ERGI3_BOVIN
ID ERGI3_BOVIN Reviewed; 383 AA.
AC Q5EAE0; Q0V8E8; Q3T0M8; Q58CR6; Q58CZ8;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Endoplasmic reticulum-Golgi intermediate compartment protein 3;
GN Name=ERGIC3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2005) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5EAE0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5EAE0-2; Sequence=VSP_019213, VSP_019214;
CC Name=3;
CC IsoId=Q5EAE0-3; Sequence=VSP_019215, VSP_019216;
CC -!- SIMILARITY: Belongs to the ERGIC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX46646.1; Type=Erroneous initiation; Evidence={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; BT020628; AAX08645.1; -; mRNA.
DR EMBL; BT020629; AAX08646.1; -; mRNA.
DR EMBL; BT020688; AAX08705.1; -; mRNA.
DR EMBL; BT021799; AAX46646.1; ALT_INIT; mRNA.
DR EMBL; BT021881; AAX46728.1; -; mRNA.
DR EMBL; BT026271; ABG81427.1; -; mRNA.
DR EMBL; BC102326; AAI02327.1; -; mRNA.
DR RefSeq; NP_001029525.2; NM_001034353.2. [Q5EAE0-1]
DR AlphaFoldDB; Q5EAE0; -.
DR SMR; Q5EAE0; -.
DR STRING; 9913.ENSBTAP00000008782; -.
DR PRIDE; Q5EAE0; -.
DR Ensembl; ENSBTAT00000008782; ENSBTAP00000008782; ENSBTAG00000006670. [Q5EAE0-1]
DR GeneID; 509546; -.
DR KEGG; bta:509546; -.
DR CTD; 51614; -.
DR VEuPathDB; HostDB:ENSBTAG00000006670; -.
DR GeneTree; ENSGT00530000063113; -.
DR InParanoid; Q5EAE0; -.
DR OMA; IGNFHIA; -.
DR OrthoDB; 1318747at2759; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000006670; Expressed in theca cell and 109 other tissues.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0061852; C:retrograte transporter complex, Golgi to ER; IEA:Ensembl.
DR GO; GO:0043621; F:protein self-association; IEA:Ensembl.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
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; Alternative splicing; Endoplasmic reticulum;
KW ER-Golgi transport; Glycoprotein; Golgi apparatus; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..383
FT /note="Endoplasmic reticulum-Golgi intermediate compartment
FT protein 3"
FT /id="PRO_0000239387"
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"
FT VAR_SEQ 229..231
FT /note="VHD -> GLR (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_019213"
FT VAR_SEQ 232..383
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_019214"
FT VAR_SEQ 240..283
FT /note="INMTHYIRHLSFGEDYPGIVNPLDHTNVTAPQASMMFQYFVKVV -> VRTR
FT WKPWRVDGGGGLVAAFILCRDILGWGSRYRTMNHGLTGAV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_019215"
FT VAR_SEQ 284..383
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_019216"
SQ SEQUENCE 383 AA; 43375 MW; E97E82112E8D835E CRC64;
MEALGKLKQF DAYPKTLEDF RVKTCGGATV TIVSGLLMLL LFLSELQYYL TTEVHPELYV
DKSRGDKLKI NINVLFPHMP CAYLSIDAMD VAGEQQLDVE HNLFKKRLDK DGFPVSSEAE
RHELGKVEVK VFDPDSLDPD RCESCYGAEM EDIKCCNSCE DVREAYRRRG WAFKNPDTIE
QCRREGFSQK MQEQKNEGCQ VYGFLEVNKV AGNFHFAPGK SFQQSHVHVH DLQSFGLDNI
NMTHYIRHLS FGEDYPGIVN PLDHTNVTAP QASMMFQYFV KVVPTVYMKV DGEVLRTNQF
SVTRHEKVAN GLMGDQGLPG VFVLYELSPM MVKLTEKHRS FTHFLTGVCA IIGGMFTVAG
LIDSLIYHSA RAIQKKIDLG KTT
