ID A7TT08_VANPO Unreviewed; 194 AA.
AC A7TT08;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 22-FEB-2023, entry version 56.
DE RecName: Full=Endoplasmic reticulum transmembrane protein {ECO:0000256|RuleBase:RU367026};
GN ORFNames=Kpol_262p4 {ECO:0000313|EMBL:EDO14599.1};
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN [1] {ECO:0000313|EMBL:EDO14599.1, ECO:0000313|Proteomes:UP000000267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC -!- FUNCTION: May play a role in anterograde transport of membrane proteins
CC from the endoplasmic reticulum to the Golgi.
CC {ECO:0000256|RuleBase:RU367026}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU367026}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU367026}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the BCAP29/BCAP31 family.
CC {ECO:0000256|RuleBase:RU367026}.
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DR EMBL; DS480533; EDO14599.1; -; Genomic_DNA.
DR RefSeq; XP_001642457.1; XM_001642407.1.
DR AlphaFoldDB; A7TT08; -.
DR STRING; 436907.A7TT08; -.
DR GeneID; 5542619; -.
DR KEGG; vpo:Kpol_262p4; -.
DR eggNOG; KOG1962; Eukaryota.
DR HOGENOM; CLU_087648_1_0_1; -.
DR InParanoid; A7TT08; -.
DR OMA; RNMYISG; -.
DR OrthoDB; 1969211at2759; -.
DR PhylomeDB; A7TT08; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:UniProtKB-UniRule.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IEA:UniProtKB-UniRule.
DR InterPro; IPR008417; BAP29/BAP31.
DR InterPro; IPR040463; BAP29/BAP31_N.
DR PANTHER; PTHR12701; BCR-ASSOCIATED PROTEIN, BAP; 1.
DR PANTHER; PTHR12701:SF19; ENDOPLASMIC RETICULUM TRANSMEMBRANE PROTEIN 1-RELATED; 1.
DR Pfam; PF05529; Bap31; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU367026};
KW ER-Golgi transport {ECO:0000256|RuleBase:RU367026};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367026};
KW Protein transport {ECO:0000256|RuleBase:RU367026};
KW Reference proteome {ECO:0000313|Proteomes:UP000000267};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367026};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367026}; Transport {ECO:0000256|RuleBase:RU367026}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367026"
FT TRANSMEM 47..66
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367026"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367026"
FT DOMAIN 1..137
FT /note="BAP29/BAP31 transmembrane"
FT /evidence="ECO:0000259|Pfam:PF05529"
FT REGION 174..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 194 AA; 22340 MW; 04F5958D57BFFEF0 CRC64;
MSIYFTLLFV ALTLEMGTLF FLVLPLPFRL RKSMCTVYDR LYYNQQFRTV GAILGVLVGM
LFADSWKRAN VHVSTYHDQN SNEMTNDAGS LITPVQVLTS RAYNQRNVYI SGFILYFVLC
IITVMSIVRR LVKYQSLINE SDKNIDDDRL LQELKSKKTS LEGLKSQIAN LEKQFDQTND
AKNEPVSELD KKDN
//
