ID A0A1X7VSC0_AMPQE Unreviewed; 228 AA.
AC A0A1X7VSC0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Endoplasmic reticulum transmembrane protein {ECO:0000256|RuleBase:RU367026};
GN Name=105314241 {ECO:0000313|EnsemblMetazoa:Aqu2.1.42715_001};
OS Amphimedon queenslandica (Sponge).
OC Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC Haplosclerida; Niphatidae; Amphimedon.
OX NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:Aqu2.1.42715_001, ECO:0000313|Proteomes:UP000007879};
RN [1] {ECO:0000313|Proteomes:UP000007879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20686567; DOI=10.1038/nature09201;
RA Srivastava M., Simakov O., Chapman J., Fahey B., Gauthier M.E., Mitros T.,
RA Richards G.S., Conaco C., Dacre M., Hellsten U., Larroux C., Putnam N.H.,
RA Stanke M., Adamska M., Darling A., Degnan S.M., Oakley T.H.,
RA Plachetzki D.C., Zhai Y., Adamski M., Calcino A., Cummins S.F.,
RA Goodstein D.M., Harris C., Jackson D.J., Leys S.P., Shu S., Woodcroft B.J.,
RA Vervoort M., Kosik K.S., Manning G., Degnan B.M., Rokhsar D.S.;
RT "The Amphimedon queenslandica genome and the evolution of animal
RT complexity.";
RL Nature 466:720-726(2010).
RN [2] {ECO:0000313|Proteomes:UP000007879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., Glavina del Rio T.,
RA Bruce D., Barry K., Pitluck S., Srivastava M., Simakov O., Chapman J.,
RA Mitros T., Hellsten U., Putnam N.H., Fahey B., Gauthier M., Larroux C.,
RA Richards G.S., Stanke M., Adamska M., Darling A., Dacre M., Degnan S.M.,
RA Zhai Y., Adamski M., Calcino A., Cummins S.F., Goodstein D.M., Harris C.,
RA Shu S., Woodcroft B., Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.;
RT "The genome of the haplosclerid demosponge Amphimedon queenslandica and the
RT evolution of animal complexity.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:Aqu2.1.42715_001}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2017) to UniProtKB.
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|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367026}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
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|ARBA:ARBA00007956, ECO:0000256|RuleBase:RU367026}.
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DR RefSeq; XP_019855950.1; XM_020000391.1.
DR AlphaFoldDB; A0A1X7VSC0; -.
DR STRING; 400682.A0A1X7VSC0; -.
DR EnsemblMetazoa; Aqu2.1.42715_001; Aqu2.1.42715_001; Aqu2.1.42715.
DR GeneID; 105314241; -.
DR KEGG; aqu:105314241; -.
DR eggNOG; KOG1962; Eukaryota.
DR InParanoid; A0A1X7VSC0; -.
DR OMA; NKCFFTM; -.
DR OrthoDB; 2882163at2759; -.
DR Proteomes; UP000007879; 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 Gene3D; 1.20.5.110; -; 1.
DR InterPro; IPR008417; BAP29/BAP31.
DR InterPro; IPR040463; BAP29/BAP31_N.
DR InterPro; IPR041672; Bap31/Bap29_C.
DR PANTHER; PTHR12701; BCR-ASSOCIATED PROTEIN, BAP; 1.
DR PANTHER; PTHR12701:SF18; ENDOPLASMIC RETICULUM TRANSMEMBRANE PROTEIN; 1.
DR Pfam; PF05529; Bap31; 1.
DR Pfam; PF18035; Bap31_Bap29_C; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU367026};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW ECO:0000256|RuleBase:RU367026};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367026};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU367026};
KW Reference proteome {ECO:0000313|Proteomes:UP000007879};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367026};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367026};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367026}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367026"
FT TRANSMEM 46..64
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367026"
FT TRANSMEM 102..123
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367026"
FT DOMAIN 1..134
FT /note="BAP29/BAP31 transmembrane"
FT /evidence="ECO:0000259|Pfam:PF05529"
FT DOMAIN 176..228
FT /note="Bap31/Bap29 cytoplasmic coiled-coil"
FT /evidence="ECO:0000259|Pfam:PF18035"
FT REGION 147..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 228 AA; 26701 MW; 5E01A5CA9BEBAB28 CRC64;
MTLQWQVVAF SLYAEIFLTI ILILPLLKPS TWKYIFSIRI FSGLKALWKT IFFASLLILV
VLFVDSIRTM NKYNDASIDK PGMTLDTKLD IRLKQCRGQR NFYITGFSLF LMFIIYRLVV
LLFERASLEA NHQAALAQAQ SVSRELQRRL DQSGKKETET ESEQPTEEEK EKYLTRITEL
EKEVKKVLAD RDAMRKQAES LHAEYDRLSG EYQKIQKEQD GEEDKKEQ
//
