PHTF1_BOVIN
ID PHTF1_BOVIN Reviewed; 762 AA.
AC Q08DA4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Protein PHTF1 {ECO:0000305};
GN Name=PHTF1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Interacts with FEM1B. {ECO:0000250|UniProtKB:Q9QZ09}.
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 -!- 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; BC123860; AAI23861.1; -; mRNA.
DR RefSeq; NP_001069545.1; NM_001076077.1.
DR RefSeq; XP_010801515.1; XM_010803213.2.
DR RefSeq; XP_015319306.1; XM_015463820.1.
DR RefSeq; XP_015319309.1; XM_015463823.1.
DR RefSeq; XP_015319317.1; XM_015463831.1.
DR AlphaFoldDB; Q08DA4; -.
DR STRING; 9913.ENSBTAP00000026132; -.
DR PaxDb; Q08DA4; -.
DR PRIDE; Q08DA4; -.
DR Ensembl; ENSBTAT00000026132; ENSBTAP00000026132; ENSBTAG00000019615.
DR GeneID; 536504; -.
DR KEGG; bta:536504; -.
DR CTD; 10745; -.
DR VEuPathDB; HostDB:ENSBTAG00000019615; -.
DR VGNC; VGNC:32848; PHTF1.
DR eggNOG; ENOG502QQGQ; Eukaryota.
DR GeneTree; ENSGT00390000011648; -.
DR HOGENOM; CLU_013937_0_0_1; -.
DR InParanoid; Q08DA4; -.
DR OMA; LYFMIPV; -.
DR OrthoDB; 710715at2759; -.
DR TreeFam; TF323570; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000019615; Expressed in spermatid and 108 other tissues.
DR ExpressionAtlas; Q08DA4; baseline.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; 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 2: Evidence at transcript 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_0000318508"
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 512..532
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..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..365
FT /note="Polar 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 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
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; 87159 MW; F0C228BBD2F2D093 CRC64;
MASNERDAIS WYQKKIGAYD QQIWEKSIEQ TQIKGFKNKP KKMGHIKADL IDVDLIRGST
FAKAKPEIPW TSLTRKGLVR VVFFPLFSSW WIQVTSLRIF VWLLLLYLMQ VIALVLYFMM
PIVNVSEVLG PLCLMLLMGT VHCQIVSTQI TRPSGNNGNR RRRKLRKTVN GDGSRENGNN
SSDKARGVET LESAPLNGSF WRTLFGNRMK RVKLICNRGT ETDYDSGCLH PIIKKRQCRP
EIRMWQTREK AKFSDGEKGR RESFRRLGNG ISDDLSSDDD GEAQTQMMIL RRSVEGASSD
NGCEIKSRKS ILSRHLNTQV KKTTSKWCSV VRDSDSLAES EFESAAFSQG SRSGMSGGSR
SLNMLRRDSE STRHDSETED MLWDDLLHGP ECRSSVTSDS EGAHVSSLHS GTKRDPKEDV
FQQNHLFWLQ NSSPASDRVS AIIWEGNECK KMDMSVLEIS GIIMSRVNAY QQGVGYQMLG
NIVTIGLAFF PFLHRLFREK NLDQLKSISA EEILTLFCGA PPVTPIIILS IINFFERLCL
TWMFFFMMCV AERTYKQRFL FAKLFSHITS ARKARKYEIP HFRLKKVENI KIWLSLRSFL
KRRGPQRSVD VVVSSVFLLT LSIAFICCAQ VLRGHKTFLN DAYNWEFLIW ESALLLFLLR
LASLGSETNK KYSNVSILLT EQINLYLKME KKPNKKEQLT LVNNVLKLST KLLKELDTPF
RLYGLTMNPL IYNITRVVIL SAVSGVISDL LGFNIRLWKI KS
