ERGI3_MOUSE
ID ERGI3_MOUSE Reviewed; 383 AA.
AC Q9CQE7; B7ZCN9; Q6PGA7;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Endoplasmic reticulum-Golgi intermediate compartment protein 3;
DE AltName: Full=Serologically defined breast cancer antigen NY-BR-84 homolog;
GN Name=Ergic3; Synonyms=Erv46, Sdbcag84;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Liver, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N-3; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12663859; DOI=10.1073/pnas.0730885100;
RA Orci L., Ravazzola M., Mack G.J., Barlowe C., Otte S.;
RT "Mammalian Erv46 localizes to the endoplasmic reticulum-Golgi intermediate
RT compartment and to cis-Golgi cisternae.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4586-4591(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000269|PubMed:12663859}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:12663859}. Golgi apparatus, cis-Golgi
CC network membrane {ECO:0000269|PubMed:12663859}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:12663859}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12663859}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12663859}. Note=Cycles between the endoplasmic
CC reticulum and the Golgi.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CQE7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CQE7-2; Sequence=VSP_019209, VSP_019210;
CC -!- TISSUE SPECIFICITY: Expression is particularly strong in liver, kidney
CC and brain but is almost undetectable in heart.
CC {ECO:0000269|PubMed:12663859}.
CC -!- SIMILARITY: Belongs to the ERGIC family. {ECO:0000305}.
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DR EMBL; AK009350; BAB26233.1; -; mRNA.
DR EMBL; AK013942; BAB29073.1; -; mRNA.
DR EMBL; AK050285; BAC34166.1; -; mRNA.
DR EMBL; AL833786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC043720; AAH43720.1; -; mRNA.
DR EMBL; BC057130; AAH57130.1; -; mRNA.
DR CCDS; CCDS16959.1; -. [Q9CQE7-1]
DR CCDS; CCDS89572.1; -. [Q9CQE7-2]
DR RefSeq; NP_079792.1; NM_025516.4. [Q9CQE7-1]
DR AlphaFoldDB; Q9CQE7; -.
DR SMR; Q9CQE7; -.
DR BioGRID; 211417; 3.
DR IntAct; Q9CQE7; 1.
DR MINT; Q9CQE7; -.
DR STRING; 10090.ENSMUSP00000006035; -.
DR GlyConnect; 2285; 2 N-Linked glycans (1 site).
DR GlyGen; Q9CQE7; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; Q9CQE7; -.
DR PhosphoSitePlus; Q9CQE7; -.
DR SwissPalm; Q9CQE7; -.
DR EPD; Q9CQE7; -.
DR MaxQB; Q9CQE7; -.
DR PaxDb; Q9CQE7; -.
DR PeptideAtlas; Q9CQE7; -.
DR PRIDE; Q9CQE7; -.
DR ProteomicsDB; 275773; -. [Q9CQE7-1]
DR ProteomicsDB; 275774; -. [Q9CQE7-2]
DR Antibodypedia; 3001; 256 antibodies from 31 providers.
DR DNASU; 66366; -.
DR Ensembl; ENSMUST00000006035; ENSMUSP00000006035; ENSMUSG00000005881. [Q9CQE7-1]
DR Ensembl; ENSMUST00000088650; ENSMUSP00000086025; ENSMUSG00000005881. [Q9CQE7-2]
DR GeneID; 66366; -.
DR KEGG; mmu:66366; -.
DR UCSC; uc008nlx.1; mouse. [Q9CQE7-1]
DR UCSC; uc008nly.1; mouse. [Q9CQE7-2]
DR CTD; 51614; -.
DR MGI; MGI:1913616; Ergic3.
DR VEuPathDB; HostDB:ENSMUSG00000005881; -.
DR eggNOG; KOG2667; Eukaryota.
DR GeneTree; ENSGT00530000063113; -.
DR HOGENOM; CLU_034705_1_0_1; -.
DR InParanoid; Q9CQE7; -.
DR OMA; IGNFHIA; -.
DR OrthoDB; 1318747at2759; -.
DR PhylomeDB; Q9CQE7; -.
DR TreeFam; TF300739; -.
DR BioGRID-ORCS; 66366; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Ergic3; mouse.
DR PRO; PR:Q9CQE7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9CQE7; protein.
DR Bgee; ENSMUSG00000005881; Expressed in molar tooth and 259 other tissues.
DR ExpressionAtlas; Q9CQE7; baseline and differential.
DR Genevisible; Q9CQE7; MM.
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:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISS:HGNC-UCL.
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; ISO:MGI.
DR GO; GO:1990351; C:transporter complex; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; ISO:MGI.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:HGNC-UCL.
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 1: Evidence at protein 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_0000097641"
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
FT /note="V -> VHAVEI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019209"
FT VAR_SEQ 239
FT /note="N -> NPSDCLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019210"
SQ SEQUENCE 383 AA; 43208 MW; 97EF08712201E0C2 CRC64;
MEALGKLKQF DAYPKTLEDF RVKTCGGATV TIVSGLLMLL LFLSELQYYL TTEVHPELYV
DKSRGDKLKI NIDVLFPHMP CAYLSIDAMD VAGEQQLDVE HNLFKKRLDK DGVPVSSEAE
RHELGKVEVT VFDPNSLDPN RCESCYGAES EDIKCCNSCE DVREAYRRRG WAFKNPDTIE
QCRREGFSQK MQEQKNEGCQ VYGFLEVNKV AGNFHFAPGK SFQQSHVHVH DLQSFGLDNI
NMTHYIKHLS FGEDYPGIVN PLDHTNVTAP QASMMFQYFV KVVPTVYMKV DGEVLRTNQF
SVTRHEKVAN GLLGDQGLPG VFVLYELSPM MVKLTEKHRS FTHFLTGVCA IIGGMFTVAG
LIDSLIYHSA RAIQKKIDLG KTT
