ID D3TQU8_GLOMM Unreviewed; 282 AA.
AC D3TQU8;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Translocon-associated protein subunit alpha {ECO:0000256|ARBA:ARBA00020280};
DE AltName: Full=Signal sequence receptor subunit alpha {ECO:0000256|ARBA:ARBA00031071};
OS Glossina morsitans morsitans (Savannah tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=37546 {ECO:0000313|EMBL:ADD20076.1};
RN [1] {ECO:0000313|EMBL:ADD20076.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland {ECO:0000313|EMBL:ADD20076.1};
RX PubMed=20353571; DOI=10.1186/1471-2164-11-213;
RA Alves-Silva J., Ribeiro J.M., Van Den Abbeele J., Attardo G., Hao Z.,
RA Haines L.R., Soares M.B., Berriman M., Aksoy S., Lehane M.J.;
RT "An insight into the sialome of Glossina morsitans morsitans.";
RL BMC Genomics 11:213-213(2010).
RN [2] {ECO:0000313|EMBL:ADD20076.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland {ECO:0000313|EMBL:ADD20076.1};
RG International Glossina Genome Initiative;
RA da Silva J., Ribeiro J.M.C., Abbeele J.V., Attardo G., Hao Z., Haines L.R.,
RA Soares M.B., Berriman M., Aksoy S., Lehane M.J.;
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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; EZ423800; ADD20076.1; -; mRNA.
DR AlphaFoldDB; D3TQU8; -.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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..282
FT /note="Translocon-associated protein subunit alpha"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003051049"
FT TRANSMEM 185..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 246..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 282 AA; 31087 MW; AC831F6020EFC123 CRC64;
MKDHLVIFLL ILPTIICTFN AHNKLFVYAE DEAIEDDIVE VEVEDGAVTG DDADADDDTE
SLSSSSPYAD TFLLFTKPTY KPGQQLDLPG GKPVEFLIGF TNKGTNEFII ETNFSAVAYN
REVKPGLEAT VSYSFMPSDQ FAGRPFGLNI ALNYRDGNGV QYSEAVFNET VLISEVDEGL
DGETFFLYVL LAGIVVLLLV IGQQYLLGSS GKRKRAAAKK IIETGTTNDS TIDYEWLPQE
TLRALQKSSP KNKISKISPK PIKPSSPKQS QSPKQKKTVK QQ
//
