T214A_XENLA
ID T214A_XENLA Reviewed; 681 AA.
AC A0JMW6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Transmembrane protein 214-A;
GN Name=tmem214-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
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; BC126031; AAI26032.1; -; mRNA.
DR RefSeq; NP_001090439.1; NM_001096970.1.
DR AlphaFoldDB; A0JMW6; -.
DR DNASU; 779351; -.
DR GeneID; 779351; -.
DR KEGG; xla:779351; -.
DR CTD; 779351; -.
DR Xenbase; XB-GENE-6252459; tmem214.L.
DR OrthoDB; 1409017at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 779351; Expressed in liver and 19 other tissues.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR019308; TMEM214.
DR PANTHER; PTHR13448; PTHR13448; 1.
DR Pfam; PF10151; TMEM214; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..681
FT /note="Transmembrane protein 214-A"
FT /id="PRO_0000321900"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 608..628
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 681 AA; 76871 MW; A384BF2CD9ED0D0E CRC64;
MASGAPDGKW KVVKKGKKSG EKGGGRKALS ESNVTPGGTA PIKMANTVYE MGFEQILKKQ
NKEQVPPNNI PAEQPQKKQQ QQQNPGRKKP QSGDTGSRQR KFHTLEEGLK ALDLAELQRE
LEKSQNMFPE SPSIWVKDLA GYLNYKLQTV KNDVLIQQSH DYPYCLVNKE LKGIVRSLLA
KAPHVLDVMV DHCIFSMFQE LDKPTGESLH GYRICLQAVL LDKPKTVTNN LPKYLELLRS
QVNRPMKCLA VMWAVGQAGF TDLSEGLKVW LGLMFPVLGV KTLTPYAILY LDRLLLAHSN
LTKGFGMIGP KDFFPLLDFA FMPNNSLTSS QQENLRNLYP RLKVLAFGAT PESTLHTYFP
SFLSRVTPSC PAEMRKELIN SLTDCLNKDP LSFSVWRQLY TKHLSQSSFL LQHLVETWDS
NSKAMRKSVR ETVHSFKVTN GEFSGKGSSL KDLEACDAAC QALLHKMKGS GFPWRRLIVI
AFVFLFGFVF YDVRTHNSFQ ASTSHKVLQQ SGLLSVSQQA WSKVSNYSLQ GQSWLERNVP
QYYSQAVEVL GPVLEQVWAK TQEGAAYACE KGSVLITYTK DNLPRLIEWL HSHTPDSVCQ
FIEYLRELLL HLHRTYLLPA VTYLEAAVQN AWQQYVASCN GKVTWDCVRG QVSNISHSSW
TYLQNTTMTV TNWALSIISH H