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Q9JIF7

- COPB_MOUSE

UniProt

Q9JIF7 - COPB_MOUSE

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Protein

Coatomer subunit beta

Gene

Copb1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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. 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.By similarity2 Publications

GO - Molecular functioni

  1. structural molecule activity Source: InterPro

GO - Biological processi

  1. intracellular protein transport Source: InterPro
  2. intra-Golgi vesicle-mediated transport Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_227904. COPI Mediated Transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Coatomer subunit beta
Alternative name(s):
Beta-coat protein
Short name:
Beta-COP
Gene namesi
Name:Copb1
Synonyms:Copb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1917599. Copb1.

Subcellular locationi

Cytoplasm By similarity. Golgi apparatus membrane By similarity; Peripheral membrane protein By similarity; 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).By similarity

GO - Cellular componenti

  1. COPI-coated vesicle Source: MGI
  2. COPI vesicle coat Source: Ensembl
  3. Golgi apparatus Source: MGI
  4. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 953952Coatomer subunit betaPRO_0000193834Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity
Modified residuei494 – 4941N6-acetyllysine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9JIF7.
PaxDbiQ9JIF7.
PRIDEiQ9JIF7.

PTM databases

PhosphoSiteiQ9JIF7.

Expressioni

Tissue specificityi

Predominantly expressed in the upper one-third of the oxyntic mucosa and in most regions of the pyloric mucosa (PubMed:16476741). Ubiquitiously expressed including platelet, liver, heart, spleen, lung and kidney (PubMed:11441537).2 Publications

Gene expression databases

BgeeiQ9JIF7.
CleanExiMM_COPB1.
GenevestigatoriQ9JIF7.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi213992. 3 interactions.
DIPiDIP-42642N.
IntActiQ9JIF7. 9 interactions.
MINTiMINT-1489518.
STRINGi10090.ENSMUSP00000033012.

Structurei

3D structure databases

ProteinModelPortaliQ9JIF7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati96 – 13136HEAT 1Add
BLAST
Repeati132 – 16837HEAT 2Add
BLAST
Repeati240 – 27637HEAT 3Add
BLAST
Repeati277 – 31438HEAT 4Add
BLAST
Repeati316 – 35338HEAT 5Add
BLAST
Repeati396 – 43338HEAT 6Add
BLAST

Sequence similaritiesi

Contains 6 HEAT repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5096.
GeneTreeiENSGT00390000005270.
HOGENOMiHOG000207417.
HOVERGENiHBG005380.
InParanoidiQ9JIF7.
KOiK17301.
OMAiVHALMEF.
OrthoDBiEOG7ZWD12.
PhylomeDBiQ9JIF7.
TreeFamiTF105737.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. 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]
PANTHERiPTHR10635. PTHR10635. 1 hit.
PfamiPF01602. Adaptin_N. 1 hit.
PF07718. Coatamer_beta_C. 1 hit.
PF14806. Coatomer_b_Cpla. 1 hit.
[Graphical view]
PIRSFiPIRSF005727. Coatomer_beta_subunit. 1 hit.
SUPFAMiSSF48371. SSF48371. 2 hits.

Sequencei

Sequence statusi: Complete.

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

Q9JIF7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTAAENVCYT LINVPMDSEP PSEISLKNDL EKGDVKSKTE ALKKVIIMIL
60 70 80 90 100
NGEKLPGLLM TIIRFVLPLQ DHTIKKLLLV FWEIVPKTTP DGRLLHEMIL
110 120 130 140 150
VCDAYRKDLQ HPNEFIRGST LRFLCKLKEA ELLEPLMPAI RACLEHRHSY
160 170 180 190 200
VRRNAVLAIY TIYRNFEHLI PDAPELIHDF LVNEKDASCK RNAFMMLIHA
210 220 230 240 250
DQDRALDYLS TCIDQVQTFG DILQLVIVEL IYKVCHANPS ERARFIRCIY
260 270 280 290 300
NLLQSSSPAV KYEAAGTLVT LSSAPTAIKA AAQCYIDLII KESDNNVKLI
310 320 330 340 350
VLDRLVELKE HPAHERVLQD LVMDILRVLS TPDLEVRKKT LQLALDLVSS
360 370 380 390 400
RNVEELVIVL KKEVIKTNNV SEHEDTDKYR QLLVRTLHSC SVRFPDMAAN
410 420 430 440 450
VIPVLMEFLS DSNEAAAADV LEFVREAIQR FDNLRMLIVE KMLEVFHAIK
460 470 480 490 500
SVKIYRGALW ILGEYCSTKE DIQSVMTEVR RSLGEIPIVE SEIKKEAGEL
510 520 530 540 550
KPEEEITVGP VQKLVTEMGT YATQSALSSS RPTKKEEDRP PLRGFLLDGD
560 570 580 590 600
FFVAASLATT LTKIALRYVA LVQEKKKQNS FVAEAMLLMA TILHLGKSSL
610 620 630 640 650
PKKPITDDDV DRISLCLKVL SECSPLMNDI FNKECRQSLS QMLSAKLEEE
660 670 680 690 700
KLSQKKESEK RNVTVQPDDP ISFMQLTAKN EMNCKEDQFQ LSLLAAMGNT
710 720 730 740 750
QRKEAADPLA SKLNKVTQLT GFSDPVYAEA YVHVNQYDIV LDVLVVNQTS
760 770 780 790 800
DTLQNCTLEL ATLGDLKLVE KPSPLTLAPH DFANIKANVK VASTENGIIF
810 820 830 840 850
GNIVYDVSGA ASDRNCVVLS DIHIDIMDYI QPATCTDAEF RQMWAEFEWE
860 870 880 890 900
NKVTVNTNMT DLNDYLQHIL KSTNMKCLTP EKALSGYCGF MAANLYARSI
910 920 930 940 950
FGEDALANVS IEKPVHQGPD AAVTGHIRIR AKSQGMALSL GDKINLSQKK

TSL
Length:953
Mass (Da):107,066
Last modified:October 1, 2000 - v1
Checksum:i4CD5407AD87ACB4B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti757 – 7571T → I in BAE29109. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS21759.1.
RefSeqiNP_203534.1. NM_033370.3.
UniGeneiMm.277024.

Genome annotation databases

EnsembliENSMUST00000033012; ENSMUSP00000033012; ENSMUSG00000030754.
GeneIDi70349.
KEGGimmu:70349.
UCSCiuc009jhx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS21759.1.
RefSeqi NP_203534.1. NM_033370.3.
UniGenei Mm.277024.

3D structure databases

ProteinModelPortali Q9JIF7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 213992. 3 interactions.
DIPi DIP-42642N.
IntActi Q9JIF7. 9 interactions.
MINTi MINT-1489518.
STRINGi 10090.ENSMUSP00000033012.

PTM databases

PhosphoSitei Q9JIF7.

Proteomic databases

MaxQBi Q9JIF7.
PaxDbi Q9JIF7.
PRIDEi Q9JIF7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000033012 ; ENSMUSP00000033012 ; ENSMUSG00000030754 .
GeneIDi 70349.
KEGGi mmu:70349.
UCSCi uc009jhx.1. mouse.

Organism-specific databases

CTDi 1315.
MGIi MGI:1917599. Copb1.

Phylogenomic databases

eggNOGi COG5096.
GeneTreei ENSGT00390000005270.
HOGENOMi HOG000207417.
HOVERGENi HBG005380.
InParanoidi Q9JIF7.
KOi K17301.
OMAi VHALMEF.
OrthoDBi EOG7ZWD12.
PhylomeDBi Q9JIF7.
TreeFami TF105737.

Enzyme and pathway databases

Reactomei REACT_227904. COPI Mediated Transport.

Miscellaneous databases

NextBioi 331414.
PROi Q9JIF7.
SOURCEi Search...

Gene expression databases

Bgeei Q9JIF7.
CleanExi MM_COPB1.
Genevestigatori Q9JIF7.

Family and domain databases

Gene3Di 1.25.10.10. 3 hits.
InterProi IPR011989. 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 ]
PANTHERi PTHR10635. PTHR10635. 1 hit.
Pfami PF01602. Adaptin_N. 1 hit.
PF07718. Coatamer_beta_C. 1 hit.
PF14806. Coatomer_b_Cpla. 1 hit.
[Graphical view ]
PIRSFi PIRSF005727. Coatomer_beta_subunit. 1 hit.
SUPFAMi SSF48371. SSF48371. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiCOPB_MOUSE
AccessioniPrimary (citable) accession number: Q9JIF7
Secondary accession number(s): Q3T9Y4
, Q3TT72, Q3U8G9, Q3UE02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: October 1, 2000
Last modified: October 29, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3