PHTF1_RAT
ID PHTF1_RAT Reviewed; 762 AA.
AC F1M8G0;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Protein PHTF1 {ECO:0000305};
GN Name=Phtf1 {ECO:0000303|PubMed:12604659, ECO:0000312|RGD:620426};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12604659; DOI=10.1095/biolreprod.102.009787;
RA Oyhenart J., Le Goffic R., Samson M., Jegou B., Raich N.;
RT "Phtf1 is an integral membrane protein localized in an endoplasmic
RT reticulum domain in maturing male germ cells.";
RL Biol. Reprod. 68:1044-1053(2003).
CC -!- SUBUNIT: Interacts with FEM1B. {ECO:0000250|UniProtKB:Q9QZ09}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12604659}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000269|PubMed:12604659}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis.
CC {ECO:0000269|PubMed:12604659}.
CC -!- DEVELOPMENTAL STAGE: The protein first appears in meiotic spermatocytes
CC and becomes abundant in spermatids around stage III-IV (at protein
CC level). {ECO:0000269|PubMed:12604659}.
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
CC (PubMed:12604659). {ECO:0000250|UniProtKB:Q9UMS5,
CC ECO:0000269|PubMed:12604659}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AABR07012761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001178031.1; NM_001191102.1.
DR RefSeq; XP_006233123.1; XM_006233061.3.
DR AlphaFoldDB; F1M8G0; -.
DR SMR; F1M8G0; -.
DR STRING; 10116.ENSRNOP00000026863; -.
DR GlyGen; F1M8G0; 6 sites.
DR iPTMnet; F1M8G0; -.
DR PhosphoSitePlus; F1M8G0; -.
DR PaxDb; F1M8G0; -.
DR Ensembl; ENSRNOT00000026863; ENSRNOP00000026863; ENSRNOG00000019785.
DR GeneID; 252962; -.
DR KEGG; rno:252962; -.
DR CTD; 10745; -.
DR RGD; 620426; Phtf1.
DR eggNOG; ENOG502QQGQ; Eukaryota.
DR GeneTree; ENSGT00390000011648; -.
DR HOGENOM; CLU_013937_0_0_1; -.
DR InParanoid; F1M8G0; -.
DR OMA; LYFMIPV; -.
DR OrthoDB; 710715at2759; -.
DR TreeFam; TF323570; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000019785; Expressed in testis and 20 other tissues.
DR Genevisible; F1M8G0; RN.
DR GO; GO:0005801; C:cis-Golgi network; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR GO; GO:0007283; P:spermatogenesis; NAS:RGD.
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..762
FT /note="Protein PHTF1"
FT /id="PRO_0000451603"
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 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 611..631
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 645..665
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 737..757
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..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZ09"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZ09"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZ09"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZ09"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZ09"
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 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 674
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 733
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 762 AA; 86835 MW; DDAE49E75A0F3E96 CRC64;
MASNERDAIS WYQKKIGAYD QQIWEKSIEQ TQIKGFKNKP KKMGHIKPDL IDVDLIRGST
FAKAKPEIPW TSLTRKGLVR VVFFPLFSSW WIQVTSLRIF VWLLLLYLMQ VTAIVLYLMM
PIVSVSEVLG PLCLMLLMGT VHCQIVSTQI TRPSGNNGNR RRRKLRKTVN GDGTRDNGNN
SPDKIRAVET LDSAPSVGGF WGTLFGNRIK RVKLVSNKGT ETDNDSGCFH PIIKKRQGRP
EIRMWQAREK AKVSDGEKCR REAYRRLGNG VSDDLSSEED GEARTQMILL RRSVEGASSD
NGCEVKNRKS ILSRHLNSQV KKTATRWCHI VRDSDSLAES EFESAAFSQG SRSGMSGGSR
SLNLSRRDSE STRHDSETED MLWDDLLHGP ECRSSVTSDS EGAHVNTLHS GTKRDPKEDV
FQQNHLFWLQ NSSPASERVS AIIWEGNECK KMDMSVLEIS GIIMSRVNAY EQGVGYQMLG
NAVTIGLALF PFLYRLFREK SFDQLKSISA EEVLTLFCGA PPVTPVVILS IINFFERLCL
TWIFFFMMCV AERTYKQRFL FAKLFSHITS ARKARKYEIP HFRLKKVENI KIWLSLRSYL
KRRGPQRSVD VVVSSVFLLT LSIAFICCAQ VLQGHKTFLN DAYNWEFLIW ETALLLFLLR
LASLGSETNK KYSNVSILLT EQINLYLKME KKPNKKEQLT LVNNVLKLST KLLKELDTPF
RLYGLTMNPL IYNITRVVIL SAVSGVISDL LGFNIRLWKI KS
