TM214_MOUSE
ID TM214_MOUSE Reviewed; 687 AA.
AC Q8BM55; Q3TLH3; Q3UPX9; Q78HK3; Q8R0D5; Q8R237; Q8VC05;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Transmembrane protein 214;
GN Name=Tmem214;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Eye;
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] (ISOFORMS 1; 2 AND 3).
RC STRAIN=FVB/N; TISSUE=Colon, Eye, Liver, and Mammary tumor;
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=Liver, Lung, Pancreas, and Spleen;
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).
CC -!- FUNCTION: Critical mediator, in cooperation with CASP4, of endoplasmic
CC reticulum-stress induced apoptosis. Required or the activation of CASP4
CC following endoplasmic reticulum stress (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Constitutively interacts with CASP4; required for the
CC localization of procaspase 4 to the ER. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BM55-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BM55-2; Sequence=VSP_031817;
CC Name=3;
CC IsoId=Q8BM55-3; Sequence=VSP_031816;
CC -!- SIMILARITY: Belongs to the TMEM214 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22142.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH26651.1; Type=Erroneous initiation; Evidence={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; AK143078; BAE25265.1; -; mRNA.
DR EMBL; AK166510; BAE38819.1; -; mRNA.
DR EMBL; AK034883; BAC28866.1; -; mRNA.
DR EMBL; BC022602; AAH22602.1; -; mRNA.
DR EMBL; BC022142; AAH22142.1; ALT_INIT; mRNA.
DR EMBL; BC026651; AAH26651.1; ALT_INIT; mRNA.
DR EMBL; BC027046; AAH27046.1; -; mRNA.
DR EMBL; BC029150; AAH29150.3; -; mRNA.
DR CCDS; CCDS19164.1; -. [Q8BM55-1]
DR RefSeq; NP_653108.2; NM_144525.3. [Q8BM55-1]
DR RefSeq; XP_006504153.1; XM_006504090.1.
DR RefSeq; XP_017176576.1; XM_017321087.1.
DR AlphaFoldDB; Q8BM55; -.
DR BioGRID; 213055; 3.
DR IntAct; Q8BM55; 1.
DR STRING; 10090.ENSMUSP00000037484; -.
DR GlyGen; Q8BM55; 2 sites.
DR iPTMnet; Q8BM55; -.
DR PhosphoSitePlus; Q8BM55; -.
DR SwissPalm; Q8BM55; -.
DR EPD; Q8BM55; -.
DR jPOST; Q8BM55; -.
DR MaxQB; Q8BM55; -.
DR PaxDb; Q8BM55; -.
DR PeptideAtlas; Q8BM55; -.
DR PRIDE; Q8BM55; -.
DR ProteomicsDB; 259222; -. [Q8BM55-1]
DR ProteomicsDB; 259223; -. [Q8BM55-2]
DR ProteomicsDB; 259224; -. [Q8BM55-3]
DR Antibodypedia; 28071; 126 antibodies from 26 providers.
DR DNASU; 68796; -.
DR Ensembl; ENSMUST00000201203; ENSMUSP00000144615; ENSMUSG00000038828. [Q8BM55-1]
DR GeneID; 68796; -.
DR KEGG; mmu:68796; -.
DR UCSC; uc008wwa.1; mouse. [Q8BM55-1]
DR CTD; 54867; -.
DR MGI; MGI:1916046; Tmem214.
DR VEuPathDB; HostDB:ENSMUSG00000038828; -.
DR eggNOG; KOG4467; Eukaryota.
DR GeneTree; ENSGT00390000002693; -.
DR HOGENOM; CLU_025330_1_0_1; -.
DR InParanoid; Q8BM55; -.
DR OMA; IGQNWPS; -.
DR OrthoDB; 1409017at2759; -.
DR PhylomeDB; Q8BM55; -.
DR TreeFam; TF329489; -.
DR BioGRID-ORCS; 68796; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Tmem214; mouse.
DR PRO; PR:Q8BM55; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BM55; protein.
DR Bgee; ENSMUSG00000038828; Expressed in lacrimal gland and 248 other tissues.
DR ExpressionAtlas; Q8BM55; baseline and differential.
DR Genevisible; Q8BM55; MM.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR InterPro; IPR019308; TMEM214.
DR PANTHER; PTHR13448; PTHR13448; 1.
DR Pfam; PF10151; TMEM214; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Endoplasmic reticulum;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6NUQ4"
FT CHAIN 2..687
FT /note="Transmembrane protein 214"
FT /id="PRO_0000321898"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 614..634
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q6NUQ4"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..313
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031816"
FT VAR_SEQ 1..303
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031817"
FT CONFLICT 33
FT /note="S -> G (in Ref. 1; BAE38819)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="G -> R (in Ref. 1; BAE25265)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="S -> N (in Ref. 1; BAE38819)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="V -> I (in Ref. 1; BAE38819)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="G -> S (in Ref. 1; BAE38819)"
FT /evidence="ECO:0000305"
FT CONFLICT 658
FT /note="L -> F (in Ref. 1; BAE38819)"
FT /evidence="ECO:0000305"
FT CONFLICT 670
FT /note="Q -> H (in Ref. 1; BAE25265)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 687 AA; 76430 MW; E72AA7DF5486E968 CRC64;
MAARSAGSGG WEVVKRGRRP GASSGGRGGG GGSDRRALGE ANGVLKYDLS SPIQTTSTLY
ERGFEKIMKR QNKEQVPPPA AESKKPINKK QPKKVTAVPS QNQKQGPFRR LEDALKALDV
AALQKELDKS QSVFTGNPSV WLKDLASYLN YKLQTPRMEP TLSQYPHDYP YSLVSRELRG
IIRGLLTKAA GSVELFFDHC LFTMLQELDK TPGESLHGYR ICIQAVLQDK PKIVTSNLDK
FLELLRSHQS RPAKCLTIMW ALGQAGFTNL TEGLKVWLGI MLPVLGIKAL SPFAIAYLDR
LLLMHPNLTK GFGMIGPKDF FPLLDFAYMP NNSLSPSLQE QLCQLFPRLK VLAFGAKPES
SLHTYFPSFL SRATPSCPAA MKKELLASLT QCLTVDPLST SVWRQLYPKH LSQSSLLLEH
LLKSWEHIPK KARKSLQETI QSLKVTNQEL LKKGSGGSEH VLTCDTACKG LLQRARGPRP
PWARLFLLLL VFAVGFLCHD LRSNSSLQAS LTGRLLRSSG LLPVGQQVCA RLSSYSLQSY
NWLQETLPAC GSHLLAVVQP SLQLAWTHIY AIFSFLSAHC ASYLACFSDS LAGFFQRVQL
PEALQQLFHA LKELLLLFCH SVLLPTWHLL LAALAQVQEH CHEACRGDVT WDCIKTQLSR
AAQWTWLCLQ DVTVAFLDWA LTMISQQ
