ID A0A0V0UFA2_9BILA Unreviewed; 298 AA.
AC A0A0V0UFA2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 16.
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 Name=SSR1 {ECO:0000313|EMBL:KRX50054.1};
GN ORFNames=T05_5051 {ECO:0000313|EMBL:KRX50054.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX50054.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX50054.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX50054.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX50054.1}.
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DR EMBL; JYDJ01000009; KRX50054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0UFA2; -.
DR STRING; 144512.A0A0V0UFA2; -.
DR Proteomes; UP000055048; 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:UP000055048};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 209..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 269..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 298 AA; 33385 MW; E4F19092822F210C CRC64;
MQCYSMRNNQ VESCKMIFGK WFITAVCLLL ISIPVRNVLS ADEDDDDALV EEEGDKLKAG
GKSLGDSDDE EVLEGLAPSP DIEAAMLFTE PPNSKELPSG KPAHMLISFF NGGIDEYFVD
SIQAFLKYPT DYSYNVHNYS VRSYHQAVYP DTEASFEYSM MAFDSLAGRP FGLVVLVDYK
LADGREFRST VFNETVHIVE EESAFNPEMI FLVMVFVIIG CLVAAFAYQF ISGKSRKHVV
KKHAEVEMGT TNAGDVDLDW IPKQILAMSE RSRQPTQKTS PRMRKNGKNA HQAKARAD
//
