TM225_BOVIN
ID TM225_BOVIN Reviewed; 231 AA.
AC Q32KQ5;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Transmembrane protein 225;
GN Name=TMEM225; Synonyms=PMP22CD;
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=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably inhibits protein phosphatase 1 (PP1) in sperm via
CC binding to catalytic subunit PPP1CC. {ECO:0000250|UniProtKB:Q9D9S2}.
CC -!- SUBUNIT: Interacts (via RVxF motif) with PPP1CC.
CC {ECO:0000250|UniProtKB:Q9D9S2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC membrane {ECO:0000250|UniProtKB:Q9D9S2}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- CAUTION: This protein is not related to the claudin family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI09976.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC109975; AAI09976.1; ALT_INIT; mRNA.
DR RefSeq; NP_001073753.2; NM_001080284.2.
DR AlphaFoldDB; Q32KQ5; -.
DR SMR; Q32KQ5; -.
DR STRING; 9913.ENSBTAP00000044826; -.
DR PaxDb; Q32KQ5; -.
DR GeneID; 519985; -.
DR KEGG; bta:519985; -.
DR CTD; 338661; -.
DR eggNOG; ENOG502TDTU; Eukaryota.
DR InParanoid; Q32KQ5; -.
DR OrthoDB; 1369226at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0002080; C:acrosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0010923; P:negative regulation of phosphatase activity; IEA:InterPro.
DR InterPro; IPR033542; TMEM225.
DR PANTHER; PTHR36477; PTHR36477; 1.
PE 2: Evidence at transcript level;
KW Cytoplasmic vesicle; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..231
FT /note="Transmembrane protein 225"
FT /id="PRO_0000339349"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..67
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..135
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOTIF 225..229
FT /note="RVxF"
FT /evidence="ECO:0000250|UniProtKB:Q9D9S2"
SQ SEQUENCE 231 AA; 26224 MW; 28FB56CDDCD70AFB CRC64;
MVHILVRKVE ATNMFFSSWT LVFLAVGIII EEWAELKLGP QKPTITHSPW ICCTPLWPSD
GLEVIRNILI VVLSLSFMHN LLLGFEFTYM IPQTKYTLIM TACLAFLTGI LLLGALLLYH
HMLRQGESVY YSSYKISWII FTAYLNVLFL FISGFLSLLQ YKQPIDGSGS LIPRSARKSQ
VMEQHGVSIK VVSLPAGTAM PRSIVRLHSA HMKEDSPERL NIQARRVTWA L