T150A_XENLA
ID T150A_XENLA Reviewed; 271 AA.
AC Q6GPL4;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Transmembrane protein 150A;
DE AltName: Full=Transmembrane protein 150;
GN Name=tmem150a; Synonyms=tmem150;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulates localization of phosphatidylinositol 4-kinase
CC (PI4K) to the plasma membrane. {ECO:0000250|UniProtKB:Q86TG1}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86TG1};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q86TG1}.
CC -!- SIMILARITY: Belongs to the DRAM/TMEM150 family. {ECO:0000305}.
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DR EMBL; BC073101; AAH73101.1; -; mRNA.
DR RefSeq; NP_001085656.1; NM_001092187.1.
DR AlphaFoldDB; Q6GPL4; -.
DR DNASU; 444082; -.
DR GeneID; 444082; -.
DR KEGG; xla:444082; -.
DR CTD; 444082; -.
DR Xenbase; XB-GENE-866465; tmem150a.L.
DR OMA; CWINTNA; -.
DR OrthoDB; 955528at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 444082; Expressed in neurula embryo and 19 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR InterPro; IPR019402; Frag1/DRAM/Sfk1.
DR InterPro; IPR027315; TMEM150A.
DR PANTHER; PTHR21324:SF6; PTHR21324:SF6; 1.
DR Pfam; PF10277; Frag1; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..271
FT /note="Transmembrane protein 150A"
FT /id="PRO_0000274778"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..75
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..140
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..205
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q86TG1"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 271 AA; 29404 MW; 4CEFD965A6DA8708 CRC64;
MTGWIVLPIS LTAFSIPGIW IVYAMAVMNH HVCPVENWTY NLTCTDDNTK AGTPKSCCTL
EDVPLISKCG TYPPESCLFS LIGNVGAFMV VIICLLRYSQ VIEISQRSWL NTTALIAGCT
NAAGLVMVGN FQVDYAKSLH YIGAGVAFPA GLLFVCLSSI LSYQLAASAL DYWLGHLRVS
LTIVALISLV LTGVFFIQES FLMQHLVAIC EWIFVLDILV FYGTFAYEFG SVSTDTMMAA
LQSSAARSCK SPGSSSTSTQ LHCNAERIAM I