ID   GET2_VANPO              Reviewed;         294 AA.
AC   A7TRN7;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Golgi to ER traffic protein 2 {ECO:0000255|HAMAP-Rule:MF_03114};
GN   Name=GET2 {ECO:0000255|HAMAP-Rule:MF_03114}; ORFNames=Kpol_411p4;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
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: Required for the post-translational delivery of tail-anchored
CC       (TA) proteins to the endoplasmic reticulum. Together with GET1, acts as
CC       a membrane receptor for soluble GET3, which recognizes and selectively
CC       binds the transmembrane domain of TA proteins in the cytosol. The GET
CC       complex cooperates with the HDEL receptor ERD2 to mediate the ATP-
CC       dependent retrieval of resident ER proteins that contain a C-terminal
CC       H-D-E-L retention signal from the Golgi to the ER. {ECO:0000255|HAMAP-
CC       Rule:MF_03114}.
CC   -!- SUBUNIT: Component of the Golgi to ER traffic (GET) complex, which is
CC       composed of GET1, GET2 and GET3. Within the complex, GET1 and GET2 form
CC       a heterotetramer which is stabilized by phosphatidylinositol binding
CC       and which binds to the GET3 homodimer. {ECO:0000255|HAMAP-
CC       Rule:MF_03114}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000255|HAMAP-Rule:MF_03114}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_03114}. Golgi apparatus membrane
CC       {ECO:0000255|HAMAP-Rule:MF_03114}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_03114}.
CC   -!- SIMILARITY: Belongs to the GET2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03114}.
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DR   EMBL; DS480484; EDO15059.1; -; Genomic_DNA.
DR   RefSeq; XP_001642917.1; XM_001642867.1.
DR   AlphaFoldDB; A7TRN7; -.
DR   STRING; 436907.A7TRN7; -.
DR   EnsemblFungi; EDO15059; EDO15059; Kpol_411p4.
DR   GeneID; 5543101; -.
DR   KEGG; vpo:Kpol_411p4; -.
DR   eggNOG; ENOG502QW0H; Eukaryota.
DR   HOGENOM; CLU_066477_0_0_1; -.
DR   InParanoid; A7TRN7; -.
DR   OMA; ALQYWDV; -.
DR   OrthoDB; 1324439at2759; -.
DR   PhylomeDB; A7TRN7; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043529; C:GET complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045048; P:protein insertion into ER membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   HAMAP; MF_03114; Get2; 1.
DR   InterPro; IPR014802; GET2.
DR   InterPro; IPR028143; Get2/sif1.
DR   PANTHER; PTHR28263; PTHR28263; 1.
DR   Pfam; PF08690; GET2; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..294
FT                   /note="Golgi to ER traffic protein 2"
FT                   /id="PRO_0000388640"
FT   TOPO_DOM        1..166
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT   TOPO_DOM        188..205
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT   TRANSMEM        206..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT   TOPO_DOM        226..272
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT   TOPO_DOM        294
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT   REGION          1..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   294 AA;  33597 MW;  BC451D7B20DC0406 CRC64;
     MSSELSETEK RKLIRERRQK KFSNGGASAR LNRITGQAEN SQLDTESPLD SKSSRETTPT
     VTKVDSNTEE MDELLENIAT SPSNKVEKSQ KKKEQATSPQ ETIDPELEIF KQLAENQQND
     VSTPDLFSML RSMKDNMAKS AATDTNPPLE PVDQQLLDYN NYLINNLKVW SIIFKWCFFL
     IPYLFALTRS EPISFLPEQF SNPSNFFMIF LSFEIVATSI YFQKLQNIEK SNKINGFQSN
     NKIVNLVSLI PEGVLPVPDI KGKVIMALQY WDVFSMFLTD ICFVLVMMGL FKLI