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CYHR1_MOUSE
ID   CYHR1_MOUSE             Reviewed;         311 AA.
AC   Q9QXA1; Q6P6J7; Q6ZQA2; Q9D134;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Cysteine and histidine-rich protein 1;
GN   Name=Cyhr1; Synonyms=Chrp, Kiaa0496;
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 [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND INTERACTION WITH LGALS3.
RX   PubMed=10745073; DOI=10.1016/s0014-5793(00)01310-7;
RA   Menon R.P., Strom M., Hughes R.C.;
RT   "Interaction of a novel cysteine and histidine-rich cytoplasmic protein
RT   with galectin-3 in a carbohydrate-independent manner galectin 3.";
RL   FEBS Lett. 470:227-231(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Embryonic tail;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC   STRAIN=FVB/N; TISSUE=Limb, and Mammary tumor;
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   [5]
RP   INTERACTION WITH LGALS3.
RX   PubMed=12765788; DOI=10.1016/s0300-9084(03)00007-5;
RA   Bawumia S., Barboni E.A., Menon R.P., Hughes R.C.;
RT   "Specificity of interactions of galectin-3 with Chrp, a cysteine- and
RT   histidine-rich cytoplasmic protein.";
RL   Biochimie 85:189-194(2003).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   -!- SUBUNIT: Interacts with LGALS3. {ECO:0000269|PubMed:10745073,
CC       ECO:0000269|PubMed:12765788}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10745073}.
CC       Cytoplasm, perinuclear region {ECO:0000269|PubMed:10745073}. Note=Shows
CC       a prominent perinuclear and cytoplasmic localization.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9QXA1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9QXA1-2; Sequence=VSP_032822, VSP_032824;
CC       Name=3;
CC         IsoId=Q9QXA1-3; Sequence=VSP_032821, VSP_032824;
CC       Name=4;
CC         IsoId=Q9QXA1-4; Sequence=VSP_032823;
CC   -!- TISSUE SPECIFICITY: Expressed in heart, brain, liver, testis and
CC       kidney. {ECO:0000269|PubMed:10745073}.
CC   -!- SIMILARITY: Belongs to the CYHR1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC97966.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ251516; CAB62575.1; -; mRNA.
DR   EMBL; AK129156; BAC97966.1; ALT_INIT; mRNA.
DR   EMBL; AK004009; BAB23122.1; -; mRNA.
DR   EMBL; BC016196; AAH16196.1; -; mRNA.
DR   EMBL; BC025112; AAH25112.1; -; mRNA.
DR   EMBL; BC062184; AAH62184.1; -; mRNA.
DR   EMBL; BC082772; AAH82772.1; -; mRNA.
DR   CCDS; CCDS27581.1; -. [Q9QXA1-1]
DR   CCDS; CCDS27582.1; -. [Q9QXA1-4]
DR   RefSeq; NP_001263251.1; NM_001276322.1. [Q9QXA1-4]
DR   RefSeq; NP_001263262.1; NM_001276333.1. [Q9QXA1-4]
DR   RefSeq; NP_001263263.1; NM_001276334.1. [Q9QXA1-4]
DR   RefSeq; NP_001263264.1; NM_001276335.1. [Q9QXA1-4]
DR   RefSeq; NP_062269.1; NM_019396.3. [Q9QXA1-1]
DR   RefSeq; NP_851293.1; NM_180962.2. [Q9QXA1-4]
DR   RefSeq; XP_006521232.1; XM_006521169.3. [Q9QXA1-1]
DR   AlphaFoldDB; Q9QXA1; -.
DR   BioGRID; 207579; 1.
DR   STRING; 10090.ENSMUSP00000080043; -.
DR   PhosphoSitePlus; Q9QXA1; -.
DR   EPD; Q9QXA1; -.
DR   MaxQB; Q9QXA1; -.
DR   PaxDb; Q9QXA1; -.
DR   PeptideAtlas; Q9QXA1; -.
DR   PRIDE; Q9QXA1; -.
DR   ProteomicsDB; 279134; -. [Q9QXA1-1]
DR   ProteomicsDB; 279135; -. [Q9QXA1-2]
DR   ProteomicsDB; 279136; -. [Q9QXA1-3]
DR   ProteomicsDB; 279137; -. [Q9QXA1-4]
DR   Antibodypedia; 52728; 24 antibodies from 11 providers.
DR   DNASU; 54151; -.
DR   Ensembl; ENSMUST00000066677; ENSMUSP00000063317; ENSMUSG00000053929. [Q9QXA1-4]
DR   Ensembl; ENSMUST00000081291; ENSMUSP00000080043; ENSMUSG00000053929. [Q9QXA1-1]
DR   Ensembl; ENSMUST00000177359; ENSMUSP00000135505; ENSMUSG00000053929. [Q9QXA1-4]
DR   Ensembl; ENSMUST00000231152; ENSMUSP00000155579; ENSMUSG00000053929. [Q9QXA1-4]
DR   GeneID; 54151; -.
DR   KEGG; mmu:54151; -.
DR   UCSC; uc007wlf.2; mouse. [Q9QXA1-1]
DR   UCSC; uc007wli.2; mouse. [Q9QXA1-4]
DR   CTD; 50626; -.
DR   MGI; MGI:1859320; Cyhr1.
DR   VEuPathDB; HostDB:ENSMUSG00000053929; -.
DR   eggNOG; KOG3002; Eukaryota.
DR   GeneTree; ENSGT00390000018258; -.
DR   HOGENOM; CLU_035849_0_0_1; -.
DR   InParanoid; Q9QXA1; -.
DR   OMA; TNEHERN; -.
DR   PhylomeDB; Q9QXA1; -.
DR   TreeFam; TF324281; -.
DR   BioGRID-ORCS; 54151; 2 hits in 69 CRISPR screens.
DR   ChiTaRS; Cyhr1; mouse.
DR   PRO; PR:Q9QXA1; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q9QXA1; protein.
DR   Bgee; ENSMUSG00000053929; Expressed in ileal epithelium and 265 other tissues.
DR   ExpressionAtlas; Q9QXA1; baseline and differential.
DR   Genevisible; Q9QXA1; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR039338; CYHR1.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001293; Znf_TRAF.
DR   PANTHER; PTHR23059; PTHR23059; 1.
DR   PROSITE; PS50145; ZF_TRAF; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Metal-binding; Reference proteome; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..311
FT                   /note="Cysteine and histidine-rich protein 1"
FT                   /id="PRO_0000328853"
FT   ZN_FING         17..63
FT                   /note="RING-type; degenerate"
FT   ZN_FING         59..132
FT                   /note="TRAF-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
FT   VAR_SEQ         1..37
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14621295"
FT                   /id="VSP_032821"
FT   VAR_SEQ         1..30
FT                   /note="MVSKPRTEWSTVLSHLVLAGVSLHAAVSSV -> MSGAEEAGGGGPAAGPAG
FT                   AVPAGVGVGAGPGAAAGPAAAALGEAAGPGIPDEAALAGARQLQEAAGDPDAPPKKRLR
FT                   AAEAAEAAAAAVAAGSGKLEERLYSVLCCTVCLDLPKASVY (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_032822"
FT   VAR_SEQ         32..311
FT                   /note="CTNGHLMCAGCFIHLLADARLKEEQATCPNCRCEISKSLCCRNLAVEKAVSE
FT                   LPSECGFCLRQFPRSLLERHQKEECQDRVTQCKYKRIGCPWHGPFHELTVHEAACAHPT
FT                   KTGNELMEILDEMDQSHRKEMQLYNSIFSLLSFEKIGYTEVQFRPYRTDDFITRLYYET
FT                   PRFTVLNQTWVLKARVNDSERNPNLSCKRTLSFQLLLKSKVTAPLECSFLLLKGPYDDV
FT                   RISPVIYHFVFTNESNETDYVPLPIIDSVECNKLLAAKNINLRLFLFQIQK -> SSRG
FT                   AAAGFLLQTFAAIIMLAPGPSTHEDCLAGAWVATVIGLPLLAFDFHWVNGDRSSANLLL
FT                   GGGMVLAVAGDHLGPEGCSVAGQAVLLVVAVTILIVAVFTANTYGMWGGTLLGVAGLLS
FT                   RLEEDRLLLLPKEDVCRWALAAGSWAYCRALHTQRLQWE (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_032823"
FT   VAR_SEQ         182..311
FT                   /note="EVQFRPYRTDDFITRLYYETPRFTVLNQTWVLKARVNDSERNPNLSCKRTLS
FT                   FQLLLKSKVTAPLECSFLLLKGPYDDVRISPVIYHFVFTNESNETDYVPLPIIDSVECN
FT                   KLLAAKNINLRLFLFQIQK -> VWVFGPYLWSTEQEEHSIKSDPVYRCSLKATEPPEA
FT                   GKKLFGDRVPEQAEGLSSNCRTGNGCPQMSKLDQARPTGSHGSRASVTSSEHVGEQEPG
FT                   HTLGQRTRSTC (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14621295,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_032824"
SQ   SEQUENCE   311 AA;  35757 MW;  C9DBBAEE3939E6DF CRC64;
     MVSKPRTEWS TVLSHLVLAG VSLHAAVSSV QCTNGHLMCA GCFIHLLADA RLKEEQATCP
     NCRCEISKSL CCRNLAVEKA VSELPSECGF CLRQFPRSLL ERHQKEECQD RVTQCKYKRI
     GCPWHGPFHE LTVHEAACAH PTKTGNELME ILDEMDQSHR KEMQLYNSIF SLLSFEKIGY
     TEVQFRPYRT DDFITRLYYE TPRFTVLNQT WVLKARVNDS ERNPNLSCKR TLSFQLLLKS
     KVTAPLECSF LLLKGPYDDV RISPVIYHFV FTNESNETDY VPLPIIDSVE CNKLLAAKNI
     NLRLFLFQIQ K
 
 
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