T214B_XENLA
ID T214B_XENLA Reviewed; 679 AA.
AC A1L2I9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Transmembrane protein 214-B;
GN Name=tmem214-b;
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=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-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}.
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DR EMBL; BC129551; AAI29552.1; -; mRNA.
DR RefSeq; NP_001090615.1; NM_001097146.1.
DR AlphaFoldDB; A1L2I9; -.
DR GeneID; 100036861; -.
DR KEGG; xla:100036861; -.
DR CTD; 100036861; -.
DR Xenbase; XB-GENE-5827050; tmem214.S.
DR OrthoDB; 1409017at2759; -.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 100036861; Expressed in testis and 19 other tissues.
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; IPR019308; TMEM214.
DR PANTHER; PTHR13448; PTHR13448; 1.
DR Pfam; PF10151; TMEM214; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..679
FT /note="Transmembrane protein 214-B"
FT /id="PRO_0000321901"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..626
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 679 AA; 76807 MW; A1BC9BF17FFFE8CA CRC64;
MASGAPDGKW KVVKKGKKSG ERREGERKAL TESNVTPGGT APIKMANTVY EMGFDRIHKK
QNKEQVPPNN MSSEQPQKQQ QNPGKKKPQS GDSVCKQSKF HTLECALKAL DVAELQRDLE
KSQNMFPENP SIWVKDLAGY LNYKLQTVKN DVLIQQSHDY PYCLINKELK GIVRSLLAKA
PHVLDVMVDH CIFSMLQELD KPTGESLHGY RICIQAVLLD KPKTVTSNLP KYLELLRSHL
NRPMKCLTVM WAVGQAGFTD FTEGLKVWLG LMFPVLGVKN LTPYAILYLD RLLLAHSNLT
KGFGMIGPKD FFPILDFAFM PNNSLTPSQQ ENLRNLYPKL KVLALGATPE STLHTYFPSF
LSRATPSCPA EMRKELIHSL TDCLNKDSLS FSVWRQLYTK HLSQSSLLLQ HLVETWDSNS
RAMRKSVRET VHSFKVTNGE FSGKGSSSKD LEACDAACQA LLHKMKSGGF PWWRLIVIAF
VFLFGSVLYD VRTHNSFQES TSAQILQQSG LLSVSREAWN KVSNYSLQGQ SWLERNVPQY
YSQAVEVLGP VLEQVWAKTQ EGGAYACEKG SVLLSYAKDN LPRLIEWLHS SIPDSVFQFI
EYLRELLLHL HQTYLLPAVT YLEAAVQNSW QQYVKSCNGK VTWDCVRGQV GNISHSSWTY
LQNTTMTFTN WALTIISRH