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Protein

Coatomer subunit delta

Gene

Arcn1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • adult locomotory behavior Source: MGI
  • cerebellar Purkinje cell layer maturation Source: MGI
  • Golgi vesicle transport Source: MGI
  • pigmentation Source: MGI
  • protein transport Source: UniProtKB-KW
  • retrograde vesicle-mediated transport, Golgi to ER Source: InterPro
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-199997. COPI Mediated Transport.
R-MMU-6807878. COPI-mediated anterograde transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Coatomer subunit delta
Alternative name(s):
Archain
Delta-coat protein
Short name:
Delta-COP
Gene namesi
Name:Arcn1
Synonyms:Copd
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:2387591. Arcn1.

Subcellular locationi

GO - Cellular componenti

  • COPI-coated vesicle Source: MGI
  • COPI vesicle coat Source: InterPro
  • cytoplasm Source: MGI
  • endoplasmic reticulum Source: MGI
  • Golgi apparatus Source: MGI
  • intracellular membrane-bounded organelle Source: MGI
  • membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 511510Coatomer subunit deltaPRO_0000193842Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei233 – 2331N6-acetyllysineBy similarity
Modified residuei241 – 2411N6-acetyllysineCombined sources
Modified residuei309 – 3091N6-acetyllysineBy similarity
Modified residuei351 – 3511N6-acetyllysineCombined sources
Modified residuei493 – 4931PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ5XJY5.
MaxQBiQ5XJY5.
PaxDbiQ5XJY5.
PRIDEiQ5XJY5.

2D gel databases

REPRODUCTION-2DPAGEQ5XJY5.

PTM databases

iPTMnetiQ5XJY5.
PhosphoSiteiQ5XJY5.
SwissPalmiQ5XJY5.

Expressioni

Gene expression databases

BgeeiQ5XJY5.
CleanExiMM_ARCN1.
GenevisibleiQ5XJY5. MM.

Interactioni

Subunit structurei

Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits.By similarity

Protein-protein interaction databases

BioGridi229475. 2 interactions.
IntActiQ5XJY5. 3 interactions.
MINTiMINT-1857447.
STRINGi10090.ENSMUSP00000034607.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5A1Uelectron microscopy13.00H1-511[»]
5A1Velectron microscopy21.00H/P/Y1-511[»]
5A1Welectron microscopy18.00H1-511[»]
5A1Xelectron microscopy23.00H/P/Q1-511[»]
5A1Yelectron microscopy21.00H/P1-511[»]
ProteinModelPortaliQ5XJY5.
SMRiQ5XJY5. Positions 1-134, 270-511.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini271 – 511241MHDPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 MHD (mu homology) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2635. Eukaryota.
ENOG410XRH2. LUCA.
GeneTreeiENSGT00390000017207.
HOGENOMiHOG000203984.
HOVERGENiHBG005381.
InParanoidiQ5XJY5.
OMAiRNILEWC.
OrthoDBiEOG7CG6ZW.
TreeFamiTF105760.

Family and domain databases

InterProiIPR022775. AP_mu_sigma_su.
IPR027059. Coatomer_dsu.
IPR011012. Longin-like_dom.
IPR028565. MHD.
[Graphical view]
PANTHERiPTHR10121. PTHR10121. 1 hit.
PfamiPF00928. Adap_comp_sub. 1 hit.
PF01217. Clat_adaptor_s. 1 hit.
[Graphical view]
SUPFAMiSSF49447. SSF49447. 1 hit.
SSF64356. SSF64356. 1 hit.
PROSITEiPS51072. MHD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5XJY5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLLAAAVCT KAGKAIVSRQ FVEMTRTRIE GLLAAFPKLM NTGKQHTFVE
60 70 80 90 100
TESVRYVYQP MEKLYMVLIT TKNSNILEDL ETLRLFSRVI PEYCRALEEN
110 120 130 140 150
EISEHCFDLI FAFDEIVALG YRENVNLAQI RTFTEMDSHE EKVFRAVRET
160 170 180 190 200
QEREAKAEMR RKAKELQQAR RDAERQGKKA PGFGGFGSSA VSGGSTAAMI
210 220 230 240 250
TETIIETDKP KVAPAPARPS GPSKALKLGA KGKEVDNFVD KLKSEGETIM
260 270 280 290 300
SSNMGKRTSE ATKVHAPPIN MESVHMKIEE KITLTCGRDG GLQNMELHGM
310 320 330 340 350
IMLRISDDKF GRIRLHVENE DKKGVQLQTH PNVDKKLFTA ESLIGLKNPE
360 370 380 390 400
KSFPVNSDVG VLKWRLQTTE ESFIPLTINC WPSESGNGCD VNIEYELQED
410 420 430 440 450
NLELNDVVIT IPLPSGVGAP VIGEIDGEYR HDSRRNTLEW CLPVIDAKNK
460 470 480 490 500
SGSLEFSIPG QPNDFFPVQV SFISKKNYCN IQVTKVTQVD GNSPVRFSTE
510
TTFLVDKYEI L
Length:511
Mass (Da):57,229
Last modified:June 28, 2011 - v2
Checksum:i4C20F48A75330DC8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti301 – 3011I → T in AAH83152 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK028556 mRNA. Translation: BAC26007.1.
CH466522 Genomic DNA. Translation: EDL25614.1.
BC017124 mRNA. Translation: AAH17124.1.
BC023728 mRNA. Translation: AAH23728.1.
BC033387 mRNA. Translation: AAH33387.1.
BC034754 mRNA. Translation: AAH34754.1.
BC083152 mRNA. Translation: AAH83152.1.
CCDSiCCDS40602.1.
RefSeqiNP_666097.3. NM_145985.4.
UniGeneiMm.371682.

Genome annotation databases

EnsembliENSMUST00000034607; ENSMUSP00000034607; ENSMUSG00000032096.
GeneIDi213827.
KEGGimmu:213827.
UCSCiuc009pei.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK028556 mRNA. Translation: BAC26007.1.
CH466522 Genomic DNA. Translation: EDL25614.1.
BC017124 mRNA. Translation: AAH17124.1.
BC023728 mRNA. Translation: AAH23728.1.
BC033387 mRNA. Translation: AAH33387.1.
BC034754 mRNA. Translation: AAH34754.1.
BC083152 mRNA. Translation: AAH83152.1.
CCDSiCCDS40602.1.
RefSeqiNP_666097.3. NM_145985.4.
UniGeneiMm.371682.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5A1Uelectron microscopy13.00H1-511[»]
5A1Velectron microscopy21.00H/P/Y1-511[»]
5A1Welectron microscopy18.00H1-511[»]
5A1Xelectron microscopy23.00H/P/Q1-511[»]
5A1Yelectron microscopy21.00H/P1-511[»]
ProteinModelPortaliQ5XJY5.
SMRiQ5XJY5. Positions 1-134, 270-511.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi229475. 2 interactions.
IntActiQ5XJY5. 3 interactions.
MINTiMINT-1857447.
STRINGi10090.ENSMUSP00000034607.

PTM databases

iPTMnetiQ5XJY5.
PhosphoSiteiQ5XJY5.
SwissPalmiQ5XJY5.

2D gel databases

REPRODUCTION-2DPAGEQ5XJY5.

Proteomic databases

EPDiQ5XJY5.
MaxQBiQ5XJY5.
PaxDbiQ5XJY5.
PRIDEiQ5XJY5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034607; ENSMUSP00000034607; ENSMUSG00000032096.
GeneIDi213827.
KEGGimmu:213827.
UCSCiuc009pei.2. mouse.

Organism-specific databases

CTDi372.
MGIiMGI:2387591. Arcn1.

Phylogenomic databases

eggNOGiKOG2635. Eukaryota.
ENOG410XRH2. LUCA.
GeneTreeiENSGT00390000017207.
HOGENOMiHOG000203984.
HOVERGENiHBG005381.
InParanoidiQ5XJY5.
OMAiRNILEWC.
OrthoDBiEOG7CG6ZW.
TreeFamiTF105760.

Enzyme and pathway databases

ReactomeiR-MMU-199997. COPI Mediated Transport.
R-MMU-6807878. COPI-mediated anterograde transport.

Miscellaneous databases

NextBioi374120.
PROiQ5XJY5.
SOURCEiSearch...

Gene expression databases

BgeeiQ5XJY5.
CleanExiMM_ARCN1.
GenevisibleiQ5XJY5. MM.

Family and domain databases

InterProiIPR022775. AP_mu_sigma_su.
IPR027059. Coatomer_dsu.
IPR011012. Longin-like_dom.
IPR028565. MHD.
[Graphical view]
PANTHERiPTHR10121. PTHR10121. 1 hit.
PfamiPF00928. Adap_comp_sub. 1 hit.
PF01217. Clat_adaptor_s. 1 hit.
[Graphical view]
SUPFAMiSSF49447. SSF49447. 1 hit.
SSF64356. SSF64356. 1 hit.
PROSITEiPS51072. MHD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Skin.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and FVB/N.
    Tissue: Embryonic germ cell, Eye and Mammary tumor.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-241 AND LYS-351, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiCOPD_MOUSE
AccessioniPrimary (citable) accession number: Q5XJY5
Secondary accession number(s): Q91W48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: June 28, 2011
Last modified: March 16, 2016
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.