Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Coatomer subunit delta

Gene

ARCN1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 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: Ensembl
  • cerebellar Purkinje cell layer maturation Source: Ensembl
  • intra-Golgi vesicle-mediated transport Source: UniProtKB
  • pigmentation Source: Ensembl
  • protein transport Source: UniProtKB-KW
  • retrograde vesicle-mediated transport, Golgi to ER Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-BTA-6807878. COPI-mediated anterograde transport.
R-BTA-6811434. COPI-dependent Golgi-to-ER retrograde traffic.

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 15

Subcellular locationi

GO - Cellular componenti

  • COPI vesicle coat Source: UniProtKB
  • endoplasmic reticulum Source: Ensembl
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_0000193840Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP53619.
PRIDEiP53619.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
Copb1P235143EBI-620432,EBI-620488From a different organism.

Protein-protein interaction databases

IntActiP53619. 2 interactions.
STRINGi9913.ENSBTAP00000008799.

Structurei

Secondary structure

1
511
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi268 – 2703Combined sources
Beta strandi273 – 28614Combined sources
Beta strandi292 – 30615Combined sources
Helixi308 – 3103Combined sources
Beta strandi311 – 3199Combined sources
Beta strandi326 – 3294Combined sources
Helixi335 – 3417Combined sources
Beta strandi346 – 3483Combined sources
Beta strandi355 – 3573Combined sources
Beta strandi359 – 36810Combined sources
Helixi371 – 3733Combined sources
Beta strandi375 – 3839Combined sources
Beta strandi389 – 3979Combined sources
Beta strandi404 – 4129Combined sources
Beta strandi415 – 4173Combined sources
Beta strandi421 – 43212Combined sources
Turni433 – 4364Combined sources
Beta strandi437 – 4415Combined sources
Beta strandi451 – 4599Combined sources
Helixi462 – 4654Combined sources
Beta strandi467 – 47610Combined sources
Beta strandi481 – 4888Combined sources
Turni489 – 4913Combined sources
Beta strandi498 – 51013Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4O8QX-ray2.15A/B268-511[»]
ProteinModelPortaliP53619.
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.
InParanoidiP53619.
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.

P53619-1 [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 PGFGGFGSST VSGGSTTSMI
210 220 230 240 250
TETIIETDKP KVAPAPARPS GPSKALKLGA KGKEVDNFVD KLKSEGENII
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
SGSLEFSIAG QPNDFFPVQV SFISKKNYCN IQVTKVTQVD GNSPVRFSTE
510
TTFLVDKYEI L
Length:511
Mass (Da):57,274
Last modified:October 1, 1996 - v1
Checksum:i6A285798F252CC7F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94265 mRNA. Translation: CAA63941.1.
RefSeqiNP_001181942.1. NM_001195013.1.
UniGeneiBt.23103.

Genome annotation databases

EnsembliENSBTAT00000008799; ENSBTAP00000008799; ENSBTAG00000006690.
GeneIDi533078.
KEGGibta:533078.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94265 mRNA. Translation: CAA63941.1.
RefSeqiNP_001181942.1. NM_001195013.1.
UniGeneiBt.23103.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4O8QX-ray2.15A/B268-511[»]
ProteinModelPortaliP53619.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP53619. 2 interactions.
STRINGi9913.ENSBTAP00000008799.

Proteomic databases

PaxDbiP53619.
PRIDEiP53619.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000008799; ENSBTAP00000008799; ENSBTAG00000006690.
GeneIDi533078.
KEGGibta:533078.

Organism-specific databases

CTDi372.

Phylogenomic databases

eggNOGiKOG2635. Eukaryota.
ENOG410XRH2. LUCA.
GeneTreeiENSGT00390000017207.
HOGENOMiHOG000203984.
HOVERGENiHBG005381.
InParanoidiP53619.
OMAiRNILEWC.
OrthoDBiEOG7CG6ZW.
TreeFamiTF105760.

Enzyme and pathway databases

ReactomeiR-BTA-6807878. COPI-mediated anterograde transport.
R-BTA-6811434. COPI-dependent Golgi-to-ER retrograde traffic.

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. "Architecture of coatomer: molecular characterization of delta-COP and protein interactions within the complex."
    Faulstich D., Auerbach S., Orci L., Ravazzola M., Wegehingel S., Lottspeich F., Stenbeck G., Harter C., Wieland F.T., Tschochner H.
    J. Cell Biol. 135:53-61(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-511.
    Tissue: Brain.

Entry informationi

Entry nameiCOPD_BOVIN
AccessioniPrimary (citable) accession number: P53619
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 105 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.