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Q5XJY5 (COPD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coatomer subunit delta
Alternative name(s):
Archain
Delta-coat protein
Short name=Delta-COP
Gene names
Name:Arcn1
Synonyms:Copd
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subunit structure

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

Subcellular location

Cytoplasm By similarity. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmic vesicle › COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it By similarity.

Sequence similarities

Belongs to the adaptor complexes medium subunit family. Delta-COP subfamily.

Contains 1 MHD (mu homology) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 511511Coatomer subunit delta
PRO_0000193842

Regions

Domain268 – 511244MHD

Amino acid modifications

Modified residue2331N6-acetyllysine By similarity
Modified residue3091N6-acetyllysine By similarity
Modified residue4931Phosphoserine By similarity

Experimental info

Sequence conflict3011I → T in AAH83152. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q5XJY5 [UniParc].

Last modified June 28, 2011. Version 2.
Checksum: 4C20F48A75330DC8

FASTA51157,229
        10         20         30         40         50         60 
MVLLAAAVCT KAGKAIVSRQ FVEMTRTRIE GLLAAFPKLM NTGKQHTFVE TESVRYVYQP 

        70         80         90        100        110        120 
MEKLYMVLIT TKNSNILEDL ETLRLFSRVI PEYCRALEEN EISEHCFDLI FAFDEIVALG 

       130        140        150        160        170        180 
YRENVNLAQI RTFTEMDSHE EKVFRAVRET QEREAKAEMR RKAKELQQAR RDAERQGKKA 

       190        200        210        220        230        240 
PGFGGFGSSA VSGGSTAAMI TETIIETDKP KVAPAPARPS GPSKALKLGA KGKEVDNFVD 

       250        260        270        280        290        300 
KLKSEGETIM SSNMGKRTSE ATKVHAPPIN MESVHMKIEE KITLTCGRDG GLQNMELHGM 

       310        320        330        340        350        360 
IMLRISDDKF GRIRLHVENE DKKGVQLQTH PNVDKKLFTA ESLIGLKNPE KSFPVNSDVG 

       370        380        390        400        410        420 
VLKWRLQTTE ESFIPLTINC WPSESGNGCD VNIEYELQED NLELNDVVIT IPLPSGVGAP 

       430        440        450        460        470        480 
VIGEIDGEYR HDSRRNTLEW CLPVIDAKNK SGSLEFSIPG QPNDFFPVQV SFISKKNYCN 

       490        500        510 
IQVTKVTQVD GNSPVRFSTE TTFLVDKYEI L

« Hide

References

[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00313558.
RefSeqNP_666097.3. NM_145985.4.
UniGeneMm.371682.
Mm.465799.

3D structure databases

ProteinModelPortalQ5XJY5.
ModBaseSearch...

PTM databases

PhosphoSiteQ5XJY5.

2D gel databases

REPRODUCTION-2DPAGEQ5XJY5.

Proteomic databases

PaxDbQ5XJY5.
PRIDEQ5XJY5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034607; ENSMUSP00000034607; ENSMUSG00000032096.
GeneID213827.
KEGGmmu:213827.

Organism-specific databases

CTD372.
MGIMGI:2387591. Arcn1.

Phylogenomic databases

eggNOGNOG309668.
GeneTreeENSGT00390000017207.
HOGENOMHOG000203984.
HOVERGENHBG005381.
InParanoidQ91W48.
OMANNDVGVL.
OrthoDBEOG4FBHSQ.

Gene expression databases

ArrayExpressQ5XJY5.
BgeeQ5XJY5.
CleanExMM_ARCN1.
GenevestigatorQ5XJY5.
GermOnlineENSMUSG00000032096. Mus musculus.

Family and domain databases

InterProIPR022775. AP_mu_sigma_su.
IPR008968. Clathrin_mu_C.
IPR027059. Coatomer_dsu.
IPR011012. Longin-like_dom.
[Graphical view]
PANTHERPTHR10121. PTHR10121. 1 hit.
PfamPF00928. Adap_comp_sub. 1 hit.
PF01217. Clat_adaptor_s. 1 hit.
[Graphical view]
SUPFAMSSF49447. AP50. 1 hit.
SSF64356. Longin_like. 1 hit.
PROSITEPS51072. MHD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio374120.
SOURCESearch...

Entry information

Entry nameCOPD_MOUSE
AccessionPrimary (citable) accession number: Q5XJY5
Secondary accession number(s): Q91W48
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: June 28, 2011
Last modified: May 1, 2013
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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