K (found in patients with severe ciliopathies
FT and left-right asymmetry defects; inhibits AURKA activity;
FT dbSNP:rs150508940)"
FT /evidence="ECO:0000269|PubMed:20643351"
FT /id="VAR_066484"
FT VARIANT 97
FT /note="K -> N (in dbSNP:rs15396)"
FT /id="VAR_031767"
FT VARIANT 105
FT /note="H -> N (in dbSNP:rs2184884)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:20643351"
FT /id="VAR_031768"
FT CONFLICT 63
FT /note="K -> R (in Ref. 2; BAB85081)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="N -> D (in Ref. 4; AAH50319)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 191 AA; 21973 MW; CEEDE39D1F7381C5 CRC64;
MCFSRADAAD NYPFGTCQQR KLFPHFHPPN LIGNKFVPLR GSPHRGPGCY FSDGYGLAYD
LSKIPTSIKG YTLGARTAVR FKPIQKEMTP HAGRYQKVSP QQEKHKQNFA PFNVLVPRFK
NYPKDTYYPS PGAYNPEKKP PPKIAWPMKF GSPDWAQVPC LQKRTLKAEL STDKDFRKHR
NRVAYLSLYY N
