ID   ERGI3_PONAB             Reviewed;         383 AA.
AC   Q5R8G3;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Endoplasmic reticulum-Golgi intermediate compartment protein 3;
GN   Name=ERGIC3;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Possible role in transport between endoplasmic reticulum and
CC       Golgi. Positively regulates trafficking of the secretory proteins
CC       alpha1-antitrypsin/SERPINA1 and HP/haptoglobin (By similarity).
CC       {ECO:0000250|UniProtKB:Q9Y282}.
CC   -!- SUBUNIT: Forms homodimers (By similarity). May form a heteromeric
CC       complex composed of ERGIC1, ERGIC2 and ERGIC3 (By similarity). Within
CC       the complex, the interaction with ERGIC1 is direct (By similarity).
CC       Interacts with ERGIC1/ERGIC32 (By similarity). Interacts with ERGIC2,
CC       the interaction is required for the stable expression of both proteins
CC       (By similarity). Interacts with MARCHF2 (By similarity). Interacts with
CC       SERPINA1/alpha1-antitrypsin and HP/haptoglobin (By similarity).
CC       {ECO:0000250|UniProtKB:Q9Y282}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC       compartment membrane {ECO:0000250}; Multi-pass membrane protein
CC       {ECO:0000250}. Golgi apparatus, cis-Golgi network membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic
CC       reticulum membrane {ECO:0000250}; Multi-pass membrane protein
CC       {ECO:0000250}. Note=Cycles between the endoplasmic reticulum and the
CC       Golgi. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ERGIC family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR859789; CAH91947.1; -; mRNA.
DR   RefSeq; NP_001126130.1; NM_001132658.1.
DR   AlphaFoldDB; Q5R8G3; -.
DR   SMR; Q5R8G3; -.
DR   STRING; 9601.ENSPPYP00000012233; -.
DR   GeneID; 100173087; -.
DR   KEGG; pon:100173087; -.
DR   CTD; 51614; -.
DR   eggNOG; KOG2667; Eukaryota.
DR   InParanoid; Q5R8G3; -.
DR   OrthoDB; 1318747at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   InterPro; IPR045888; Erv.
DR   InterPro; IPR012936; Erv_C.
DR   InterPro; IPR039542; Erv_N.
DR   PANTHER; PTHR10984; PTHR10984; 1.
DR   Pfam; PF07970; COPIIcoated_ERV; 1.
DR   Pfam; PF13850; ERGIC_N; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Endoplasmic reticulum; ER-Golgi transport; Glycoprotein;
KW   Golgi apparatus; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..383
FT                   /note="Endoplasmic reticulum-Golgi intermediate compartment
FT                   protein 3"
FT                   /id="PRO_0000239389"
FT   TOPO_DOM        1..25
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        47..341
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        342..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        363..383
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..25
FT                   /note="Required for MARCHF2-mediated degradation"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y282"
FT   SITE            8
FT                   /note="Ubiquitinated; by MARCHF2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y282"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y282"
FT   MOD_RES         116
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y282"
FT   CARBOHYD        266
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   383 AA;  43252 MW;  7FD73418D162B496 CRC64;
     MEALGKLKQF DAYPKTLEDF RVKTCGGATV TIVSGLLMLL LFLSELQYYL TTEVHPELYV
     DKSRGDKLKI NIDVLFPHMP CAYLSIDAMD VAGEQQLDVE HNLFKQRLDK DGIPVSSEAE
     RHELGKVEVT VFDPDSLDPD RCESCYGAEA EDIKCCNTCE DVRETYRRRG WAFKNPDTIE
     QCRREGFSQK MQEQKNEGCQ VYGFLEVNKV AGNFHFAPGK SFQQSHVHVH DLQSFGLDNI
     NMTHYIQHLS FGEDYPGIVN PLDHTNVTAP QASMMFQYFV KVVPTVYMKV DGEVLRTNQF
     SVTRHEKVAN GLLGDQGLPG VFVLYELSPM MVKLTEKHRS FTHFLTGVCA IIGGMFTVAG
     LIDSLIYHSA RAIQKKIDLG KTT