ID   TM214_RAT               Reviewed;         685 AA.
AC   A1L1L2; Q5U4F5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Transmembrane protein 214;
GN   Name=Tmem214;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney, and Testis;
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).
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   -!- SIMILARITY: Belongs to the TMEM214 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH85114.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; BC085114; AAH85114.1; ALT_FRAME; mRNA.
DR   EMBL; BC129115; AAI29116.1; -; mRNA.
DR   RefSeq; NP_001014217.2; NM_001014195.2.
DR   AlphaFoldDB; A1L1L2; -.
DR   STRING; 10116.ENSRNOP00000011838; -.
DR   GlyGen; A1L1L2; 2 sites.
DR   PaxDb; A1L1L2; -.
DR   PeptideAtlas; A1L1L2; -.
DR   PRIDE; A1L1L2; -.
DR   Ensembl; ENSRNOT00000011838; ENSRNOP00000011838; ENSRNOG00000008812.
DR   GeneID; 362711; -.
DR   KEGG; rno:362711; -.
DR   CTD; 54867; -.
DR   RGD; 1311324; Tmem214.
DR   eggNOG; KOG4467; Eukaryota.
DR   GeneTree; ENSGT00390000002693; -.
DR   HOGENOM; CLU_025330_1_0_1; -.
DR   InParanoid; A1L1L2; -.
DR   OMA; IGQNWPS; -.
DR   OrthoDB; 1409017at2759; -.
DR   PhylomeDB; A1L1L2; -.
DR   TreeFam; TF329489; -.
DR   PRO; PR:A1L1L2; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000008812; Expressed in testis and 19 other tissues.
DR   Genevisible; A1L1L2; RN.
DR   GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Acetylation; Apoptosis; Endoplasmic reticulum; Glycoprotein; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q6NUQ4"
FT   CHAIN           2..685
FT                   /note="Transmembrane protein 214"
FT                   /id="PRO_0000321899"
FT   TRANSMEM        479..499
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        612..632
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          66..104
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        267
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        305
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   685 AA;  76566 MW;  76EAA04ECB7D1416 CRC64;
     MAARAAGSGG WEVVKRSRRP GASSGGRGGG GDRRALGEAN GVWKYDLSSP IQPTSTLYER
     GFEKIMKRQN KEQVPPPAAE SKKPVNKKQP KKVTAVASQN QKQGPFRSLE DALKALDVAA
     LQKELDKSQS VFTGNPSVWL KDLASYLNYK LQTPRMEPTL SQYPHDYPYS LVSRELRGII
     RGLLTKAAGS VELFFDHCLF TMLQELDKTP GESLHGYRIC IQAILQDKPK IVTSNLDKFL
     ELLRSHQSRP AKCLTIMWAL GQAGFTNLTE GLKVWLGIML PVLGIKSLSP FAIAYLDRLL
     LMYPNLTKGF GMIGPKDFFP LLDFAYMPNN SLSPSLQEQL CQLFPRLKVL AFGAKPESSL
     HTYFPSFLSR ATPSCPAAMK KELLASLTQC LTVDPLSTSV WRQLYPKHLS QSSLLLEHLL
     TSWEQIPKKA RKCLQETIQS FTLTNQELLK KGSGSNEHVV TCDTACKGLL QQARGPRPPW
     ARLLLLLLVF AVGFLCHDLR SHSSFQASLT GRLLQSSGLL PVAQQVCAKL YSYSLQSYNW
     LQETLPACGS YLLAVVQPSL QLAWTYIYAT FSFLSAYCAS YLAFFSDSLA GVLQRVQLPE
     ALHQLFHSLK ELLLLFYHSV LLPMWHLLLA ALAQVQEHCH EACRGEMTWD CIKTQFSTAA
     HWTWLCLQDV TVAFLDWALT MISQQ