ID   ERGI1_HUMAN             Reviewed;         290 AA.
AC   Q969X5; Q9H0L0; Q9H2J2; Q9ULN9;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=Endoplasmic reticulum-Golgi intermediate compartment protein 1;
DE   AltName: Full=ER-Golgi intermediate compartment 32 kDa protein;
DE            Short=ERGIC-32;
GN   Name=ERGIC1; Synonyms=ERGIC32, KIAA1181 {ECO:0000312|EMBL:BAA86495.1};
GN   ORFNames=HT034;
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] {ECO:0000312|EMBL:BAA86495.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain {ECO:0000312|EMBL:BAA86495.1};
RX   PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA   Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT   "Characterization of cDNA clones selected by the GeneMark analysis from
RT   size-fractionated cDNA libraries from human brain.";
RL   DNA Res. 6:329-336(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Hypothalamus;
RX   PubMed=10931946; DOI=10.1073/pnas.160270997;
RA   Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA   Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA   Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA   Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA   Chen M.-D., Chen J.-L.;
RT   "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT   and full-length cDNA cloning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Testis;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000305, ECO:0000312|EMBL:AAH14490.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lymph {ECO:0000312|EMBL:AAH12766.1}, and Pancreas
RC   {ECO:0000312|EMBL:AAH14490.1};
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   [6] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 177-199 AND 233-241, SUBCELLULAR LOCATION, TOPOLOGY,
RP   GLYCOSYLATION, AND INTERACTION WITH ERGIC3.
RC   TISSUE=Hepatoma {ECO:0000269|PubMed:15308636};
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   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [11]
RP   IDENTIFICATION IN A COMPLEX WITH ERGIC2 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).
RN   [12]
RP   INVOLVEMENT IN AMC2, AND VARIANT AMC2 GLU-98.
RX   PubMed=28317099; DOI=10.1111/cge.13018;
RA   Reinstein E., Drasinover V., Lotan R., Gal-Tanamy M., Bolocan Nachman I.,
RA   Eyal E., Jaber L., Magal N., Shohat M.;
RT   "Mutations in ERGIC1 cause Arthrogryposis multiplex congenita, neuropathic
RT   type.";
RL   Clin. Genet. 93:160-163(2018).
CC   -!- FUNCTION: Possible role in transport between endoplasmic reticulum and
CC       Golgi. {ECO:0000303|PubMed:15308636}.
CC   -!- SUBUNIT: May form a heteromeric complex composed of ERGIC1, ERGIC2 and
CC       ERGIC3 (PubMed:31142615). Within the complex, the interaction with
CC       ERGIC3 is direct (PubMed:31142615). Interacts with ERGIC3/ERV46
CC       (PubMed:15308636). {ECO:0000269|PubMed:15308636,
CC       ECO:0000269|PubMed:31142615}.
CC   -!- INTERACTION:
CC       Q969X5; Q08426: EHHADH; NbExp=3; IntAct=EBI-781527, EBI-2339219;
CC       Q969X5; Q9Y282: ERGIC3; NbExp=4; IntAct=EBI-781527, EBI-781551;
CC       Q969X5; O14901: KLF11; NbExp=3; IntAct=EBI-781527, EBI-948266;
CC       Q969X5; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-781527, EBI-2811583;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:15308636}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:15308636}. Endoplasmic reticulum-Golgi intermediate
CC       compartment membrane {ECO:0000269|PubMed:15308636}; Multi-pass membrane
CC       protein {ECO:0000269|PubMed:15308636}. Golgi apparatus membrane
CC       {ECO:0000269|PubMed:15308636}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:15308636}. Note=Cycles between the endoplasmic
CC       reticulum and the Golgi.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q969X5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q969X5-2; Sequence=VSP_011560;
CC       Name=3;
CC         IsoId=Q969X5-3; Sequence=VSP_011561, VSP_011562, VSP_011563,
CC                                  VSP_011564;
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15308636,
CC       ECO:0000269|PubMed:19159218}.
CC   -!- DISEASE: Arthrogryposis multiplex congenita 2, neurogenic type (AMC2)
CC       [MIM:208100]: A form of arthrogryposis multiplex congenita, a
CC       heterogeneous group of disorders characterized by multiple joint
CC       contractures resulting, in some cases, from reduced or absent fetal
CC       movements. AMC2 is due to a neurogenic defect and is characterized by
CC       congenital immobility of the limbs with fixation of multiple joints,
CC       and muscle wasting. AMC2 transmission pattern is consistent with
CC       autosomal recessive inheritance in several families. Penetrance may be
CC       incomplete in females. {ECO:0000269|PubMed:28317099}. Note=The disease
CC       is caused by variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the ERGIC family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG44724.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAA86495.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB033007; BAA86495.1; ALT_INIT; mRNA.
DR   EMBL; AF267855; AAG44724.1; ALT_FRAME; mRNA.
DR   EMBL; AL136753; CAB66687.1; -; mRNA.
DR   EMBL; CR533474; CAG38505.1; -; mRNA.
DR   EMBL; BC012766; AAH12766.1; -; mRNA.
DR   EMBL; BC014490; AAH14490.1; -; mRNA.
DR   CCDS; CCDS34292.1; -. [Q969X5-1]
DR   RefSeq; NP_001026881.1; NM_001031711.2. [Q969X5-1]
DR   RefSeq; XP_006714955.1; XM_006714892.1.
DR   AlphaFoldDB; Q969X5; -.
DR   SMR; Q969X5; -.
DR   BioGRID; 121458; 307.
DR   IntAct; Q969X5; 34.
DR   MINT; Q969X5; -.
DR   STRING; 9606.ENSP00000377374; -.
DR   GlyCosmos; Q969X5; 2 sites, 1 glycan.
DR   GlyGen; Q969X5; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q969X5; -.
DR   PhosphoSitePlus; Q969X5; -.
DR   SwissPalm; Q969X5; -.
DR   BioMuta; ERGIC1; -.
DR   DMDM; 51701446; -.
DR   EPD; Q969X5; -.
DR   jPOST; Q969X5; -.
DR   MassIVE; Q969X5; -.
DR   MaxQB; Q969X5; -.
DR   PaxDb; 9606-ENSP00000377374; -.
DR   PeptideAtlas; Q969X5; -.
DR   ProteomicsDB; 75870; -. [Q969X5-1]
DR   ProteomicsDB; 75871; -. [Q969X5-2]
DR   ProteomicsDB; 75872; -. [Q969X5-3]
DR   Pumba; Q969X5; -.
DR   TopDownProteomics; Q969X5-1; -. [Q969X5-1]
DR   Antibodypedia; 17012; 98 antibodies from 18 providers.
DR   DNASU; 57222; -.
DR   Ensembl; ENST00000393784.8; ENSP00000377374.3; ENSG00000113719.17. [Q969X5-1]
DR   Ensembl; ENST00000687901.1; ENSP00000509817.1; ENSG00000113719.17. [Q969X5-2]
DR   Ensembl; ENST00000693299.1; ENSP00000509429.1; ENSG00000113719.17. [Q969X5-2]
DR   GeneID; 57222; -.
DR   KEGG; hsa:57222; -.
DR   MANE-Select; ENST00000393784.8; ENSP00000377374.3; NM_001031711.3; NP_001026881.1.
DR   UCSC; uc003mbw.5; human. [Q969X5-1]
DR   AGR; HGNC:29205; -.
DR   CTD; 57222; -.
DR   DisGeNET; 57222; -.
DR   GeneCards; ERGIC1; -.
DR   HGNC; HGNC:29205; ERGIC1.
DR   HPA; ENSG00000113719; Low tissue specificity.
DR   MalaCards; ERGIC1; -.
DR   MIM; 208100; phenotype.
DR   MIM; 617946; gene.
DR   neXtProt; NX_Q969X5; -.
DR   OpenTargets; ENSG00000113719; -.
DR   Orphanet; 1143; Neurogenic arthrogryposis multiplex congenita.
DR   PharmGKB; PA143485456; -.
DR   VEuPathDB; HostDB:ENSG00000113719; -.
DR   eggNOG; KOG2667; Eukaryota.
DR   GeneTree; ENSGT00530000063113; -.
DR   HOGENOM; CLU_034705_0_1_1; -.
DR   InParanoid; Q969X5; -.
DR   OMA; DDMGRHE; -.
DR   OrthoDB; 506854at2759; -.
DR   PhylomeDB; Q969X5; -.
DR   TreeFam; TF354253; -.
DR   PathwayCommons; Q969X5; -.
DR   SignaLink; Q969X5; -.
DR   SIGNOR; Q969X5; -.
DR   BioGRID-ORCS; 57222; 11 hits in 1161 CRISPR screens.
DR   ChiTaRS; ERGIC1; human.
DR   GenomeRNAi; 57222; -.
DR   Pharos; Q969X5; Tbio.
DR   PRO; PR:Q969X5; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q969X5; Protein.
DR   Bgee; ENSG00000113719; Expressed in stromal cell of endometrium and 181 other cell types or tissues.
DR   ExpressionAtlas; Q969X5; baseline and differential.
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:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:HGNC-UCL.
DR   GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:HGNC-UCL.
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; ENDOPLASMIC RETICULUM-GOLGI INTERMEDIATE COMPARTMENT PROTEIN; 1.
DR   PANTHER; PTHR10984:SF36; ENDOPLASMIC RETICULUM-GOLGI INTERMEDIATE COMPARTMENT PROTEIN 1; 1.
DR   Pfam; PF07970; COPIIcoated_ERV; 1.
DR   Pfam; PF13850; ERGIC_N; 1.
DR   Genevisible; Q969X5; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing; Disease variant;
KW   Endoplasmic reticulum; ER-Golgi transport; Glycoprotein; Golgi apparatus;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..290
FT                   /note="Endoplasmic reticulum-Golgi intermediate compartment
FT                   protein 1"
FT                   /id="PRO_0000087023"
FT   TOPO_DOM        1..26
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..254
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        255..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        276..290
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15308636,
FT                   ECO:0000269|PubMed:19159218"
FT   VAR_SEQ         1..92
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10931946"
FT                   /id="VSP_011560"
FT   VAR_SEQ         1..45
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11230166, ECO:0000303|Ref.4"
FT                   /id="VSP_011561"
FT   VAR_SEQ         46..52
FT                   /note="GFITTEV -> MERWAMR (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11230166, ECO:0000303|Ref.4"
FT                   /id="VSP_011562"
FT   VAR_SEQ         127..204
FT                   /note="PGNFHVSTHSATAQPQNPDMTHVIHKLSFGDTLQVQNIHGAFNALGGADRLT
FT                   SNPLASHDYILKIVPTVYEDKSGKQR -> WKPCLSPFYLLPFPAVSPLPGNWLWRHSL
FT                   DLTLTQPPASEGSCPAAWPFLLRIWMGVQAPWGFKPLMAGSGRSYSSLQ (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11230166, ECO:0000303|Ref.4"
FT                   /id="VSP_011563"
FT   VAR_SEQ         205..290
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11230166, ECO:0000303|Ref.4"
FT                   /id="VSP_011564"
FT   VARIANT         98
FT                   /note="V -> E (in AMC2; uncertain significance;
FT                   dbSNP:rs1554112524)"
FT                   /evidence="ECO:0000269|PubMed:28317099"
FT                   /id="VAR_080480"
SQ   SEQUENCE   290 AA;  32592 MW;  5B13C7B8B9F8E51D CRC64;
     MPFDFRRFDI YRKVPKDLTQ PTYTGAIISI CCCLFILFLF LSELTGFITT EVVNELYVDD
     PDKDSGGKID VSLNISLPNL HCELVGLDIQ DEMGRHEVGH IDNSMKIPLN NGAGCRFEGQ
     FSINKVPGNF HVSTHSATAQ PQNPDMTHVI HKLSFGDTLQ VQNIHGAFNA LGGADRLTSN
     PLASHDYILK IVPTVYEDKS GKQRYSYQYT VANKEYVAYS HTGRIIPAIW FRYDLSPITV
     KYTERRQPLY RFITTICAII GGTFTVAGIL DSCIFTASEA WKKIQLGKMH
//