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Q9JIF7 (COPB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. 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

Names and origin

Protein namesRecommended name:
Coatomer subunit beta
Alternative name(s):
Beta-coat protein
Short name=Beta-COP
Gene names
Name:Copb1
Synonyms:Copb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length953 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. Involved in the Golgi disassembly and reassembly processes during cell cycle. Involved in autophagy by playing a role in early endosome function. Plays a role in organellar compartmentalization of secretory compartments including endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling endosomes, and in biosynthetic transport of CAV1 By similarity. Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins in cortical neurons. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis. Ref.6 Ref.7

Subunit structure

Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits By similarity. Interacts with CAPN8. Interacts with SCYL1 and PRKCE By similarity. Interacts with COPG1 By similarity. Interacts with ARF1 (myristoylated); this interaction is required for binding of COPB1 to Golgi membranes By similarity. Interacts (via trunk domain) with ARF1 (via switch I region); the interaction is direct By similarity. Interacts with KCNK2 (via N-terminus); this interaction increases the channel-mediated whole cell currents and promotes plasma membrane expression of KCNK2 By similarity. Interacts with STX17 By similarity. Ref.5

Subcellular location

Cytoplasm By similarity. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmic vesicleCOPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane By similarity. Endoplasmic reticulum-Golgi intermediate compartment 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. Proteolytic cleavage by CAPN8 triggers translocation from Golgi to cytoplasm. Found in perinuclear vesicular-tubular clusters (VTCs) and in the Golgi region where associated with vesicles, buds and rims of the Golgi stack By similarity. Occasionally present at the trans-side of Golgi, but mainly present at the cis- Golgi side in transitional areas (TA), on so-called peripheral elements (PE) consisting of tubules and vesicles located between the cup-shaped transitional elements (TE) of the rough endoplasmic reticulum (RER) and the cis-most Golgi cisternae By similarity. Present in cytoplasm, not associated with visible coats or membranes, with a minor fraction present on small clusters of tubules and vesicles By similarity. Some association with high-density and low-density microsomes and mitochondria/nuclei fraction By similarity. Very little found in plasma membrane fraction By similarity. Ref.5 Ref.8

Tissue specificity

Predominantly expressed in the upper one-third of the oxyntic mucosa and in most regions of the pyloric mucosa (Ref.5). Ubiquitiously expressed including platelet, liver, heart, spleen, lung and kidney (Ref.1). Ref.1 Ref.5

Post-translational modification

Proteolytically cleaved between Ser-528 and Ser-529 by CAPN8.

Miscellaneous

Brefeldin A induces dissociation from the Golgi of the beta-COP and presumably the other coatomer subunits.

Sequence similarities

Contains 6 HEAT repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 953952Coatomer subunit beta
PRO_0000193834

Regions

Repeat96 – 13136HEAT 1
Repeat132 – 16837HEAT 2
Repeat240 – 27637HEAT 3
Repeat277 – 31438HEAT 4
Repeat316 – 35338HEAT 5
Repeat396 – 43338HEAT 6

Amino acid modifications

Modified residue21N-acetylthreonine By similarity
Modified residue4941N6-acetyllysine Ref.9

Experimental info

Sequence conflict7571T → I in BAE29109. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9JIF7 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 4CD5407AD87ACB4B

FASTA953107,066
        10         20         30         40         50         60 
MTAAENVCYT LINVPMDSEP PSEISLKNDL EKGDVKSKTE ALKKVIIMIL NGEKLPGLLM 

        70         80         90        100        110        120 
TIIRFVLPLQ DHTIKKLLLV FWEIVPKTTP DGRLLHEMIL VCDAYRKDLQ HPNEFIRGST 

       130        140        150        160        170        180 
LRFLCKLKEA ELLEPLMPAI RACLEHRHSY VRRNAVLAIY TIYRNFEHLI PDAPELIHDF 

       190        200        210        220        230        240 
LVNEKDASCK RNAFMMLIHA DQDRALDYLS TCIDQVQTFG DILQLVIVEL IYKVCHANPS 

       250        260        270        280        290        300 
ERARFIRCIY NLLQSSSPAV KYEAAGTLVT LSSAPTAIKA AAQCYIDLII KESDNNVKLI 

       310        320        330        340        350        360 
VLDRLVELKE HPAHERVLQD LVMDILRVLS TPDLEVRKKT LQLALDLVSS RNVEELVIVL 

       370        380        390        400        410        420 
KKEVIKTNNV SEHEDTDKYR QLLVRTLHSC SVRFPDMAAN VIPVLMEFLS DSNEAAAADV 

       430        440        450        460        470        480 
LEFVREAIQR FDNLRMLIVE KMLEVFHAIK SVKIYRGALW ILGEYCSTKE DIQSVMTEVR 

       490        500        510        520        530        540 
RSLGEIPIVE SEIKKEAGEL KPEEEITVGP VQKLVTEMGT YATQSALSSS RPTKKEEDRP 

       550        560        570        580        590        600 
PLRGFLLDGD FFVAASLATT LTKIALRYVA LVQEKKKQNS FVAEAMLLMA TILHLGKSSL 

       610        620        630        640        650        660 
PKKPITDDDV DRISLCLKVL SECSPLMNDI FNKECRQSLS QMLSAKLEEE KLSQKKESEK 

       670        680        690        700        710        720 
RNVTVQPDDP ISFMQLTAKN EMNCKEDQFQ LSLLAAMGNT QRKEAADPLA SKLNKVTQLT 

       730        740        750        760        770        780 
GFSDPVYAEA YVHVNQYDIV LDVLVVNQTS DTLQNCTLEL ATLGDLKLVE KPSPLTLAPH 

       790        800        810        820        830        840 
DFANIKANVK VASTENGIIF GNIVYDVSGA ASDRNCVVLS DIHIDIMDYI QPATCTDAEF 

       850        860        870        880        890        900 
RQMWAEFEWE NKVTVNTNMT DLNDYLQHIL KSTNMKCLTP EKALSGYCGF MAANLYARSI 

       910        920        930        940        950 
FGEDALANVS IEKPVHQGPD AAVTGHIRIR AKSQGMALSL GDKINLSQKK TSL 

« Hide

References

« Hide 'large scale' references
[1]"cDNA sequence and mapping of the mouse Copb gene encoding the beta subunit of the COPI coatomer complex."
Li W., Elliott R.W., Novak E.K., Swank R.T.
Somat. Cell Mol. Genet. 25:177-183(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: C57BL/6.
Tissue: Bone marrow.
[2]"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 and NOD.
Tissue: Bone marrow, Pituitary and Spleen.
[3]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].
[4]"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: Czech II.
Tissue: Mammary gland.
[5]"Stomach-specific calpain, nCL-2, localizes in mucus cells and proteolyzes the beta-subunit of coatomer complex, beta-COP."
Hata S., Koyama S., Kawahara H., Doi N., Maeda T., Toyama-Sorimachi N., Abe K., Suzuki K., Sorimachi H.
J. Biol. Chem. 281:11214-11224(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CAPN8, SUBCELLULAR LOCATION, PTM, TISSUE SPECIFICITY.
[6]"Copb1-facilitated axonal transport and translation of kappa opioid-receptor mRNA."
Bi J., Tsai N.P., Lu H.Y., Loh H.H., Wei L.N.
Proc. Natl. Acad. Sci. U.S.A. 104:13810-13815(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"COPI complex is a regulator of lipid homeostasis."
Beller M., Sztalryd C., Southall N., Bell M., Jackle H., Auld D.S., Oliver B.
PLoS Biol. 6:E292-E292(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Novel Golgi protein, GoPro49, is a specific dental follicle marker."
Takatalo M.S., Tummers M., Thesleff I., Roennholm R.
J. Dent. Res. 88:534-538(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"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-494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF231925 mRNA. Translation: AAF76856.1.
AK149828 mRNA. Translation: BAE29109.1.
AK152222 mRNA. Translation: BAE31049.1.
AK161544 mRNA. Translation: BAE36453.1.
AK172214 mRNA. Translation: BAE42886.1.
CH466531 Genomic DNA. Translation: EDL17060.1.
BC030837 mRNA. Translation: AAH30837.1.
CCDSCCDS21759.1.
RefSeqNP_203534.1. NM_033370.3.
UniGeneMm.277024.

3D structure databases

ProteinModelPortalQ9JIF7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid213992. 3 interactions.
DIPDIP-42642N.
IntActQ9JIF7. 9 interactions.
MINTMINT-1489518.
STRING10090.ENSMUSP00000033012.

PTM databases

PhosphoSiteQ9JIF7.

Proteomic databases

MaxQBQ9JIF7.
PaxDbQ9JIF7.
PRIDEQ9JIF7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033012; ENSMUSP00000033012; ENSMUSG00000030754.
GeneID70349.
KEGGmmu:70349.
UCSCuc009jhx.1. mouse.

Organism-specific databases

CTD1315.
MGIMGI:1917599. Copb1.

Phylogenomic databases

eggNOGCOG5096.
GeneTreeENSGT00390000005270.
HOGENOMHOG000207417.
HOVERGENHBG005380.
InParanoidQ3T9Y4.
KOK17301.
OMAVHALMEF.
OrthoDBEOG7ZWD12.
PhylomeDBQ9JIF7.
TreeFamTF105737.

Gene expression databases

BgeeQ9JIF7.
CleanExMM_COPB1.
GenevestigatorQ9JIF7.

Family and domain databases

Gene3D1.25.10.10. 3 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002553. Clathrin/coatomer_adapt-like_N.
IPR011710. Coatomer_bsu_C.
IPR016460. COPB1.
IPR029446. COPB1_appendage_platform_dom.
[Graphical view]
PANTHERPTHR10635. PTHR10635. 1 hit.
PfamPF01602. Adaptin_N. 1 hit.
PF07718. Coatamer_beta_C. 1 hit.
PF14806. Coatomer_b_Cpla. 1 hit.
[Graphical view]
PIRSFPIRSF005727. Coatomer_beta_subunit. 1 hit.
SUPFAMSSF48371. SSF48371. 2 hits.
ProtoNetSearch...

Other

NextBio331414.
PROQ9JIF7.
SOURCESearch...

Entry information

Entry nameCOPB_MOUSE
AccessionPrimary (citable) accession number: Q9JIF7
Secondary accession number(s): Q3T9Y4 expand/collapse secondary AC list , Q3TT72, Q3U8G9, Q3UE02
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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