ID   TM38A_HUMAN             Reviewed;         299 AA.
AC   Q9H6F2; A8K9P9;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   24-JAN-2024, entry version 140.
DE   RecName: Full=Trimeric intracellular cation channel type A;
DE            Short=TRIC-A;
DE            Short=TRICA;
DE   AltName: Full=Transmembrane protein 38A;
GN   Name=TMEM38A;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TOPOLOGY.
RX   PubMed=17611541; DOI=10.1038/nature05928;
RA   Yazawa M., Ferrante C., Feng J., Mio K., Ogura T., Zhang M., Lin P.-H.,
RA   Pan Z., Komazaki S., Kato K., Nishi M., Zhao X., Weisleder N., Sato C.,
RA   Ma J., Takeshima H.;
RT   "TRIC channels are essential for Ca2+ handling in intracellular stores.";
RL   Nature 448:78-82(2007).
CC   -!- FUNCTION: Monovalent cation channel required for maintenance of rapid
CC       intracellular calcium release. May act as a potassium counter-ion
CC       channel that functions in synchronization with calcium release from
CC       intracellular stores. {ECO:0000250|UniProtKB:Q3TMP8}.
CC   -!- SUBUNIT: Homotrimer; trimerization probably requires binding to
CC       phosphatidylinositol 4,5-bisphosphate (PIP2).
CC       {ECO:0000250|UniProtKB:A5A6S6, ECO:0000250|UniProtKB:Q9NA73}.
CC   -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:A5A6S6}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:A5A6S6}. Nucleus membrane
CC       {ECO:0000250|UniProtKB:A5A6S6}.
CC   -!- SIMILARITY: Belongs to the TMEM38 family. {ECO:0000305}.
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DR   EMBL; AK025981; BAB15307.1; -; mRNA.
DR   EMBL; AK292764; BAF85453.1; -; mRNA.
DR   EMBL; CH471106; EAW84559.1; -; Genomic_DNA.
DR   EMBL; BC001195; AAH01195.1; -; mRNA.
DR   CCDS; CCDS12349.1; -.
DR   RefSeq; NP_076979.1; NM_024074.2.
DR   AlphaFoldDB; Q9H6F2; -.
DR   SMR; Q9H6F2; -.
DR   BioGRID; 122504; 11.
DR   IntAct; Q9H6F2; 6.
DR   STRING; 9606.ENSP00000187762; -.
DR   iPTMnet; Q9H6F2; -.
DR   PhosphoSitePlus; Q9H6F2; -.
DR   BioMuta; TMEM38A; -.
DR   DMDM; 74733603; -.
DR   MassIVE; Q9H6F2; -.
DR   PaxDb; 9606-ENSP00000187762; -.
DR   PeptideAtlas; Q9H6F2; -.
DR   ProteomicsDB; 80984; -.
DR   Antibodypedia; 27435; 137 antibodies from 27 providers.
DR   DNASU; 79041; -.
DR   Ensembl; ENST00000187762.7; ENSP00000187762.1; ENSG00000072954.7.
DR   GeneID; 79041; -.
DR   KEGG; hsa:79041; -.
DR   MANE-Select; ENST00000187762.7; ENSP00000187762.1; NM_024074.4; NP_076979.1.
DR   UCSC; uc002nes.4; human.
DR   AGR; HGNC:28462; -.
DR   CTD; 79041; -.
DR   DisGeNET; 79041; -.
DR   GeneCards; TMEM38A; -.
DR   HGNC; HGNC:28462; TMEM38A.
DR   HPA; ENSG00000072954; Tissue enhanced (skeletal muscle, tongue).
DR   MIM; 611235; gene.
DR   neXtProt; NX_Q9H6F2; -.
DR   OpenTargets; ENSG00000072954; -.
DR   PharmGKB; PA134891982; -.
DR   VEuPathDB; HostDB:ENSG00000072954; -.
DR   eggNOG; KOG3944; Eukaryota.
DR   GeneTree; ENSGT00390000018845; -.
DR   HOGENOM; CLU_076376_0_1_1; -.
DR   InParanoid; Q9H6F2; -.
DR   OMA; SMSFPTK; -.
DR   OrthoDB; 36169at2759; -.
DR   PhylomeDB; Q9H6F2; -.
DR   TreeFam; TF313483; -.
DR   PathwayCommons; Q9H6F2; -.
DR   SignaLink; Q9H6F2; -.
DR   BioGRID-ORCS; 79041; 28 hits in 1152 CRISPR screens.
DR   ChiTaRS; TMEM38A; human.
DR   GenomeRNAi; 79041; -.
DR   Pharos; Q9H6F2; Tbio.
DR   PRO; PR:Q9H6F2; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q9H6F2; Protein.
DR   Bgee; ENSG00000072954; Expressed in hindlimb stylopod muscle and 135 other cell types or tissues.
DR   ExpressionAtlas; Q9H6F2; baseline and differential.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0031965; C:nuclear membrane; NAS:BHF-UCL.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; NAS:BHF-UCL.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0005267; F:potassium channel activity; TAS:BHF-UCL.
DR   GO; GO:0071313; P:cellular response to caffeine; IEA:Ensembl.
DR   GO; GO:0007029; P:endoplasmic reticulum organization; IEA:Ensembl.
DR   GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IEA:Ensembl.
DR   GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IEA:Ensembl.
DR   InterPro; IPR007866; TRIC_channel.
DR   PANTHER; PTHR12454; TRIMERIC INTRACELLULAR CATION CHANNEL; 1.
DR   PANTHER; PTHR12454:SF3; TRIMERIC INTRACELLULAR CATION CHANNEL TYPE A; 1.
DR   Pfam; PF05197; TRIC; 1.
DR   Genevisible; Q9H6F2; HS.
PE   1: Evidence at protein level;
KW   Ion channel; Ion transport; Membrane; Nucleus; Potassium;
KW   Potassium channel; Potassium transport; Reference proteome;
KW   Sarcoplasmic reticulum; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..299
FT                   /note="Trimeric intracellular cation channel type A"
FT                   /id="PRO_0000271068"
FT   TOPO_DOM        1..18
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        19..39
FT                   /note="Helical;Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        40..51
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        52..72
FT                   /note="Helical;Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        73..85
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        86..106
FT                   /note="Helical;Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        107..144
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        145..165
FT                   /note="Helical;Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        166..178
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        179..199
FT                   /note="Helical;Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        200..209
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        210..230
FT                   /note="Helical;Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        231..234
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        235..255
FT                   /note="Helical;Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        256..299
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          260..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..299
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         122
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-4,5-bisphosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58456"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NA73"
FT   BINDING         126
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-4,5-bisphosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58456"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NA73"
SQ   SEQUENCE   299 AA;  33260 MW;  40E9D5917F5E3907 CRC64;
     MELLSALSLG ELALSFSRVP LFPVFDLSYF IVSILYLKYE PGAVELSRRH PIASWLCAML
     HCFGSYILAD LLLGEPLIDY FSNNSSILLA SAVWYLIFFC PLDLFYKCVC FLPVKLIFVA
     MKEVVRVRKI AVGIHHAHHH YHHGWFVMIA TGWVKGSGVA LMSNFEQLLR GVWKPETNEI
     LHMSFPTKAS LYGAILFTLQ QTRWLPVSKA SLIFIFTLFM VSCKVFLTAT HSHSSPFDAL
     EGYICPVLFG SACGGDHHHD NHGGSHSGGG PGAQHSAMPA KSKEELSEGS RKKKAKKAD
//