PHTF1_MOUSE
ID PHTF1_MOUSE Reviewed; 761 AA.
AC Q9QZ09; Q9CS51; Q9CSB9; Q9QZ14;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Protein PHTF1 {ECO:0000305};
GN Name=Phtf1 {ECO:0000312|MGI:MGI:1332671};
GN Synonyms=Phtf {ECO:0000303|PubMed:10729229};
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], AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=10729229; DOI=10.1006/geno.1999.6079;
RA Manuel A., Beaupain D., Romeo P.-H., Raich N.;
RT "Molecular characterization of a novel gene family (PHTF) conserved from
RT Drosophila to mammals.";
RL Genomics 64:216-220(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-685.
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 [3]
RP INTERACTION WITH FEM1B.
RX PubMed=15601915; DOI=10.1095/biolreprod.104.035964;
RA Oyhenart J., Benichou S., Raich N.;
RT "Putative homeodomain transcription factor 1 interacts with the
RT feminization factor homolog fem1b in male germ cells.";
RL Biol. Reprod. 72:780-787(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272; SER-276; SER-277;
RP SER-333 AND SER-335, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 -!- SUBUNIT: Interacts with FEM1B. {ECO:0000269|PubMed:15601915}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:F1M8G0}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000250|UniProtKB:F1M8G0}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in testis.
CC {ECO:0000269|PubMed:10729229}.
CC -!- CAUTION: The PHTF domain was initially defined as an atypical
CC homeodomain, suggesting that this protein could act as a transcription
CC regulator (By similarity). However, the protein is not found in the
CC nucleus and mainly localizes in the endoplasmic reticulum membrane,
CC suggesting that it does not act as a transcription factor (By
CC similarity). {ECO:0000250|UniProtKB:F1M8G0,
CC ECO:0000250|UniProtKB:Q9UMS5}.
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DR EMBL; AJ242864; CAB62242.1; -; mRNA.
DR EMBL; AJ133721; CAB62241.1; -; mRNA.
DR EMBL; AK019146; BAB31567.1; -; mRNA.
DR EMBL; AK013292; BAB28772.2; ALT_SEQ; mRNA.
DR CCDS; CCDS17698.1; -.
DR RefSeq; NP_001156939.1; NM_001163467.1.
DR RefSeq; NP_001156940.1; NM_001163468.1.
DR RefSeq; NP_001156941.1; NM_001163469.1.
DR RefSeq; NP_038657.2; NM_013629.2.
DR AlphaFoldDB; Q9QZ09; -.
DR BioGRID; 202147; 2.
DR IntAct; Q9QZ09; 1.
DR STRING; 10090.ENSMUSP00000066607; -.
DR GlyGen; Q9QZ09; 6 sites.
DR iPTMnet; Q9QZ09; -.
DR PhosphoSitePlus; Q9QZ09; -.
DR PaxDb; Q9QZ09; -.
DR PRIDE; Q9QZ09; -.
DR ProteomicsDB; 289554; -.
DR Antibodypedia; 20143; 28 antibodies from 12 providers.
DR DNASU; 18685; -.
DR Ensembl; ENSMUST00000063717; ENSMUSP00000066607; ENSMUSG00000058388.
DR Ensembl; ENSMUST00000117150; ENSMUSP00000113973; ENSMUSG00000058388.
DR Ensembl; ENSMUST00000145727; ENSMUSP00000114722; ENSMUSG00000058388.
DR GeneID; 18685; -.
DR KEGG; mmu:18685; -.
DR UCSC; uc008qtz.1; mouse.
DR CTD; 10745; -.
DR MGI; MGI:1332671; Phtf1.
DR VEuPathDB; HostDB:ENSMUSG00000058388; -.
DR eggNOG; ENOG502QQGQ; Eukaryota.
DR GeneTree; ENSGT00390000011648; -.
DR InParanoid; Q9QZ09; -.
DR OMA; LYFMIPV; -.
DR OrthoDB; 710715at2759; -.
DR PhylomeDB; Q9QZ09; -.
DR TreeFam; TF323570; -.
DR BioGRID-ORCS; 18685; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Phtf1; mouse.
DR PRO; PR:Q9QZ09; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9QZ09; protein.
DR Bgee; ENSMUSG00000058388; Expressed in spermatocyte and 259 other tissues.
DR ExpressionAtlas; Q9QZ09; baseline and differential.
DR Genevisible; Q9QZ09; MM.
DR GO; GO:0005801; C:cis-Golgi network; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR039775; PHTF1/2.
DR InterPro; IPR021980; PHTF1/2_N.
DR PANTHER; PTHR12680; PTHR12680; 1.
DR Pfam; PF12129; Phtf-FEM1B_bdg; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..761
FT /note="Protein PHTF1"
FT /id="PRO_0000127424"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 514..534
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 610..630
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 644..664
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 736..756
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 6..150
FT /note="PHTF"
FT /evidence="ECO:0000255"
FT REGION 152..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 673
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 732
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 156
FT /note="N -> T (in Ref. 1; CAB62242)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="R -> G (in Ref. 2; BAB31567)"
FT /evidence="ECO:0000305"
FT CONFLICT 657..658
FT /note="LL -> FV (in Ref. 2; BAB31567)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 761 AA; 86779 MW; BBDA5E1492B85C41 CRC64;
MASNERDAIS WYQKKIGAYD QQIWEKSIEQ TQIKGFKNKP KKMGHIKPDL IDVDLIRGST
FAKAKPEIPW TSLTRKGLVR VVFFPLFSSW WIQVTSLRIF VWLLLLYLMQ VTAVVLYLLM
PIVSASEVLG PLCLMLLMGT VHCQIVSTQI TRPSGNNGNR RRRKLRKTVN GDGSRDNGNN
SPDKVRAVET LESASSVGGF WGTLFGNRIK RVKLVSNKGT ETDNDSGCFH PILKKRQGRP
EIRMWQAREK AKVSDGEKCR REAYRRLGNG ISDDLSSEED GEARTQMILL RRSVEGASSD
NGYEVKNRRS ILSRHLNSQV KKTTRWCHIV RDSDSLAESE FESAVFSQGS RSGMSGGSRS
LNLSRRDSES TRHDSETEDM LWDDLLHGPE CRSSVTSDSE GAHVNTIHSG TKRDPKEDVF
QQNHLFWLQN SSPASERVSA IIWEGNECKK MDMSVLEISG IIMSRVNAYE QGVGYQMLGN
AVTVGLALFP FLYRLFREKS FDQLKSISAE EVLTLFCGAP PVTPVVILSI INFIERLCLT
WMFFFMMCVA ERTYKQRFLF AKLFSHITSA RKARKYEIPH FRLKKVENIK IWLSLRSYLK
RRGPQRSVDV VVSSVFLLTL SIAFICCAQV LQGHKTFLND AYNWEFLIWE TALLLFLLRL
ASLGSETNKK YSNVSILLTE QINLYLKMEK KPNKKEQLTL VNNVLKLSTK LLKELDTPFR
LYGLTMNPLI YNITRVVILS AVSGVISDLL GFNIRLWKIK S
