TMM33_MOUSE
ID TMM33_MOUSE Reviewed; 247 AA.
AC Q9CR67; Q544Q3; Q9D3M3; Q9DAV4;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Transmembrane protein 33;
DE AltName: Full=Protein DB83;
GN Name=Tmem33; Synonyms=Db83;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow, Brain, Head, Pancreas, Placenta, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, INTERACTION WITH PKD2, DISRUPTION PHENOTYPE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=31048699; DOI=10.1038/s41467-019-10045-y;
RA Arhatte M., Gunaratne G.S., El Boustany C., Kuo I.Y., Moro C., Duprat F.,
RA Plaisant M., Duval H., Li D., Picard N., Couvreux A., Duranton C.,
RA Rubera I., Pagnotta S., Lacas-Gervais S., Ehrlich B.E., Marchant J.S.,
RA Savage A.M., van Eeden F.J.M., Wilkinson R.N., Demolombe S., Honore E.,
RA Patel A.;
RT "TMEM33 regulates intracellular calcium homeostasis in renal tubular
RT epithelial cells.";
RL Nat. Commun. 10:2024-2024(2019).
CC -!- FUNCTION: Acts as a regulator of the tubular endoplasmic reticulum (ER)
CC network by modulating intracellular calcium homeostasis.
CC Mechanistically, stimulates PKD2 calcium-dependent activity
CC (PubMed:31048699). Suppresses the RTN3/4-induced formation of the ER
CC tubules. Positively regulates PERK-mediated and IRE1-mediated unfolded
CC protein response signaling. Plays an essential role in VEGF-mediated
CC release of Ca(2+) from ER stores during angiogenesis. Also plays a role
CC in the modulation of innate immune signaling through the cGAS-STING
CC pathway by interacting with RNF26. Participates in lipid metabolism by
CC acting as a downstream effector of the pyruvate kinase/PKM. Forms a
CC complex with RNF5 to facilitate polyubiquitination and subsequent
CC degradation of SCAP on the ER membrane (By similarity).
CC {ECO:0000250|UniProtKB:P57088, ECO:0000269|PubMed:31048699}.
CC -!- SUBUNIT: Interacts with EIF2AK3 (By similarity). Interacts with RTN1,
CC RTN2, RTN3, RTN4 and ARL6IP1 (By similarity). Interacts with RNF5.
CC Interacts with RNF26 (By similarity). Interacts with PKD2
CC (PubMed:31048699). {ECO:0000250|UniProtKB:P57088,
CC ECO:0000269|PubMed:31048699}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:31048699}; Multi-pass membrane protein
CC {ECO:0000255}. Melanosome {ECO:0000250|UniProtKB:P57088}. Nucleus
CC envelope {ECO:0000250|UniProtKB:P57088}. Note=Co-localizes with RTN4 at
CC the ER sheets. {ECO:0000250|UniProtKB:P57088}.
CC -!- DISRUPTION PHENOTYPE: Deletion mice show renal protection against acute
CC kidney injury (AKI). {ECO:0000269|PubMed:31048699}.
CC -!- SIMILARITY: Belongs to the PER33/POM33 family. {ECO:0000305}.
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DR EMBL; AK005493; BAB24078.1; -; mRNA.
DR EMBL; AK007607; BAB25131.1; -; mRNA.
DR EMBL; AK007750; BAB25233.1; -; mRNA.
DR EMBL; AK017281; BAB30671.1; -; mRNA.
DR EMBL; AK032555; BAC27922.1; -; mRNA.
DR EMBL; AK153441; BAE31997.1; -; mRNA.
DR EMBL; AK165369; BAE38149.1; -; mRNA.
DR EMBL; BC005562; AAH05562.1; -; mRNA.
DR EMBL; BC016570; AAH16570.1; -; mRNA.
DR EMBL; BC023966; AAH23966.1; -; mRNA.
DR CCDS; CCDS19317.1; -.
DR RefSeq; NP_001272381.1; NM_001285452.1.
DR RefSeq; NP_083251.2; NM_028975.4.
DR RefSeq; NP_084384.1; NM_030108.2.
DR AlphaFoldDB; Q9CR67; -.
DR SMR; Q9CR67; -.
DR BioGRID; 212504; 8.
DR IntAct; Q9CR67; 2.
DR MINT; Q9CR67; -.
DR STRING; 10090.ENSMUSP00000042852; -.
DR iPTMnet; Q9CR67; -.
DR PhosphoSitePlus; Q9CR67; -.
DR SwissPalm; Q9CR67; -.
DR EPD; Q9CR67; -.
DR jPOST; Q9CR67; -.
DR MaxQB; Q9CR67; -.
DR PaxDb; Q9CR67; -.
DR PeptideAtlas; Q9CR67; -.
DR PRIDE; Q9CR67; -.
DR ProteomicsDB; 259033; -.
DR TopDownProteomics; Q9CR67; -.
DR Antibodypedia; 60901; 93 antibodies from 19 providers.
DR DNASU; 67878; -.
DR Ensembl; ENSMUST00000037918; ENSMUSP00000042852; ENSMUSG00000037720.
DR Ensembl; ENSMUST00000161369; ENSMUSP00000124390; ENSMUSG00000037720.
DR GeneID; 67878; -.
DR KEGG; mmu:67878; -.
DR UCSC; uc008xpp.2; mouse.
DR CTD; 55161; -.
DR MGI; MGI:1915128; Tmem33.
DR VEuPathDB; HostDB:ENSMUSG00000037720; -.
DR eggNOG; KOG4002; Eukaryota.
DR GeneTree; ENSGT00390000011368; -.
DR HOGENOM; CLU_071391_0_0_1; -.
DR InParanoid; Q9CR67; -.
DR OMA; FFSIRPT; -.
DR OrthoDB; 1360050at2759; -.
DR PhylomeDB; Q9CR67; -.
DR TreeFam; TF314068; -.
DR BioGRID-ORCS; 67878; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Tmem33; mouse.
DR PRO; PR:Q9CR67; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9CR67; protein.
DR Bgee; ENSMUSG00000037720; Expressed in choroid plexus epithelium and 257 other tissues.
DR ExpressionAtlas; Q9CR67; baseline and differential.
DR Genevisible; Q9CR67; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0071786; P:endoplasmic reticulum tubular network organization; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0061024; P:membrane organization; IBA:GO_Central.
DR GO; GO:1903896; P:positive regulation of IRE1-mediated unfolded protein response; ISS:UniProtKB.
DR GO; GO:1903899; P:positive regulation of PERK-mediated unfolded protein response; ISS:UniProtKB.
DR GO; GO:1903371; P:regulation of endoplasmic reticulum tubular network organization; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR InterPro; IPR005344; TMEM33/Pom33.
DR Pfam; PF03661; TMEM33_Pom33; 1.
PE 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; Immunity; Innate immunity; Membrane;
KW Nucleus; Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P57088"
FT CHAIN 2..247
FT /note="Transmembrane protein 33"
FT /id="PRO_0000220900"
FT TOPO_DOM 2..31
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..155
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P57088"
FT CONFLICT 39
FT /note="A -> T (in Ref. 1; BAB24078)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="Missing (in Ref. 1; BAB30671)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 247 AA; 28031 MW; 1813EF1C109ACC05 CRC64;
MADTTPNGPQ GAGAVQFMMT NKLDTAMWLS RLFTVYCSAL FVLPLLGLHE AASFYQRALL
ANALTSALRL HQRLPHFQLS RAFLAQALLE DSCHYLLYSL IFVNSYPVTM SIFPVLLFSL
LHAATYTKKV LDAKGSNSLP LLRSFLDKLS TNQQNILKFI ACNEIFLMPA TVFMLFSGQG
SLLQPFIYYR FLTLRYSSRR NPYCRNLFNE LRIVVEHIIM KPSCPLFVRR LCLQSIAFIS
RLAPTVA
