R3HCL_MOUSE
ID R3HCL_MOUSE Reviewed; 775 AA.
AC Q8BJM3; Q3UGJ8; Q5U5U8;
DT 02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Coiled-coil domain-containing protein R3HCC1L;
DE AltName: Full=Growth inhibition and differentiation-related protein 88 homolog;
DE AltName: Full=R3H and coiled-coil domain-containing protein 1-like;
GN Name=R3hcc1l; Synonyms=D19Ertd386e, Gidrp88;
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;
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 STRAIN=Czech II; TISSUE=Mammary gland;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-695, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 -!- SUBUNIT: May interact with the exon junction complex (EJC) composed at
CC least of CASC3, EIF4A3, MAGOH and RBM8A. {ECO:0000250}.
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; AK082926; BAC38694.1; -; mRNA.
DR EMBL; AK147893; BAE28210.1; -; mRNA.
DR EMBL; BC038935; AAH38935.1; -; mRNA.
DR CCDS; CCDS29829.1; -.
DR RefSeq; NP_803415.1; NM_177464.4.
DR AlphaFoldDB; Q8BJM3; -.
DR SMR; Q8BJM3; -.
DR STRING; 10090.ENSMUSP00000026188; -.
DR iPTMnet; Q8BJM3; -.
DR PhosphoSitePlus; Q8BJM3; -.
DR EPD; Q8BJM3; -.
DR MaxQB; Q8BJM3; -.
DR PaxDb; Q8BJM3; -.
DR PRIDE; Q8BJM3; -.
DR ProteomicsDB; 253135; -.
DR Antibodypedia; 52284; 102 antibodies from 24 providers.
DR Ensembl; ENSMUST00000026188; ENSMUSP00000026188; ENSMUSG00000025184.
DR GeneID; 52013; -.
DR KEGG; mmu:52013; -.
DR UCSC; uc008hnq.1; mouse.
DR CTD; 27291; -.
DR MGI; MGI:1196316; R3hcc1l.
DR VEuPathDB; HostDB:ENSMUSG00000025184; -.
DR eggNOG; KOG4483; Eukaryota.
DR GeneTree; ENSGT00530000063711; -.
DR HOGENOM; CLU_025109_0_0_1; -.
DR InParanoid; Q8BJM3; -.
DR OMA; CEENDST; -.
DR OrthoDB; 844916at2759; -.
DR PhylomeDB; Q8BJM3; -.
DR TreeFam; TF324168; -.
DR BioGRID-ORCS; 52013; 1 hit in 72 CRISPR screens.
DR ChiTaRS; R3hcc1l; mouse.
DR PRO; PR:Q8BJM3; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8BJM3; protein.
DR Bgee; ENSMUSG00000025184; Expressed in granulocyte and 210 other tissues.
DR ExpressionAtlas; Q8BJM3; baseline and differential.
DR Genevisible; Q8BJM3; MM.
DR GO; GO:0035145; C:exon-exon junction complex; ISO:MGI.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR039884; R3HC1/R3HCL.
DR PANTHER; PTHR21678; PTHR21678; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Phosphoprotein; Reference proteome.
FT CHAIN 1..775
FT /note="Coiled-coil domain-containing protein R3HCC1L"
FT /id="PRO_0000087488"
FT REGION 1..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 7..27
FT /note="EJC-binding motif; may mediate interaction with the
FT EJC"
FT /evidence="ECO:0000250"
FT REGION 235..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 734..766
FT /evidence="ECO:0000255"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5L2"
FT MOD_RES 695
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 72
FT /note="G -> D (in Ref. 2; AAH38935)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="C -> G (in Ref. 2; AAH38935)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="C -> F (in Ref. 2; AAH38935)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="K -> E (in Ref. 2; AAH38935)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="S -> F (in Ref. 2; AAH38935)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="T -> S (in Ref. 2; AAH38935)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="A -> V (in Ref. 2; AAH38935)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="K -> E (in Ref. 2; AAH38935)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="D -> N (in Ref. 2; AAH38935)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="T -> S (in Ref. 2; AAH38935)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 775 AA; 84481 MW; FAEB7A971F2675AD CRC64;
MQQEAERCRV RTKRPDMALY VPKARRGTAL LKSSDQEEGH GPPAFVPKDQ KEGCLPQKIS
ASKPESQRRG AGHSDRKDVD CREGKRSASQ LRKDRCPQKQ NKEKACSKKG AEESTEASSQ
EHQHRAPDAG IVSSIPLQRL FKPKDMDCWE VQTAGATGHW RVSPSQSSSE VSAAQVPSRP
FQNVELCDFS GETFVNRNLE SSIVTEAKVP ELVSQFPQVV TTLLKPDGMA MPVTLSSDSE
TAPSSLETPD GMSKHSPGDI SVVSVPGGPD EDVDSTFVDF EVESEGTVNS TESVLGQKGV
DSILETVDNV SLKMAVVSKL ESTNGTIDPA VTRECESDSS ADELCVKSEP SDTAVLVHEI
DTDDGFRNVC DSTSKACMVD IAGTACDPVT EGSSCTGAVG ESGESSGNMR NFSDYIEMSA
DVAPLDRAKS ENDSENISSL SACSDIYAES IASGFTESTG KLIESVSDGA SSLPIKKTAD
SNIATCLDSE LSMSDASDVL LESALGSDLD TTEEMTEALH DLKTAEEFKT KEEDYSESVV
CGISFSDSSV ETSVDLKTTD TSHIQGSSAV EESWESMFND DGDCVDPRLL LELSGNVKNR
KSIQEPRFDY YSHELPDIDL SECEFPHVIE IYDFPQEFRT EDLLRIFCSY QKKGFDIKWV
DDTHALGVFA SPITARDALG TKHTMVKIRP LSQATRAAKA KARACAEFLQ PAKERPETSA
ALARRLVISA LGVRSKQSKT EREAELRKLQ EARERKRLEA KQREDIWEGR DQSVV
