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Protein

Coatomer subunit delta

Gene

ARCN1

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 - Biological processi

Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, 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
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
Proteomesi
  • UP000001595 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

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_0000193843Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei223 – 2231PhosphoserineBy similarity
Modified residuei233 – 2331N6-acetyllysineBy similarity
Modified residuei241 – 2411N6-acetyllysineBy similarity
Modified residuei244 – 2441PhosphoserineBy similarity
Modified residuei309 – 3091N6-acetyllysineBy similarity
Modified residuei351 – 3511N6-acetyllysineBy similarity
Modified residuei493 – 4931PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiQ5RA77.

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

STRINGi9601.ENSPPYP00000004511.

Structurei

3D structure databases

ProteinModelPortaliQ5RA77.
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.
HOVERGENiHBG005381.
InParanoidiQ5RA77.

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.

Q5RA77-1 [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
SSSMGKRTSE ASKMHAPPIN MESVHMKIEE KITLTCGRDG GLQNMELHGM
310 320 330 340 350
IMLRISDDKY 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
SGSLEFSIAG QPNDFFPVQV SFVSKKNYCN IQVTKVTQVD GNSPVRFSTE
510
TTFLVDKYEI L
Length:511
Mass (Da):57,196
Last modified:December 21, 2004 - v1
Checksum:i4ED02CD2D1296F75
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR858065 mRNA. Translation: CAH90304.1.
CR859142 mRNA. Translation: CAH91333.1.
RefSeqiNP_001125788.1. NM_001132316.1.

Genome annotation databases

GeneIDi100172716.
KEGGipon:100172716.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR858065 mRNA. Translation: CAH90304.1.
CR859142 mRNA. Translation: CAH91333.1.
RefSeqiNP_001125788.1. NM_001132316.1.

3D structure databases

ProteinModelPortaliQ5RA77.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000004511.

Proteomic databases

PRIDEiQ5RA77.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100172716.
KEGGipon:100172716.

Organism-specific databases

CTDi372.

Phylogenomic databases

eggNOGiKOG2635. Eukaryota.
ENOG410XRH2. LUCA.
HOVERGENiHBG005381.
InParanoidiQ5RA77.

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 German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain cortex.

Entry informationi

Entry nameiCOPD_PONAB
AccessioniPrimary (citable) accession number: Q5RA77
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: December 21, 2004
Last modified: July 6, 2016
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.