Full text data of CORO7
CORO7
[Confidence: low (only semi-automatic identification from reviews)]
Coronin-7; Crn7 (70 kDa WD repeat tumor rejection antigen homolog)
Coronin-7; Crn7 (70 kDa WD repeat tumor rejection antigen homolog)
UniProt
P57737
ID CORO7_HUMAN Reviewed; 925 AA.
AC P57737; B4DFD6; B4DL18; I3L416; Q17RK4;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 22-SEP-2009, sequence version 2.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=Coronin-7;
DE Short=Crn7;
DE AltName: Full=70 kDa WD repeat tumor rejection antigen homolog;
GN Name=CORO7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4), AND
RP VARIANT GLN-193.
RC TISSUE=Cerebellum, Hepatoma, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Colon, and Lymphoma;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AP1 COMPLEX.
RX PubMed=16905771; DOI=10.1074/jbc.M604680200;
RA Rybakin V., Gounko N.V., Spaete K., Hoening S., Majoul I.V., Duden R.,
RA Noegel A.A.;
RT "Crn7 interacts with AP-1 and is required for the maintenance of Golgi
RT morphology and protein export from the Golgi.";
RL J. Biol. Chem. 281:31070-31078(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May play a role in the maintenance of the Golgi
CC apparatus morphology and in the protein export from the Golgi.
CC -!- SUBUNIT: Interacted with clathrin adapter AP1 complex. This
CC interaction takes place at Golgi membranes and not AP1-positive
CC endosomal membranes.
CC -!- INTERACTION:
CC Q61471:Tob1 (xeno); NbExp=3; IntAct=EBI-6916167, EBI-8527498;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity). Golgi
CC apparatus membrane. Cytoplasmic vesicle (By similarity).
CC Note=Predominantly cytosolic. Detected on vesicle-like cytoplasmic
CC structures and on the cis-Golgi. Not associated with actin
CC filaments.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P57737-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P57737-2; Sequence=VSP_038152;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=P57737-3; Sequence=VSP_046022;
CC Note=No experimental confirmation available. Ref.4 (BC032732)
CC sequence is in conflict in position: 1037:Q->K;
CC Name=4;
CC IsoId=P57737-4; Sequence=VSP_046752;
CC Note=No experimental confirmation available;
CC -!- PTM: The membrane-associated form is phosphorylated on tyrosine
CC residues (By similarity).
CC -!- SIMILARITY: Belongs to the WD repeat coronin family.
CC -!- SIMILARITY: Contains 8 WD repeats.
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DR EMBL; AK025674; BAB15211.1; -; mRNA.
DR EMBL; AK294045; BAG57397.1; -; mRNA.
DR EMBL; AK296807; BAG59380.1; -; mRNA.
DR EMBL; AC012676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85307.1; -; Genomic_DNA.
DR EMBL; BC032732; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC117289; AAI17290.1; -; mRNA.
DR EMBL; BC117291; AAI17292.1; -; mRNA.
DR RefSeq; NP_001188401.1; NM_001201472.1.
DR RefSeq; NP_001188402.1; NM_001201473.1.
DR RefSeq; NP_001188408.1; NM_001201479.1.
DR RefSeq; NP_078811.3; NM_024535.4.
DR UniGene; Hs.437957; -.
DR UniGene; Hs.739021; -.
DR ProteinModelPortal; P57737; -.
DR SMR; P57737; 7-385, 444-867.
DR IntAct; P57737; 6.
DR STRING; 9606.ENSP00000251166; -.
DR PhosphoSite; P57737; -.
DR DMDM; 259016200; -.
DR PaxDb; P57737; -.
DR PRIDE; P57737; -.
DR DNASU; 79585; -.
DR Ensembl; ENST00000251166; ENSP00000251166; ENSG00000262246.
DR Ensembl; ENST00000537233; ENSP00000440460; ENSG00000262246.
DR Ensembl; ENST00000574025; ENSP00000461702; ENSG00000262246.
DR GeneID; 100529144; -.
DR GeneID; 79585; -.
DR KEGG; hsa:100529144; -.
DR KEGG; hsa:79585; -.
DR UCSC; uc010uxh.2; human.
DR CTD; 100529144; -.
DR CTD; 79585; -.
DR GeneCards; GC16M004405; -.
DR H-InvDB; HIX0012777; -.
DR HGNC; HGNC:26161; CORO7.
DR HPA; HPA041657; -.
DR MIM; 611668; gene.
DR neXtProt; NX_P57737; -.
DR PharmGKB; PA134910806; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000006535; -.
DR HOVERGEN; HBG051080; -.
DR InParanoid; P57737; -.
DR OMA; EVEFARC; -.
DR OrthoDB; EOG76X5ZX; -.
DR PhylomeDB; P57737; -.
DR SignaLink; P57737; -.
DR GenomeRNAi; 79585; -.
DR NextBio; 34054991; -.
DR PRO; PR:P57737; -.
DR ArrayExpress; P57737; -.
DR Bgee; P57737; -.
DR CleanEx; HS_CORO7; -.
DR Genevestigator; P57737; -.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
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 to membrane; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR027331; CORO7.
DR InterPro; IPR015505; Coronin.
DR InterPro; IPR015049; DUF1900.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR PANTHER; PTHR10856; PTHR10856; 1.
DR PANTHER; PTHR10856:SF1; PTHR10856:SF1; 1.
DR Pfam; PF08954; DUF1900; 2.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 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 Alternative splicing; Complete proteome; Cytoplasm;
KW Cytoplasmic vesicle; Golgi apparatus; Membrane; Phosphoprotein;
KW Polymorphism; Reference proteome; Repeat; WD repeat.
FT CHAIN 1 925 Coronin-7.
FT /FTId=PRO_0000050934.
FT REPEAT 75 115 WD 1.
FT REPEAT 124 163 WD 2.
FT REPEAT 166 205 WD 3.
FT REPEAT 209 253 WD 4.
FT REPEAT 542 582 WD 5.
FT REPEAT 592 632 WD 6.
FT REPEAT 635 674 WD 7.
FT REPEAT 728 768 WD 8.
FT VAR_SEQ 78 162 Missing (in isoform 2).
FT /FTId=VSP_038152.
FT VAR_SEQ 78 95 Missing (in isoform 4).
FT /FTId=VSP_046752.
FT VAR_SEQ 925 925 D -> AKYLAQIIVMGVQVVGRAFARALRQEFAASRAAADA
FT RGRAGHRSAAASNLSGLSLQEAQQILNVSKLSPEEVQKNYE
FT HLFKVNDKSVGGSFYLQSKVVRAKERLDEELKIQAQEDREK
FT GQMPHT (in isoform 3).
FT /FTId=VSP_046022.
FT VARIANT 174 174 A -> V (in dbSNP:rs17137007).
FT /FTId=VAR_057585.
FT VARIANT 193 193 R -> Q (in dbSNP:rs3747579).
FT /FTId=VAR_057586.
FT VARIANT 257 257 L -> S (in dbSNP:rs35357594).
FT /FTId=VAR_057587.
FT VARIANT 403 403 A -> T (in dbSNP:rs9928967).
FT /FTId=VAR_057588.
FT CONFLICT 324 324 S -> G (in Ref. 2; BAB15211).
FT CONFLICT 371 371 S -> G (in Ref. 2; BAB15211).
FT CONFLICT 848 848 A -> T (in Ref. 2; BAB15211).
SQ SEQUENCE 925 AA; 100605 MW; FC8680F8CCB409C0 CRC64;
MNRFRVSKFR HTEARPPRRE SWISDIRAGT APSCRNHIKS SCSLIAFNSD RPGVLGIVPL
QGQGEDKRRV AHLGCHSDLV TDLDFSPFDD FLLATGSADR TVKLWRLPGP GQALPSAPGV
VLGPEDLPVE VLQFHPTSDG ILVSAAGTTV KVWDAAKQQP LTELAAHGDL VQSAVWSRDG
ALVGTACKDK QLRIFDPRTK PRASQSTQAH ENSRDSRLAW MGTWEHLVST GFNQMREREV
KLWDTRFFSS ALASLTLDTS LGCLVPLLDP DSGLLVLAGK GERQLYCYEV VPQQPALSPV
TQCVLESVLR GAALVPRQAL AVMSCEVLRV LQLSDTAIVP IGYHVPRKAV EFHEDLFPDT
AGCVPATDPH SWWAGDNQQV QKVSLNPACR PHPSFTSCLV PPAEPLPDTA QPAVMETPVG
DADASEGFSS PPSSLTSPST PSSLGPSLSS TSGIGTSPSL RSLQSLLGPS SKFRHAQGTV
LHRDSHITNL KGLNLTTPGE SDGFCANKLR VAVPLLSSGG QVAVLELRKP GRLPDTALPT
LQNGAAVTDL AWDPFDPHRL AVAGEDARIR LWRVPAEGLE EVLTTPETVL TGHTEKICSL
RFHPLAANVL ASSSYDLTVR IWDLQAGADR LKLQGHQDQI FSLAWSPDGQ QLATVCKDGR
VRVYRPRSGP EPLQEGPGPK GGRGARIVWV CDGRCLLVSG FDSQSERQLL LYEAEALAGG
PLAVLGLDVA PSTLLPSYDP DTGLVLLTGK GDTRVFLYEL LPESPFFLEC NSFTSPDPHK
GLVLLPKTEC DVREVELMRC LRLRQSSLEP VAFRLPRVRK EFFQDDVFPD TAVIWEPVLS
AEAWLQGANG QPWLLSLQPP DMSPVSQAPR EAPARRAPSS AQYLEEKSDQ QKKEELLNAM
VAKLGNREDP LPQDSFEGVD EDEWD
//
ID CORO7_HUMAN Reviewed; 925 AA.
AC P57737; B4DFD6; B4DL18; I3L416; Q17RK4;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 22-SEP-2009, sequence version 2.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=Coronin-7;
DE Short=Crn7;
DE AltName: Full=70 kDa WD repeat tumor rejection antigen homolog;
GN Name=CORO7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4), AND
RP VARIANT GLN-193.
RC TISSUE=Cerebellum, Hepatoma, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Colon, and Lymphoma;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AP1 COMPLEX.
RX PubMed=16905771; DOI=10.1074/jbc.M604680200;
RA Rybakin V., Gounko N.V., Spaete K., Hoening S., Majoul I.V., Duden R.,
RA Noegel A.A.;
RT "Crn7 interacts with AP-1 and is required for the maintenance of Golgi
RT morphology and protein export from the Golgi.";
RL J. Biol. Chem. 281:31070-31078(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May play a role in the maintenance of the Golgi
CC apparatus morphology and in the protein export from the Golgi.
CC -!- SUBUNIT: Interacted with clathrin adapter AP1 complex. This
CC interaction takes place at Golgi membranes and not AP1-positive
CC endosomal membranes.
CC -!- INTERACTION:
CC Q61471:Tob1 (xeno); NbExp=3; IntAct=EBI-6916167, EBI-8527498;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity). Golgi
CC apparatus membrane. Cytoplasmic vesicle (By similarity).
CC Note=Predominantly cytosolic. Detected on vesicle-like cytoplasmic
CC structures and on the cis-Golgi. Not associated with actin
CC filaments.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P57737-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P57737-2; Sequence=VSP_038152;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=P57737-3; Sequence=VSP_046022;
CC Note=No experimental confirmation available. Ref.4 (BC032732)
CC sequence is in conflict in position: 1037:Q->K;
CC Name=4;
CC IsoId=P57737-4; Sequence=VSP_046752;
CC Note=No experimental confirmation available;
CC -!- PTM: The membrane-associated form is phosphorylated on tyrosine
CC residues (By similarity).
CC -!- SIMILARITY: Belongs to the WD repeat coronin family.
CC -!- SIMILARITY: Contains 8 WD repeats.
CC -----------------------------------------------------------------------
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DR EMBL; AK025674; BAB15211.1; -; mRNA.
DR EMBL; AK294045; BAG57397.1; -; mRNA.
DR EMBL; AK296807; BAG59380.1; -; mRNA.
DR EMBL; AC012676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85307.1; -; Genomic_DNA.
DR EMBL; BC032732; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC117289; AAI17290.1; -; mRNA.
DR EMBL; BC117291; AAI17292.1; -; mRNA.
DR RefSeq; NP_001188401.1; NM_001201472.1.
DR RefSeq; NP_001188402.1; NM_001201473.1.
DR RefSeq; NP_001188408.1; NM_001201479.1.
DR RefSeq; NP_078811.3; NM_024535.4.
DR UniGene; Hs.437957; -.
DR UniGene; Hs.739021; -.
DR ProteinModelPortal; P57737; -.
DR SMR; P57737; 7-385, 444-867.
DR IntAct; P57737; 6.
DR STRING; 9606.ENSP00000251166; -.
DR PhosphoSite; P57737; -.
DR DMDM; 259016200; -.
DR PaxDb; P57737; -.
DR PRIDE; P57737; -.
DR DNASU; 79585; -.
DR Ensembl; ENST00000251166; ENSP00000251166; ENSG00000262246.
DR Ensembl; ENST00000537233; ENSP00000440460; ENSG00000262246.
DR Ensembl; ENST00000574025; ENSP00000461702; ENSG00000262246.
DR GeneID; 100529144; -.
DR GeneID; 79585; -.
DR KEGG; hsa:100529144; -.
DR KEGG; hsa:79585; -.
DR UCSC; uc010uxh.2; human.
DR CTD; 100529144; -.
DR CTD; 79585; -.
DR GeneCards; GC16M004405; -.
DR H-InvDB; HIX0012777; -.
DR HGNC; HGNC:26161; CORO7.
DR HPA; HPA041657; -.
DR MIM; 611668; gene.
DR neXtProt; NX_P57737; -.
DR PharmGKB; PA134910806; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000006535; -.
DR HOVERGEN; HBG051080; -.
DR InParanoid; P57737; -.
DR OMA; EVEFARC; -.
DR OrthoDB; EOG76X5ZX; -.
DR PhylomeDB; P57737; -.
DR SignaLink; P57737; -.
DR GenomeRNAi; 79585; -.
DR NextBio; 34054991; -.
DR PRO; PR:P57737; -.
DR ArrayExpress; P57737; -.
DR Bgee; P57737; -.
DR CleanEx; HS_CORO7; -.
DR Genevestigator; P57737; -.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
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 to membrane; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR027331; CORO7.
DR InterPro; IPR015505; Coronin.
DR InterPro; IPR015049; DUF1900.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR PANTHER; PTHR10856; PTHR10856; 1.
DR PANTHER; PTHR10856:SF1; PTHR10856:SF1; 1.
DR Pfam; PF08954; DUF1900; 2.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 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 Alternative splicing; Complete proteome; Cytoplasm;
KW Cytoplasmic vesicle; Golgi apparatus; Membrane; Phosphoprotein;
KW Polymorphism; Reference proteome; Repeat; WD repeat.
FT CHAIN 1 925 Coronin-7.
FT /FTId=PRO_0000050934.
FT REPEAT 75 115 WD 1.
FT REPEAT 124 163 WD 2.
FT REPEAT 166 205 WD 3.
FT REPEAT 209 253 WD 4.
FT REPEAT 542 582 WD 5.
FT REPEAT 592 632 WD 6.
FT REPEAT 635 674 WD 7.
FT REPEAT 728 768 WD 8.
FT VAR_SEQ 78 162 Missing (in isoform 2).
FT /FTId=VSP_038152.
FT VAR_SEQ 78 95 Missing (in isoform 4).
FT /FTId=VSP_046752.
FT VAR_SEQ 925 925 D -> AKYLAQIIVMGVQVVGRAFARALRQEFAASRAAADA
FT RGRAGHRSAAASNLSGLSLQEAQQILNVSKLSPEEVQKNYE
FT HLFKVNDKSVGGSFYLQSKVVRAKERLDEELKIQAQEDREK
FT GQMPHT (in isoform 3).
FT /FTId=VSP_046022.
FT VARIANT 174 174 A -> V (in dbSNP:rs17137007).
FT /FTId=VAR_057585.
FT VARIANT 193 193 R -> Q (in dbSNP:rs3747579).
FT /FTId=VAR_057586.
FT VARIANT 257 257 L -> S (in dbSNP:rs35357594).
FT /FTId=VAR_057587.
FT VARIANT 403 403 A -> T (in dbSNP:rs9928967).
FT /FTId=VAR_057588.
FT CONFLICT 324 324 S -> G (in Ref. 2; BAB15211).
FT CONFLICT 371 371 S -> G (in Ref. 2; BAB15211).
FT CONFLICT 848 848 A -> T (in Ref. 2; BAB15211).
SQ SEQUENCE 925 AA; 100605 MW; FC8680F8CCB409C0 CRC64;
MNRFRVSKFR HTEARPPRRE SWISDIRAGT APSCRNHIKS SCSLIAFNSD RPGVLGIVPL
QGQGEDKRRV AHLGCHSDLV TDLDFSPFDD FLLATGSADR TVKLWRLPGP GQALPSAPGV
VLGPEDLPVE VLQFHPTSDG ILVSAAGTTV KVWDAAKQQP LTELAAHGDL VQSAVWSRDG
ALVGTACKDK QLRIFDPRTK PRASQSTQAH ENSRDSRLAW MGTWEHLVST GFNQMREREV
KLWDTRFFSS ALASLTLDTS LGCLVPLLDP DSGLLVLAGK GERQLYCYEV VPQQPALSPV
TQCVLESVLR GAALVPRQAL AVMSCEVLRV LQLSDTAIVP IGYHVPRKAV EFHEDLFPDT
AGCVPATDPH SWWAGDNQQV QKVSLNPACR PHPSFTSCLV PPAEPLPDTA QPAVMETPVG
DADASEGFSS PPSSLTSPST PSSLGPSLSS TSGIGTSPSL RSLQSLLGPS SKFRHAQGTV
LHRDSHITNL KGLNLTTPGE SDGFCANKLR VAVPLLSSGG QVAVLELRKP GRLPDTALPT
LQNGAAVTDL AWDPFDPHRL AVAGEDARIR LWRVPAEGLE EVLTTPETVL TGHTEKICSL
RFHPLAANVL ASSSYDLTVR IWDLQAGADR LKLQGHQDQI FSLAWSPDGQ QLATVCKDGR
VRVYRPRSGP EPLQEGPGPK GGRGARIVWV CDGRCLLVSG FDSQSERQLL LYEAEALAGG
PLAVLGLDVA PSTLLPSYDP DTGLVLLTGK GDTRVFLYEL LPESPFFLEC NSFTSPDPHK
GLVLLPKTEC DVREVELMRC LRLRQSSLEP VAFRLPRVRK EFFQDDVFPD TAVIWEPVLS
AEAWLQGANG QPWLLSLQPP DMSPVSQAPR EAPARRAPSS AQYLEEKSDQ QKKEELLNAM
VAKLGNREDP LPQDSFEGVD EDEWD
//
MIM
611668
*RECORD*
*FIELD* NO
611668
*FIELD* TI
*611668 CORONIN 7; CORO7
;;POLARITY-OSMOTIC DEFECTIVE 1, DROSOPHILA, HOMOLOG OF; POD1;;
read moreCRN7
*FIELD* TX
DESCRIPTION
Coronins, such as CORO7, constitute an evolutionarily conserved family
of WD-repeat actin-binding proteins. CORO7 plays a role in Golgi complex
morphology and function (Rybakin et al., 2004, 2006).
CLONING
By EST database analysis, followed by RT-PCR of human liver carcinoma
cDNA, Rybakin et al. (2004) cloned CORO7, which they called CRN7. The
deduced 924-amino acid protein has a calculated molecular mass of 100.5
kD, which was confirmed experimentally. CORO7 contains 2 coronin WD
repeat-containing domains with a proline-, serine-, and
threonine-enriched region (PST motif) preceding the second WD-repeat.
CORO7 shares 30% and 29% amino acid identity with Drosophila Pod1 and C.
elegans Pod1, respectively. Northern blot analysis detected expression
in mouse embryos as early as day 5 postcoitum and expression increased
through day 15. Coro7 expression was detected in most mouse tissues
examined with high levels in brain, thymus, and kidney and low levels in
heart, liver, testis, and muscle. Western blot analysis of mouse tissues
showed a similar distribution of Coro7 with low expression in skeletal
and heart muscle. Immunofluorescence studies detected developmental
expression of mouse Coro7 in embryonic brain, thymus, intestine, skin,
and eye. Indirect immunofluorescence studies detected Coro7 in
vesicle-like structures and in a Golgi-like perinuclear compartment in
mouse fibroblasts. Sucrose gradient centrifugation and
immunoprecipitation studies demonstrated that Coro7 localized to
cytosolic vesicles and to the cis-Golgi region. The membrane-associated
form of Coro7 was tyrosine-phosphorylated, whereas the cytosolic form
was not.
GENE FUNCTION
By electron microscopy, Rybakin et al. (2006) showed that siRNA
knockdown of CORO7 in HeLa cells caused loss of Golgi integrity and
membrane scattering. CORO7 knockdown caused a defect in Golgi export of
vesicular stomatitis virus glycoprotein (VSVG) but did not alter protein
import into the trans-Golgi network. Golgi cargo glycosylation was not
affected. Using in vitro binding, coimmunoprecipitation, and
colocalization studies, the authors demonstrated that CORO7 interacted
with clathrin adaptor AP1 (see 600157) and that this interaction takes
place at Golgi membranes. Rybakin et al. (2006) showed that CORO7 was
not required for AP1 targeting to Golgi membranes and suggested that
CORO7 acts downstream of AP1 recruitment.
*FIELD* RF
1. Rybakin, V.; Gounko, N. V.; Spate, K.; Honing, S.; Majoul, I. V.;
Duden, R.; Noegel, A. A.: Crn7 interacts with AP-1 and is required
for the maintenance of Golgi morphology and protein export from the
Golgi. J. Biol. Chem. 281: 31070-31078, 2006.
2. Rybakin, V.; Stumpf, M.; Schulze, A.; Majoul, I. V.; Noegel, A.
A.; Hasse, A.: Coronin 7, the mammalian POD-1 homologue, localizes
to the Golgi apparatus. FEBS Lett. 573: 161-167, 2004.
*FIELD* CD
Dorothy S. Reilly: 12/13/2007
*FIELD* ED
wwang: 12/14/2007
wwang: 12/13/2007
*RECORD*
*FIELD* NO
611668
*FIELD* TI
*611668 CORONIN 7; CORO7
;;POLARITY-OSMOTIC DEFECTIVE 1, DROSOPHILA, HOMOLOG OF; POD1;;
read moreCRN7
*FIELD* TX
DESCRIPTION
Coronins, such as CORO7, constitute an evolutionarily conserved family
of WD-repeat actin-binding proteins. CORO7 plays a role in Golgi complex
morphology and function (Rybakin et al., 2004, 2006).
CLONING
By EST database analysis, followed by RT-PCR of human liver carcinoma
cDNA, Rybakin et al. (2004) cloned CORO7, which they called CRN7. The
deduced 924-amino acid protein has a calculated molecular mass of 100.5
kD, which was confirmed experimentally. CORO7 contains 2 coronin WD
repeat-containing domains with a proline-, serine-, and
threonine-enriched region (PST motif) preceding the second WD-repeat.
CORO7 shares 30% and 29% amino acid identity with Drosophila Pod1 and C.
elegans Pod1, respectively. Northern blot analysis detected expression
in mouse embryos as early as day 5 postcoitum and expression increased
through day 15. Coro7 expression was detected in most mouse tissues
examined with high levels in brain, thymus, and kidney and low levels in
heart, liver, testis, and muscle. Western blot analysis of mouse tissues
showed a similar distribution of Coro7 with low expression in skeletal
and heart muscle. Immunofluorescence studies detected developmental
expression of mouse Coro7 in embryonic brain, thymus, intestine, skin,
and eye. Indirect immunofluorescence studies detected Coro7 in
vesicle-like structures and in a Golgi-like perinuclear compartment in
mouse fibroblasts. Sucrose gradient centrifugation and
immunoprecipitation studies demonstrated that Coro7 localized to
cytosolic vesicles and to the cis-Golgi region. The membrane-associated
form of Coro7 was tyrosine-phosphorylated, whereas the cytosolic form
was not.
GENE FUNCTION
By electron microscopy, Rybakin et al. (2006) showed that siRNA
knockdown of CORO7 in HeLa cells caused loss of Golgi integrity and
membrane scattering. CORO7 knockdown caused a defect in Golgi export of
vesicular stomatitis virus glycoprotein (VSVG) but did not alter protein
import into the trans-Golgi network. Golgi cargo glycosylation was not
affected. Using in vitro binding, coimmunoprecipitation, and
colocalization studies, the authors demonstrated that CORO7 interacted
with clathrin adaptor AP1 (see 600157) and that this interaction takes
place at Golgi membranes. Rybakin et al. (2006) showed that CORO7 was
not required for AP1 targeting to Golgi membranes and suggested that
CORO7 acts downstream of AP1 recruitment.
*FIELD* RF
1. Rybakin, V.; Gounko, N. V.; Spate, K.; Honing, S.; Majoul, I. V.;
Duden, R.; Noegel, A. A.: Crn7 interacts with AP-1 and is required
for the maintenance of Golgi morphology and protein export from the
Golgi. J. Biol. Chem. 281: 31070-31078, 2006.
2. Rybakin, V.; Stumpf, M.; Schulze, A.; Majoul, I. V.; Noegel, A.
A.; Hasse, A.: Coronin 7, the mammalian POD-1 homologue, localizes
to the Golgi apparatus. FEBS Lett. 573: 161-167, 2004.
*FIELD* CD
Dorothy S. Reilly: 12/13/2007
*FIELD* ED
wwang: 12/14/2007
wwang: 12/13/2007