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Database: UniProt
Entry: E4XE25_OIKDI
LinkDB: E4XE25_OIKDI
Original site: E4XE25_OIKDI 
ID   E4XE25_OIKDI            Unreviewed;       252 AA.
AC   E4XE25;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Translocon-associated protein subunit alpha {ECO:0000256|ARBA:ARBA00020280};
DE   AltName: Full=Signal sequence receptor subunit alpha {ECO:0000256|ARBA:ARBA00031071};
GN   ORFNames=GSOID_T00008427001 {ECO:0000313|EMBL:CBY19415.1},
GN   GSOID_T00026705001 {ECO:0000313|EMBL:CBY42967.1};
OS   Oikopleura dioica (Tunicate).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC   Oikopleuridae; Oikopleura.
OX   NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY19415.1};
RN   [1] {ECO:0000313|EMBL:CBY19415.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21097902; DOI=10.1126/science.1194167;
RA   Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA   Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA   Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA   Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA   Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA   Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA   Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA   Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA   Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA   Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA   Roest Crollius H., Wincker P., Chourrout D.;
RT   "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT   pelagic tunicate.";
RL   Science 330:1381-1385(2010).
CC   -!- FUNCTION: TRAP proteins are part of a complex whose function is to bind
CC       calcium to the ER membrane and thereby regulate the retention of ER
CC       resident proteins. May be involved in the recycling of the
CC       translocation apparatus after completion of the translocation process
CC       or may function as a membrane-bound chaperone facilitating folding of
CC       translocated proteins. {ECO:0000256|ARBA:ARBA00025620}.
CC   -!- SUBUNIT: Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-
CC       gamma. Interacts with palmitoylated calnexin (CALX), the interaction is
CC       required for efficient folding of glycosylated proteins.
CC       {ECO:0000256|ARBA:ARBA00025854}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004115}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the TRAP-alpha family.
CC       {ECO:0000256|ARBA:ARBA00006776}.
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DR   EMBL; FN653040; CBY19415.1; -; Genomic_DNA.
DR   EMBL; FN657694; CBY42967.1; -; Genomic_DNA.
DR   AlphaFoldDB; E4XE25; -.
DR   InParanoid; E4XE25; -.
DR   Proteomes; UP000001307; Unassembled WGS sequence.
DR   Proteomes; UP000011014; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR005595; TRAP_alpha.
DR   PANTHER; PTHR12924:SF0; TRANSLOCON-ASSOCIATED PROTEIN SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR12924; TRANSLOCON-ASSOCIATED PROTEIN, ALPHA SUBUNIT; 1.
DR   Pfam; PF03896; TRAP_alpha; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001307};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..252
FT                   /note="Translocon-associated protein subunit alpha"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007653909"
FT   TRANSMEM        185..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          229..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..252
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   252 AA;  27748 MW;  23C7A27DE2A1A5D2 CRC64;
     MKLLRRMLPI AILGLALVAK AEEFDEEIGD DTVQVNEVLD EDEGEDMGIV DEEESEVQIN
     TYWPEATITA GKVSEVLVSV KVASSAMNRY QFGIIEGGFH FPQDQSYKVQ NFSSIKYNRD
     LGSGQEATFL YPFVAAELAG GRSYGLQINL AYEADSSPPR QLFASVVNQT VEVNENLDNA
     AAEQFFIFMT FAAFAAIGFF FFASKFSSKK PKAAPVEVGT GGAADASWIP EIHMKKSDTP
     KTSPQSRRRK VD
//
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