TM38A_HUMAN
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 03-AUG-2022, entry version 133.
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}.
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; 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; 10.
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; Q9H6F2; -.
DR PeptideAtlas; Q9H6F2; -.
DR PRIDE; Q9H6F2; -.
DR ProteomicsDB; 80984; -.
DR Antibodypedia; 27435; 131 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 CTD; 79041; -.
DR DisGeNET; 79041; -.
DR GeneCards; TMEM38A; -.
DR HGNC; HGNC:28462; TMEM38A.
DR HPA; ENSG00000072954; Group enriched (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; LQEAHWL; -.
DR OrthoDB; 1319985at2759; -.
DR PhylomeDB; Q9H6F2; -.
DR TreeFam; TF313483; -.
DR PathwayCommons; Q9H6F2; -.
DR SignaLink; Q9H6F2; -.
DR BioGRID-ORCS; 79041; 27 hits in 1074 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 133 other tissues.
DR ExpressionAtlas; Q9H6F2; baseline and differential.
DR Genevisible; Q9H6F2; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; PTHR12454; 1.
DR Pfam; PF05197; TRIC; 1.
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
