ID   ERGI3_MACFA             Reviewed;         382 AA.
AC   Q4R8X1;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Endoplasmic reticulum-Golgi intermediate compartment protein 3;
GN   Name=ERGIC3; ORFNames=QtsA-11239;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (MAR-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}.
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DR   EMBL; AB168326; BAE00450.1; -; mRNA.
DR   RefSeq; NP_001270982.1; NM_001284053.1.
DR   AlphaFoldDB; Q4R8X1; -.
DR   SMR; Q4R8X1; -.
DR   STRING; 9541.XP_005568911.1; -.
DR   GeneID; 101866368; -.
DR   CTD; 51614; -.
DR   eggNOG; KOG2667; Eukaryota.
DR   Proteomes; UP000233100; 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..382
FT                   /note="Endoplasmic reticulum-Golgi intermediate compartment
FT                   protein 3"
FT                   /id="PRO_0000239388"
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..340
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        341..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        362..382
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        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   382 AA;  42966 MW;  ADF98F5974D74239 CRC64;
     MEALGKLKQF DAYPKTLEDF RVKTCGGATV TIVSGLLMLL LFLSELQYYL TTEVHPELYV
     DKSRGDKLKI NIDVLFPHMP CAYLSIDAMD VAGEQQLDVE HNLFKQRLDK DGTPVSSEAE
     RHELGKVEVT VFGPDSLDPD RCESCYGAEA EDIKCCNTCE DVREAYRRRG AFKNPDTIEQ
     CRREGFSQKM QEQKNEGCQV YGFLEVNKVA GNFHFAPGKS FQQSHVHVHD LQSFGLDNIN
     MTHYIQHLSF GEDYPGIVNP LDHTNVTAPQ ASMMFQYFVK VVPTVYMKVD GEVLRTNQFS
     VTRHEKVANG LLGDQGLPGV FVLYELSPMM VKLTEKHRSF THFLTGVCAI IGGMFTVAGL
     IDSLIYHSAR AIQKKIDLGK TT