CORO7_MOUSE
ID CORO7_MOUSE Reviewed; 922 AA.
AC Q9D2V7; Q3UDJ4; Q6P8Y8; Q8C9V7;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Coronin-7;
DE Short=Crn7;
DE AltName: Full=70 kDa WD repeat tumor rejection antigen homolog;
GN Name=Coro7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Kidney, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15327992; DOI=10.1016/j.febslet.2004.07.066;
RA Rybakin V., Stumpf M., Schulze A., Majoul I.V., Noegel A.A., Hasse A.;
RT "Coronin 7, the mammalian POD-1 homologue, localizes to the Golgi
RT apparatus.";
RL FEBS Lett. 573:161-167(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459 AND SER-912, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: F-actin regulator involved in anterograde Golgi to endosome
CC transport: upon ubiquitination via 'Lys-33'-linked ubiquitin chains by
CC the BCR(KLHL20) E3 ubiquitin ligase complex, interacts with EPS15 and
CC localizes to the trans-Golgi network, where it promotes actin
CC polymerization, thereby facilitating post-Golgi trafficking. May play a
CC role in the maintenance of the Golgi apparatus morphology (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with clathrin adapter AP1 complex. This interaction
CC takes place at Golgi membranes and not AP1-positive endosomal
CC membranes. Interacts (when ubiquitinated at Lys-469) with EPS15 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:15327992}. Golgi apparatus, trans-Golgi network
CC {ECO:0000250}. Cytoplasmic vesicle {ECO:0000269|PubMed:15327992}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:15327992}. Note=Predominantly
CC cytosolic. Detected on vesicle-like cytoplasmic structures and on the
CC cis-Golgi. Not associated with actin filaments.
CC -!- TISSUE SPECIFICITY: In the adult, widely expressed with highest levels
CC in brain, thymus and kidney and low levels in skeletal and heart
CC muscle. Not expressed in lung. In the eye, strongly expressed in the
CC outer plexiform layer of the retina. In the intestine, expressed both
CC in terminally differentiated epithelial cells and in crypt epithelium.
CC In the embryo, strongest expression is seen in brain, thymus,
CC intestine, apical epidermal layers of the skin and developing lens
CC fibers of the eye. {ECO:0000269|PubMed:15327992}.
CC -!- DEVELOPMENTAL STAGE: In the embryo, expressed from 5 dpc and levels
CC increase strongly until 15 dpc. {ECO:0000269|PubMed:15327992}.
CC -!- PTM: The membrane-associated form is phosphorylated on tyrosine
CC residues.
CC -!- PTM: Ubiquitinated via 'Lys-33'-linked ubiquitin chains by the
CC BCR(KLHL20) E3 ubiquitin ligase complex: 'Lys-33'-linked ubiquitination
CC promotes interaction with EPS15 and facilitates actin polymerization at
CC the trans-Golgi network, thereby facilitating post-Golgi trafficking.
CC Deubiquitinated by ZRANB1/TRABID (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat coronin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK018739; BAB31380.1; -; mRNA.
DR EMBL; AK040408; BAC30588.1; -; mRNA.
DR EMBL; AK150051; BAE29267.1; -; mRNA.
DR EMBL; BC061006; AAH61006.1; -; mRNA.
DR CCDS; CCDS37242.1; -.
DR RefSeq; NP_084481.3; NM_030205.4.
DR AlphaFoldDB; Q9D2V7; -.
DR BioGRID; 219682; 1.
DR STRING; 10090.ENSMUSP00000048489; -.
DR iPTMnet; Q9D2V7; -.
DR PhosphoSitePlus; Q9D2V7; -.
DR SwissPalm; Q9D2V7; -.
DR EPD; Q9D2V7; -.
DR jPOST; Q9D2V7; -.
DR MaxQB; Q9D2V7; -.
DR PaxDb; Q9D2V7; -.
DR PeptideAtlas; Q9D2V7; -.
DR PRIDE; Q9D2V7; -.
DR ProteomicsDB; 284098; -.
DR DNASU; 78885; -.
DR Ensembl; ENSMUST00000038552; ENSMUSP00000048489; ENSMUSG00000039637.
DR GeneID; 78885; -.
DR KEGG; mmu:78885; -.
DR UCSC; uc007xzy.1; mouse.
DR CTD; 79585; -.
DR MGI; MGI:1926135; Coro7.
DR VEuPathDB; HostDB:ENSMUSG00000039637; -.
DR eggNOG; KOG1445; Eukaryota.
DR GeneTree; ENSGT00940000156606; -.
DR HOGENOM; CLU_006604_0_0_1; -.
DR InParanoid; Q9D2V7; -.
DR OMA; VMQGEVN; -.
DR OrthoDB; 552726at2759; -.
DR PhylomeDB; Q9D2V7; -.
DR TreeFam; TF314280; -.
DR BioGRID-ORCS; 78885; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Coro7; mouse.
DR PRO; PR:Q9D2V7; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9D2V7; protein.
DR Bgee; ENSMUSG00000039637; Expressed in mesenteric lymph node and 235 other tissues.
DR ExpressionAtlas; Q9D2V7; baseline and differential.
DR Genevisible; Q9D2V7; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IMP:MGI.
DR GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:MGI.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:MGI.
DR GO; GO:0007030; P:Golgi organization; IMP:MGI.
DR GO; GO:0006895; P:Golgi to endosome transport; ISS:UniProtKB.
DR GO; GO:0035332; P:positive regulation of hippo signaling; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR027331; CORO7.
DR InterPro; IPR015505; Coronin.
DR InterPro; IPR015048; DUF1899.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR PANTHER; PTHR10856; PTHR10856; 1.
DR PANTHER; PTHR10856:SF20; PTHR10856:SF20; 1.
DR Pfam; PF08953; DUF1899; 2.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM01166; DUF1899; 2.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Cytoplasmic vesicle; Golgi apparatus;
KW Isopeptide bond; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport; Ubl conjugation; WD repeat.
FT CHAIN 1..922
FT /note="Coronin-7"
FT /id="PRO_0000050935"
FT REPEAT 75..115
FT /note="WD 1"
FT REPEAT 124..163
FT /note="WD 2"
FT REPEAT 166..205
FT /note="WD 3"
FT REPEAT 209..253
FT /note="WD 4"
FT REPEAT 539..581
FT /note="WD 5"
FT REPEAT 589..629
FT /note="WD 6"
FT REPEAT 632..671
FT /note="WD 7"
FT REPEAT 725..765
FT /note="WD 8"
FT REGION 419..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35828"
FT MOD_RES 912
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 469
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P57737"
FT CONFLICT 364
FT /note="V -> M (in Ref. 1; BAB31380)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="W -> R (in Ref. 1; BAC30588)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="S -> C (in Ref. 1; BAB31380)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="Q -> E (in Ref. 1; BAB31380)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 922 AA; 100812 MW; 0B7F1C4166940936 CRC64;
MSRFKVSKFR HMEARPSRRE AWISDIRAVT TPTCGNHIKS SCSLIAFNSD RPGVLGVISL
EGHEENKRHV TYLGCHSDLV TDLDFSPFDD FLLASGSADR TIKLWRLSGT GEALPSVPGV
VLGPEELPVE VLQFHPTVDG VLVSTAGKTV KVWDVAKQQP LTELEAHKDL VQSAVWSRDG
AIVGTACKDK QLRIFDPRAR TQASQSTQAH ENNRDIRLAW TGIQEHLVST GFNQMREREA
KLWDTRLFSS ALASVTLDTS PGPLIPLLDP DSGLLVLAGK GENQLYCYEV TPQQPALSPV
TQCILENVLR GAALVPRRAL AVMSCEVLQV LQLSDTAIIP ISHHVPRKAV EFHEDLFPDT
AGSVPASDAH MWWAGDNQQV QKVSLNPARR PHPCFTSSLV PTMEPAPDMV QPAEMPRADT
DLSEGFSSPS SLMSPSTPSS LGPSLSSTSG IGTSPSQRSL QSLLGPSSKF RHTQGSLLHR
DSHITNLKGL NLTTPGESDG FCANRLRVAV PLLSSGGQVA VLELQKPGRL PDTALPTLQN
GTAVMDLVWD PFDPHRLAVA GEDARIRLWR VPPGGLENVL TTPETVLTGH TEKIYSLRFH
PLAADVLASS SYDLTVRIWD LQTGAERLKL QGHQDQIFSL AWSPDGKQLA TVCKDGHVRV
YEPRSSPLPL QEGPGPEGGR GARIVWVCDG GCLLVSGFDS RSERQLQLYI ADALAQGPSA
LLGLDVAPST LLPSYDPDTG LVLLTGKGDT RVFLYEVLPE APFFLECNSF TSPDPHKGFV
LLPKTECDIQ DVEFARCLRL RQTSLEPVAF RLPRVRKEFF QDDVFPDTAV TWEPALSAKA
WFEGANGQPR LLSLQPPGMT PVSQAPREVP ARRAPSSAQY LEEKSDQQKK EELLNAMVAK
LGNREDPLPQ DSFEGVDEDE WD
