ERGI2_HUMAN
ID ERGI2_HUMAN Reviewed; 377 AA.
AC Q96RQ1; A6NHH6; Q53GY2; Q8N2Q9; Q9BVV9; Q9NZA3;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Endoplasmic reticulum-Golgi intermediate compartment protein 2;
GN Name=ERGIC2; Synonyms=ERV41, PTX1; ORFNames=CDA14;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Prostate;
RX PubMed=11445006; DOI=10.1089/10445490152122460;
RA Kwok S.C.M., Liu X., Daskal I.;
RT "Molecular cloning, expression, localization, and gene organization of
RT PTX1, a human nuclear protein that is downregulated in prostate cancer.";
RL DNA Cell Biol. 20:349-357(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pheochromocytoma;
RA Song H., Gao G., Peng Y., Ren S., Chen Z., Han Z.;
RT "A novel gene expressed in human pheochromocytoma.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood vessel, and Cervix;
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 [8]
RP SUBCELLULAR LOCATION.
RX PubMed=15308636; DOI=10.1074/jbc.m406644200;
RA Breuza L., Halbeisen R., Jenoe P., Otte S., Barlowe C., Hong W.,
RA Hauri H.-P.;
RT "Proteomics of endoplasmic reticulum-Golgi intermediate compartment (ERGIC)
RT membranes from brefeldin A-treated HepG2 cells identifies ERGIC-32, a new
RT cycling protein that interacts with human Erv46.";
RL J. Biol. Chem. 279:47242-47253(2004).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH EEF1A1.
RX PubMed=17980171; DOI=10.1016/j.bbapap.2007.10.006;
RA Yang Y.F., Chou M.Y., Fan C.Y., Chen S.F., Lyu P.C., Liu C.C., Tseng T.L.;
RT "The possible interaction of CDA14 and protein elongation factor 1alpha.";
RL Biochim. Biophys. Acta 1784:312-318(2008).
RN [10]
RP IDENTIFICATION IN A COMPLEX WITH ERGIC1 AND ERGIC3, AND INTERACTION WITH
RP ERGIC3.
RX PubMed=31142615; DOI=10.1074/jbc.ra119.007435;
RA Yoo W., Cho E.B., Kim S., Yoon J.B.;
RT "The E3 ubiquitin ligase MARCH2 regulates ERGIC3-dependent trafficking of
RT secretory proteins.";
RL J. Biol. Chem. 294:10900-10912(2019).
CC -!- FUNCTION: Possible role in transport between endoplasmic reticulum and
CC Golgi. {ECO:0000250}.
CC -!- SUBUNIT: May form a heteromeric complex composed of ERGIC1, ERGIC2 and
CC ERGIC3 (PubMed:31142615). Interacts with ERGIC3, the interaction is
CC required for the stable expression of both proteins (PubMed:31142615).
CC May interact with EEF1A1 (PubMed:17980171).
CC {ECO:0000269|PubMed:17980171, ECO:0000269|PubMed:31142615}.
CC -!- INTERACTION:
CC Q96RQ1; Q9Y282: ERGIC3; NbExp=2; IntAct=EBI-4403663, EBI-781551;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment membrane; Multi-pass membrane protein. Golgi apparatus,
CC cis-Golgi network membrane; Multi-pass membrane protein. Endoplasmic
CC reticulum membrane; Multi-pass membrane protein. Cytoplasm. Nucleus.
CC Note=Cycles between the endoplasmic reticulum and the Golgi. According
CC to a report, localizes to the nucleus (PubMed:11445006). Another report
CC shows a partial localization in the nucleus (PubMed:17980171).
CC {ECO:0000269|PubMed:11445006, ECO:0000269|PubMed:17980171}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:11445006}.
CC -!- SIMILARITY: Belongs to the ERGIC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF61208.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF302767; AAK77355.1; -; mRNA.
DR EMBL; AK074520; BAC11037.1; -; mRNA.
DR EMBL; AF216751; AAF61208.1; ALT_FRAME; mRNA.
DR EMBL; AK222799; BAD96519.1; -; mRNA.
DR EMBL; AC009318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471094; EAW96592.1; -; Genomic_DNA.
DR EMBL; BC000887; AAH00887.2; -; mRNA.
DR EMBL; BC107794; AAI07795.1; -; mRNA.
DR CCDS; CCDS41765.1; -.
DR RefSeq; NP_057654.2; NM_016570.2.
DR AlphaFoldDB; Q96RQ1; -.
DR SMR; Q96RQ1; -.
DR BioGRID; 119441; 259.
DR ComplexPortal; CPX-7221; ERGIC2-ERGIC3 retrograde receptor complex.
DR IntAct; Q96RQ1; 21.
DR STRING; 9606.ENSP00000353270; -.
DR GlyGen; Q96RQ1; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q96RQ1; -.
DR MetOSite; Q96RQ1; -.
DR PhosphoSitePlus; Q96RQ1; -.
DR SwissPalm; Q96RQ1; -.
DR BioMuta; ERGIC2; -.
DR DMDM; 108935982; -.
DR EPD; Q96RQ1; -.
DR jPOST; Q96RQ1; -.
DR MassIVE; Q96RQ1; -.
DR MaxQB; Q96RQ1; -.
DR PaxDb; Q96RQ1; -.
DR PeptideAtlas; Q96RQ1; -.
DR PRIDE; Q96RQ1; -.
DR ProteomicsDB; 78002; -.
DR Antibodypedia; 7205; 215 antibodies from 28 providers.
DR DNASU; 51290; -.
DR Ensembl; ENST00000360150.9; ENSP00000353270.4; ENSG00000087502.19.
DR GeneID; 51290; -.
DR KEGG; hsa:51290; -.
DR MANE-Select; ENST00000360150.9; ENSP00000353270.4; NM_016570.3; NP_057654.2.
DR UCSC; uc001riv.4; human.
DR CTD; 51290; -.
DR DisGeNET; 51290; -.
DR GeneCards; ERGIC2; -.
DR HGNC; HGNC:30208; ERGIC2.
DR HPA; ENSG00000087502; Low tissue specificity.
DR MIM; 612236; gene.
DR neXtProt; NX_Q96RQ1; -.
DR OpenTargets; ENSG00000087502; -.
DR PharmGKB; PA143485457; -.
DR VEuPathDB; HostDB:ENSG00000087502; -.
DR eggNOG; KOG2667; Eukaryota.
DR GeneTree; ENSGT00530000063113; -.
DR HOGENOM; CLU_034705_4_1_1; -.
DR InParanoid; Q96RQ1; -.
DR OMA; TYQYSVK; -.
DR OrthoDB; 1318747at2759; -.
DR PhylomeDB; Q96RQ1; -.
DR TreeFam; TF317192; -.
DR PathwayCommons; Q96RQ1; -.
DR SignaLink; Q96RQ1; -.
DR BioGRID-ORCS; 51290; 52 hits in 1080 CRISPR screens.
DR ChiTaRS; ERGIC2; human.
DR GeneWiki; ERGIC2; -.
DR GenomeRNAi; 51290; -.
DR Pharos; Q96RQ1; Tbio.
DR PRO; PR:Q96RQ1; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q96RQ1; protein.
DR Bgee; ENSG00000087502; Expressed in buccal mucosa cell and 200 other tissues.
DR ExpressionAtlas; Q96RQ1; baseline and differential.
DR Genevisible; Q96RQ1; HS.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0061852; C:retrograte transporter complex, Golgi to ER; IPI:ComplexPortal.
DR GO; GO:1990351; C:transporter complex; IPI:ComplexPortal.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:ComplexPortal.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:WormBase.
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 Cytoplasm; Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW Membrane; Nucleus; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..377
FT /note="Endoplasmic reticulum-Golgi intermediate compartment
FT protein 2"
FT /id="PRO_0000239382"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..319
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 51
FT /note="E -> K (in Ref. 1; AAK77355)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="D -> Y (in Ref. 1; AAK77355)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="N -> S (in Ref. 4; BAD96519)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 42549 MW; 3820FA05515634ED CRC64;
MRRLNRKKTL SLVKELDAFP KVPESYVETS ASGGTVSLIA FTTMALLTIM EFSVYQDTWM
KYEYEVDKDF SSKLRINIDI TVAMKCQYVG ADVLDLAETM VASADGLVYE PTVFDLSPQQ
KEWQRMLQLI QSRLQEEHSL QDVIFKSAFK STSTALPPRE DDSSQSPNAC RIHGHLYVNK
VAGNFHITVG KAIPHPRGHA HLAALVNHES YNFSHRIDHL SFGELVPAII NPLDGTEKIA
IDHNQMFQYF ITVVPTKLHT YKISADTHQF SVTERERIIN HAAGSHGVSG IFMKYDLSSL
MVTVTEEHMP FWQFFVRLCG IVGGIFSTTG MLHGIGKFIV EIICCRFRLG SYKPVNSVPF
EDGHTDNHLP LLENNTH
