TM38B_HUMAN
ID TM38B_HUMAN Reviewed; 291 AA.
AC Q9NVV0; Q5JR63; Q5SVN5; Q5SVN6; Q5VTE2; Q6IA97;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Trimeric intracellular cation channel type B;
DE Short=TRIC-B;
DE Short=TRICB;
DE AltName: Full=Transmembrane protein 38B;
GN Name=TMEM38B; Synonyms=C9orf87;
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=Teratocarcinoma;
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 MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP INVOLVEMENT IN OI14.
RX PubMed=23054245; DOI=10.1136/jmedgenet-2012-101142;
RA Shaheen R., Alazami A.M., Alshammari M.J., Faqeih E., Alhashmi N.,
RA Mousa N., Alsinani A., Ansari S., Alzahrani F., Al-Owain M., Alzayed Z.S.,
RA Alkuraya F.S.;
RT "Study of autosomal recessive osteogenesis imperfecta in Arabia reveals a
RT novel locus defined by TMEM38B mutation.";
RL J. Med. Genet. 49:630-635(2012).
RN [10]
RP INVOLVEMENT IN OI14.
RX PubMed=23316006; DOI=10.1002/humu.22274;
RA Volodarsky M., Markus B., Cohen I., Staretz-Chacham O., Flusser H.,
RA Landau D., Shelef I., Langer Y., Birk O.S.;
RT "A deletion mutation in TMEM38B associated with autosomal recessive
RT osteogenesis imperfecta.";
RL Hum. Mutat. 34:582-586(2013).
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:Q9DAV9}.
CC -!- SUBUNIT: Homotrimer; trimerization probably requires binding to
CC phosphatidylinositol 4,5-bisphosphate (PIP2).
CC {ECO:0000250|UniProtKB:A5A6S6, ECO:0000250|UniProtKB:Q9NA73}.
CC -!- INTERACTION:
CC Q9NVV0; P29972: AQP1; NbExp=3; IntAct=EBI-1055114, EBI-745213;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9DAV9}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9DAV9}.
CC -!- DISEASE: Osteogenesis imperfecta 14 (OI14) [MIM:615066]: An autosomal
CC recessive form of osteogenesis imperfecta, a connective tissue disorder
CC characterized by low bone mass, bone fragility and susceptibility to
CC fractures after minimal trauma. Disease severity ranges from very mild
CC forms without fractures to intrauterine fractures and perinatal
CC lethality. Extraskeletal manifestations, which affect a variable number
CC of patients, are dentinogenesis imperfecta, hearing loss, and blue
CC sclerae. OI14 is characterized by variable degrees of severity of
CC multiple fractures and osteopenia, with normal teeth, sclerae, and
CC hearing. Fractures first occur prenatally or by age 6 years.
CC {ECO:0000269|PubMed:23054245, ECO:0000269|PubMed:23316006}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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; AK001355; BAA91645.1; -; mRNA.
DR EMBL; CR457258; CAG33539.1; -; mRNA.
DR EMBL; AL592437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL592488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL627247; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000049; AAH00049.1; -; mRNA.
DR CCDS; CCDS6768.1; -.
DR RefSeq; NP_060582.1; NM_018112.2.
DR AlphaFoldDB; Q9NVV0; -.
DR SMR; Q9NVV0; -.
DR BioGRID; 120454; 61.
DR IntAct; Q9NVV0; 9.
DR MINT; Q9NVV0; -.
DR STRING; 9606.ENSP00000363824; -.
DR TCDB; 1.A.62.1.3; the homotrimeric cation channel (tric) family.
DR iPTMnet; Q9NVV0; -.
DR PhosphoSitePlus; Q9NVV0; -.
DR SwissPalm; Q9NVV0; -.
DR BioMuta; TMEM38B; -.
DR DMDM; 74753001; -.
DR EPD; Q9NVV0; -.
DR jPOST; Q9NVV0; -.
DR MassIVE; Q9NVV0; -.
DR MaxQB; Q9NVV0; -.
DR PaxDb; Q9NVV0; -.
DR PeptideAtlas; Q9NVV0; -.
DR PRIDE; Q9NVV0; -.
DR ProteomicsDB; 82862; -.
DR Antibodypedia; 14850; 103 antibodies from 26 providers.
DR DNASU; 55151; -.
DR Ensembl; ENST00000374692.8; ENSP00000363824.3; ENSG00000095209.12.
DR GeneID; 55151; -.
DR KEGG; hsa:55151; -.
DR MANE-Select; ENST00000374692.8; ENSP00000363824.3; NM_018112.3; NP_060582.1.
DR UCSC; uc004bcu.3; human.
DR CTD; 55151; -.
DR DisGeNET; 55151; -.
DR GeneCards; TMEM38B; -.
DR HGNC; HGNC:25535; TMEM38B.
DR HPA; ENSG00000095209; Tissue enhanced (skeletal muscle, tongue).
DR MalaCards; TMEM38B; -.
DR MIM; 611236; gene.
DR MIM; 615066; phenotype.
DR neXtProt; NX_Q9NVV0; -.
DR OpenTargets; ENSG00000095209; -.
DR Orphanet; 216820; Osteogenesis imperfecta type 4.
DR PharmGKB; PA134916126; -.
DR VEuPathDB; HostDB:ENSG00000095209; -.
DR eggNOG; KOG3944; Eukaryota.
DR GeneTree; ENSGT00390000018845; -.
DR HOGENOM; CLU_076376_0_0_1; -.
DR InParanoid; Q9NVV0; -.
DR OMA; LPIAKHN; -.
DR OrthoDB; 1319985at2759; -.
DR PhylomeDB; Q9NVV0; -.
DR TreeFam; TF313483; -.
DR PathwayCommons; Q9NVV0; -.
DR SignaLink; Q9NVV0; -.
DR BioGRID-ORCS; 55151; 11 hits in 1079 CRISPR screens.
DR ChiTaRS; TMEM38B; human.
DR GenomeRNAi; 55151; -.
DR Pharos; Q9NVV0; Tbio.
DR PRO; PR:Q9NVV0; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9NVV0; protein.
DR Bgee; ENSG00000095209; Expressed in sperm and 185 other tissues.
DR ExpressionAtlas; Q9NVV0; baseline and differential.
DR Genevisible; Q9NVV0; HS.
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:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; NAS:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IEA:InterPro.
DR GO; GO:0005267; F:potassium channel activity; TAS:BHF-UCL.
DR GO; GO:0060348; P:bone development; IEA:Ensembl.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR GO; GO:0071313; P:cellular response to caffeine; IEA:Ensembl.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0070278; P:extracellular matrix constituent secretion; IEA:Ensembl.
DR GO; GO:0048286; P:lung alveolus development; IEA:Ensembl.
DR GO; GO:0060487; P:lung epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0008654; P:phospholipid biosynthetic process; 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 GO; GO:0061033; P:secretion by lung epithelial cell involved in lung growth; IEA:Ensembl.
DR InterPro; IPR007866; TRIC_channel.
DR PANTHER; PTHR12454; PTHR12454; 1.
DR Pfam; PF05197; TRIC; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Ion channel; Ion transport; Membrane;
KW Osteogenesis imperfecta; Phosphoprotein; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..291
FT /note="Trimeric intracellular cation channel type B"
FT /id="PRO_0000291524"
FT TOPO_DOM 1..19
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 20..33
FT /note="Helical;Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 51..70
FT /note="Helical;Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..82
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 83..99
FT /note="Helical;Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 105..121
FT /note="Helical;Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..139
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 140..156
FT /note="Helical;Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 180..195
FT /note="Helical;Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..207
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 208..227
FT /note="Helical;Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 256..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 118
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 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 MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT VARIANT 254
FT /note="C -> S (in dbSNP:rs35232724)"
FT /id="VAR_032811"
FT CONFLICT 32
FT /note="A -> E (in Ref. 2; CAG33539)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="E -> D (in Ref. 2; CAG33539)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 291 AA; 32510 MW; 1975F1E0053EAE7B CRC64;
MDSPWDELAL AFSRTSMFPF FDIAHYLVSV MAVKRQPGAA ALAWKNPISS WFTAMLHCFG
GGILSCLLLA EPPLKFLANH TNILLASSIW YITFFCPHDL VSQGYSYLPV QLLASGMKEV
TRTWKIVGGV THANSYYKNG WIVMIAIGWA RGAGGTIITN FERLVKGDWK PEGDEWLKMS
YPAKVTLLGS VIFTFQHTQH LAISKHNLMF LYTIFIVATK ITMMTTQTST MTFAPFEDTL
SWMLFGWQQP FSSCEKKSEA KSPSNGVGSL ASKPVDVASD NVKKKHTKKN E
