CORO7_RAT
ID CORO7_RAT Reviewed; 922 AA.
AC O35828; D3ZUE2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Coronin-7;
DE Short=Crn7;
DE AltName: Full=70 kDa WD repeat tumor rejection antigen;
GN Name=Coro7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 425-922.
RC STRAIN=Wistar;
RX PubMed=9703019; DOI=10.1089/dna.1998.17.603;
RA Muralikrishna T., Begum Z., Swamy C.V., Khar A.;
RT "Molecular cloning and characterization of a tumor rejection antigen from
RT rat histiocytoma, AK-5.";
RL DNA Cell Biol. 17:603-612(1998).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459; SER-462; THR-874 AND
RP SER-912, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 {ECO:0000250}. Golgi
CC apparatus, trans-Golgi network {ECO:0000250}. Cytoplasmic vesicle
CC {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=Predominantly
CC cytosolic. Detected on vesicle-like cytoplasmic structures and on the
CC cis-Golgi. Not associated with actin filaments (By similarity).
CC {ECO:0000250}.
CC -!- PTM: The membrane-associated form is phosphorylated on tyrosine
CC residues. {ECO:0000250}.
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 -!- SEQUENCE CAUTION:
CC Sequence=CAA75339.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AABR06062859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Y15054; CAA75339.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001178568.1; NM_001191639.1.
DR AlphaFoldDB; O35828; -.
DR STRING; 10116.ENSRNOP00000006067; -.
DR iPTMnet; O35828; -.
DR jPOST; O35828; -.
DR PaxDb; O35828; -.
DR PRIDE; O35828; -.
DR Ensembl; ENSRNOT00000086305; ENSRNOP00000074983; ENSRNOG00000004146.
DR GeneID; 192276; -.
DR KEGG; rno:192276; -.
DR UCSC; RGD:621591; rat.
DR CTD; 79585; -.
DR RGD; 621591; Coro7.
DR eggNOG; KOG1445; Eukaryota.
DR GeneTree; ENSGT00940000156606; -.
DR InParanoid; O35828; -.
DR OrthoDB; 552726at2759; -.
DR TreeFam; TF314280; -.
DR PRO; PR:O35828; -.
DR Proteomes; UP000002494; Chromosome 10.
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; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
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; ISO:RGD.
DR GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0030010; P:establishment of cell polarity; ISO:RGD.
DR GO; GO:0007030; P:Golgi organization; ISO:RGD.
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_0000050936"
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..579
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 386..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 874
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 912
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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 534
FT /note="A -> G (in Ref. 2; CAA75339)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="V -> I (in Ref. 2; CAA75339)"
FT /evidence="ECO:0000305"
FT CONFLICT 624
FT /note="G -> R (in Ref. 2; CAA75339)"
FT /evidence="ECO:0000305"
FT CONFLICT 819
FT /note="Missing (in Ref. 2; CAA75339)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 922 AA; 100782 MW; EFE35CD81D40E3BA CRC64;
MNRFKASKFR HMEARPSRRE AWISDIRAGT TATCGNHIKS SCSLIAFNSD RPGVLGIISL
EGHEENKRHV TYLGCHSDLV TDLDFSPFDD FLLASGSADR TIKLWRLSST GEALPSVPGV
VLGPEELPVD VLQFHPTADG VLVSTAGRTV KVWDVAKQQH LTELEAHKDL VQSAVWSRDG
ATVGTACKDK QLRIFDPRAR AQASQSTQAH ENNRDIRLAW TGIQEYLVST GFNQMREREA
KLWDTRVFSS ALASITLDTS PGSLIPLLDP DSGLLVLAGK GENQLYCYEV TPQQPALSPV
TQCILENALR GAALVPRQAL AVMNCEVLQV LQLSDTAIIP ISHRVPRKAV EFHEDLFPDT
AGSVPASDAH TWWAGDNQQV QKVSLNPAHR PHPRFTSSLL PTLEPSPNME QPAELPRADT
ELSEGFSSPS SLVSPSTPSS LGLSLSSTSG IGTSPSQRSL QSLLGPSSKF RHAEGTILHR
DSHITNLKGL NLTTPGESDG FCANRLRVAV PLLSSGGQVA VLELQKPGRL PDTALPTLQN
GAAVMDLVWD PFDPHRLAVA GEDARIRLWR VPPGGLKNVL TTPETVLTGH TEKIYSLRFH
PLAADVLASS SYDLTIRIWD LQAGTEQLRL QGHQDQIFSL AWSPDGKQLA TVCKDGRVRV
YDPRSSPLPL QDGPGPEGGR GARIVWVCNG GCLLVSGFDS RSERQLQLYM ADALAEGPSA
LLGLDVAPST LLPSYDPDTG LVLLTGKGDT RVFLYEVIPE APFFLECNSF TSPDPHKGFI
LLPKTECDIQ DVEFARCLRL RQTSLEPVAF RLPRVRKEFF QDDVFPDTAV TWASALDAKA
WFKGANGQPR LLSLQPPGMT PVSQAPREVP ARRTPSSAQY LEEKSDQQKK EELLNAMVAK
LGNREDPLPQ DSFEGVDEDE WD
