ID M2QX16_CERS8 Unreviewed; 208 AA.
AC M2QX16;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 22-FEB-2023, entry version 27.
DE RecName: Full=Endoplasmic reticulum transmembrane protein {ECO:0000256|RuleBase:RU367026};
GN ORFNames=CERSUDRAFT_120122 {ECO:0000313|EMBL:EMD31071.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD31071.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD31071.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD31071.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
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 EMBL; KB445824; EMD31071.1; -; Genomic_DNA.
DR AlphaFoldDB; M2QX16; -.
DR STRING; 914234.M2QX16; -.
DR HOGENOM; CLU_087648_0_1_1; -.
DR OrthoDB; 1332764at2759; -.
DR Proteomes; UP000016930; 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, ECO:0000256|SAM:Coils};
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:UP000016930};
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 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 107..130
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367026"
FT DOMAIN 1..138
FT /note="BAP29/BAP31 transmembrane"
FT /evidence="ECO:0000259|Pfam:PF05529"
FT DOMAIN 155..207
FT /note="Bap31/Bap29 cytoplasmic coiled-coil"
FT /evidence="ECO:0000259|Pfam:PF18035"
FT COILED 157..198
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 208 AA; 23416 MW; DF1B6A8E3A8CB762 CRC64;
MTVYYTLTFM LLASEMATFC ALVAPLPHAL RKRLFRFLSE SPLVAKLAYG VKIAFIFVAI
LFVDAVQRMW RVTAEADLAK TSAPGAQDVR AETNFAARKF YSQRNTYLTG FTLFLSLVLT
RTFYILLDLI HTQEEYAKLK QQNKASPSGA VPEAKQIQEL KQQLAAAEAK VRDYDVVKKQ
AQQNAAEYDR LASEFNAKTG AVSDKRKD
//
