HDGR3_MOUSE
ID HDGR3_MOUSE Reviewed; 202 AA.
AC Q9JMG7; Q3TRX2; Q8BQ69; Q8BR62; Q9D2M7;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Hepatoma-derived growth factor-related protein 3;
DE Short=HRP-3;
GN Name=Hdgfl3; Synonyms=Hdgfrp3;
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).
RC TISSUE=Testis;
RX PubMed=10581169; DOI=10.1006/bbrc.1999.1733;
RA Ikegame K., Yamamoto M., Kishima Y., Enomoto H., Yoshida K., Suemura M.,
RA Kishimoto T., Nakamura H.;
RT "A new member of a hepatoma-derived growth factor gene family can
RT translocate to the nucleus.";
RL Biochem. Biophys. Res. Commun. 266:81-87(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Corpora quadrigemina, Diencephalon, Embryo, Embryonic ganglion, and
RC Skin;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-110; SER-121 AND SER-122, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC 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).
RN [5]
RP STRUCTURE BY NMR OF 8-90.
RX PubMed=15689505; DOI=10.1110/ps.04975305;
RA Nameki N., Tochio N., Koshiba S., Inoue M., Yabuki T., Aoki M., Seki E.,
RA Matsuda T., Fujikura Y., Saito M., Ikari M., Watanabe M., Terada T.,
RA Shirouzu M., Yoshida M., Hirota H., Tanaka A., Hayashizaki Y., Guntert P.,
RA Kigawa T., Yokoyama S.;
RT "Solution structure of the PWWP domain of the hepatoma-derived growth
RT factor family.";
RL Protein Sci. 14:756-764(2005).
CC -!- FUNCTION: Enhances DNA synthesis and may play a role in cell
CC proliferation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JMG7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JMG7-2; Sequence=VSP_014188;
CC -!- SIMILARITY: Belongs to the HDGF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC32413.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB029493; BAA90478.1; -; mRNA.
DR EMBL; AK019487; BAB31754.1; -; mRNA.
DR EMBL; AK044858; BAC32123.1; -; mRNA.
DR EMBL; AK045542; BAC32413.1; ALT_FRAME; mRNA.
DR EMBL; AK051401; BAC34628.1; -; mRNA.
DR EMBL; AK162418; BAE36904.1; -; mRNA.
DR EMBL; BC055734; AAH55734.1; -; mRNA.
DR CCDS; CCDS40011.1; -. [Q9JMG7-1]
DR RefSeq; NP_038914.2; NM_013886.4. [Q9JMG7-1]
DR PDB; 1N27; NMR; -; A=8-90.
DR PDBsum; 1N27; -.
DR AlphaFoldDB; Q9JMG7; -.
DR BMRB; Q9JMG7; -.
DR SMR; Q9JMG7; -.
DR BioGRID; 205940; 6.
DR IntAct; Q9JMG7; 1.
DR MINT; Q9JMG7; -.
DR STRING; 10090.ENSMUSP00000102926; -.
DR iPTMnet; Q9JMG7; -.
DR PhosphoSitePlus; Q9JMG7; -.
DR EPD; Q9JMG7; -.
DR jPOST; Q9JMG7; -.
DR MaxQB; Q9JMG7; -.
DR PaxDb; Q9JMG7; -.
DR PeptideAtlas; Q9JMG7; -.
DR PRIDE; Q9JMG7; -.
DR ProteomicsDB; 269650; -. [Q9JMG7-1]
DR ProteomicsDB; 269651; -. [Q9JMG7-2]
DR Antibodypedia; 28189; 194 antibodies from 29 providers.
DR DNASU; 29877; -.
DR Ensembl; ENSMUST00000026094; ENSMUSP00000026094; ENSMUSG00000025104. [Q9JMG7-2]
DR Ensembl; ENSMUST00000107305; ENSMUSP00000102926; ENSMUSG00000025104. [Q9JMG7-1]
DR GeneID; 29877; -.
DR KEGG; mmu:29877; -.
DR UCSC; uc009icr.1; mouse. [Q9JMG7-1]
DR UCSC; uc009ics.1; mouse. [Q9JMG7-2]
DR CTD; 50810; -.
DR MGI; MGI:1352760; Hdgfl3.
DR VEuPathDB; HostDB:ENSMUSG00000025104; -.
DR eggNOG; KOG1904; Eukaryota.
DR GeneTree; ENSGT00940000153942; -.
DR HOGENOM; CLU_090867_1_0_1; -.
DR InParanoid; Q9JMG7; -.
DR OMA; CIRNPFA; -.
DR OrthoDB; 530959at2759; -.
DR PhylomeDB; Q9JMG7; -.
DR TreeFam; TF105385; -.
DR BioGRID-ORCS; 29877; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Hdgfl3; mouse.
DR EvolutionaryTrace; Q9JMG7; -.
DR PRO; PR:Q9JMG7; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9JMG7; protein.
DR Bgee; ENSMUSG00000025104; Expressed in rostral migratory stream and 239 other tissues.
DR Genevisible; Q9JMG7; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; NAS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
DR GO; GO:0046785; P:microtubule polymerization; IDA:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd05834; HDGF_related; 1.
DR IDEAL; IID50182; -.
DR InterPro; IPR035496; HDGF-rel_PWWP.
DR InterPro; IPR000313; PWWP_dom.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00293; PWWP; 1.
DR PROSITE; PS50812; PWWP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Growth factor; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..202
FT /note="Hepatoma-derived growth factor-related protein 3"
FT /id="PRO_0000191704"
FT DOMAIN 11..68
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT REGION 90..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 135..147
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 94..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..154
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 110
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3E1"
FT VAR_SEQ 202
FT /note="T -> VRMC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014188"
FT CONFLICT 198..199
FT /note="AG -> TS (in Ref. 1; BAA90478)"
FT /evidence="ECO:0000305"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:1N27"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:1N27"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:1N27"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:1N27"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:1N27"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:1N27"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1N27"
FT HELIX 65..72
FT /evidence="ECO:0007829|PDB:1N27"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1N27"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:1N27"
SQ SEQUENCE 202 AA; 22431 MW; FCDB31BD2BEAB8D6 CRC64;
MARPRPREYK AGDLVFAKMK GYPHWPARID ELPEGAVKPP ANKYPIFFFG THETAFLGPK
DLFPYKEYKD KFGKSNKRKG FNEGLWEIEN NPGVKFTGYQ TIQQQSSSET EGEGGNTADA
SSEEEGDRVE DGKGKRKNEK GGSKRKKSYT SKKSSKQSRK SPGDEDDKDC KEEENKSSSE
GGDAGNDTRN TTADLQKAGE GT
