ID   HDGR3_HUMAN             Reviewed;         203 AA.
AC   Q9Y3E1;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=Hepatoma-derived growth factor-related protein 3;
DE            Short=HRP-3;
DE   AltName: Full=Hepatoma-derived growth factor 2;
DE            Short=HDGF-2;
GN   Name=HDGFL3 {ECO:0000312|HGNC:HGNC:24937};
GN   Synonyms=HDGF2 {ECO:0000312|EMBL:AAM27001.1}, HDGFRP3;
GN   ORFNames=CGI-142;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Lymphocyte;
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 [MRNA].
RA   Yu L., Fu Q., Tu Q.;
RT   "Cloning of a novel human cDNA which is a homolog to mouse hepatoma-derived
RT   growth factor (mHDGF) and termed hHDGF2.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA   Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT   "Identification of novel human genes evolutionarily conserved in
RT   Caenorhabditis elegans by comparative proteomics.";
RL   Genome Res. 10:703-713(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Teratocarcinoma;
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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
CC   -!- FUNCTION: Enhances DNA synthesis and may play a role in cell
CC       proliferation. {ECO:0000269|PubMed:10581169}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10581169}.
CC   -!- TISSUE SPECIFICITY: Detected in testis, heart, spinal cord and brain.
CC       {ECO:0000269|PubMed:10581169}.
CC   -!- SIMILARITY: Belongs to the HDGF family. {ECO:0000305}.
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; AB029156; BAA90477.1; -; mRNA.
DR   EMBL; AF110642; AAM27001.1; -; mRNA.
DR   EMBL; AF151900; AAD34137.1; -; mRNA.
DR   EMBL; AK001280; BAA91597.1; -; mRNA.
DR   EMBL; BC015483; AAH15483.1; -; mRNA.
DR   CCDS; CCDS32314.1; -.
DR   PIR; JC7163; JC7163.
DR   RefSeq; NP_057157.1; NM_016073.3.
DR   PDB; 6IIP; X-ray; 0.95 A; A/B=8-94.
DR   PDB; 6IIQ; X-ray; 1.85 A; A/B/C=1-99.
DR   PDB; 6IIR; X-ray; 2.20 A; A/B=1-99.
DR   PDB; 6IIS; X-ray; 2.36 A; A/B=1-99.
DR   PDB; 6IIT; X-ray; 2.10 A; A/B=1-99.
DR   PDBsum; 6IIP; -.
DR   PDBsum; 6IIQ; -.
DR   PDBsum; 6IIR; -.
DR   PDBsum; 6IIS; -.
DR   PDBsum; 6IIT; -.
DR   AlphaFoldDB; Q9Y3E1; -.
DR   BMRB; Q9Y3E1; -.
DR   SMR; Q9Y3E1; -.
DR   BioGRID; 119129; 40.
DR   IntAct; Q9Y3E1; 18.
DR   STRING; 9606.ENSP00000299633; -.
DR   GlyGen; Q9Y3E1; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9Y3E1; -.
DR   PhosphoSitePlus; Q9Y3E1; -.
DR   SwissPalm; Q9Y3E1; -.
DR   BioMuta; HDGFL3; -.
DR   DMDM; 68052386; -.
DR   EPD; Q9Y3E1; -.
DR   jPOST; Q9Y3E1; -.
DR   MassIVE; Q9Y3E1; -.
DR   MaxQB; Q9Y3E1; -.
DR   PaxDb; 9606-ENSP00000299633; -.
DR   PeptideAtlas; Q9Y3E1; -.
DR   ProteomicsDB; 86028; -.
DR   Pumba; Q9Y3E1; -.
DR   TopDownProteomics; Q9Y3E1; -.
DR   Antibodypedia; 28189; 222 antibodies from 29 providers.
DR   DNASU; 50810; -.
DR   Ensembl; ENST00000299633.7; ENSP00000299633.4; ENSG00000166503.9.
DR   GeneID; 50810; -.
DR   KEGG; hsa:50810; -.
DR   MANE-Select; ENST00000299633.7; ENSP00000299633.4; NM_016073.4; NP_057157.1.
DR   UCSC; uc002bjs.3; human.
DR   AGR; HGNC:24937; -.
DR   CTD; 50810; -.
DR   DisGeNET; 50810; -.
DR   GeneCards; HDGFL3; -.
DR   HGNC; HGNC:24937; HDGFL3.
DR   HPA; ENSG00000166503; Low tissue specificity.
DR   neXtProt; NX_Q9Y3E1; -.
DR   OpenTargets; ENSG00000166503; -.
DR   VEuPathDB; HostDB:ENSG00000166503; -.
DR   eggNOG; KOG1904; Eukaryota.
DR   GeneTree; ENSGT00940000153942; -.
DR   HOGENOM; CLU_090867_1_0_1; -.
DR   InParanoid; Q9Y3E1; -.
DR   OMA; FTGYQAM; -.
DR   OrthoDB; 4271850at2759; -.
DR   PhylomeDB; Q9Y3E1; -.
DR   PathwayCommons; Q9Y3E1; -.
DR   SignaLink; Q9Y3E1; -.
DR   BioGRID-ORCS; 50810; 11 hits in 1116 CRISPR screens.
DR   ChiTaRS; HDGFL3; human.
DR   GeneWiki; HDGFRP3; -.
DR   GenomeRNAi; 50810; -.
DR   Pharos; Q9Y3E1; Tbio.
DR   PRO; PR:Q9Y3E1; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q9Y3E1; Protein.
DR   Bgee; ENSG00000166503; Expressed in cortical plate and 211 other cell types or tissues.
DR   ExpressionAtlas; Q9Y3E1; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0015631; F:tubulin binding; ISS:UniProtKB.
DR   GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0046785; P:microtubule polymerization; ISS:UniProtKB.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISS:UniProtKB.
DR   GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR   CDD; cd20150; PWWP_HDGFL3; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   InterPro; IPR000313; PWWP_dom.
DR   PANTHER; PTHR12550; HEPATOMA-DERIVED GROWTH FACTOR-RELATED; 1.
DR   PANTHER; PTHR12550:SF78; HEPATOMA-DERIVED GROWTH FACTOR-RELATED PROTEIN 3; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   SMART; SM00293; PWWP; 1.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR   PROSITE; PS50812; PWWP; 1.
DR   Genevisible; Q9Y3E1; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Growth factor; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..203
FT                   /note="Hepatoma-derived growth factor-related protein 3"
FT                   /id="PRO_0000191703"
FT   DOMAIN          11..68
FT                   /note="PWWP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT   REGION          97..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           136..148
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        97..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..155
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..181
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         110
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JMG7"
FT   MOD_RES         121
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JMG7"
FT   MOD_RES         122
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JMG7"
FT   MOD_RES         162
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   STRAND          14..17
FT                   /evidence="ECO:0007829|PDB:6IIP"
FT   STRAND          25..29
FT                   /evidence="ECO:0007829|PDB:6IIP"
FT   STRAND          34..36
FT                   /evidence="ECO:0007829|PDB:6IIT"
FT   STRAND          44..48
FT                   /evidence="ECO:0007829|PDB:6IIP"
FT   TURN            49..51
FT                   /evidence="ECO:0007829|PDB:6IIP"
FT   STRAND          54..57
FT                   /evidence="ECO:0007829|PDB:6IIP"
FT   HELIX           59..61
FT                   /evidence="ECO:0007829|PDB:6IIP"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:6IIP"
FT   HELIX           65..72
FT                   /evidence="ECO:0007829|PDB:6IIP"
FT   HELIX           79..90
FT                   /evidence="ECO:0007829|PDB:6IIP"
FT   TURN            92..95
FT                   /evidence="ECO:0007829|PDB:6IIQ"
SQ   SEQUENCE   203 AA;  22620 MW;  0B660D665F01659C CRC64;
     MARPRPREYK AGDLVFAKMK GYPHWPARID ELPEGAVKPP ANKYPIFFFG THETAFLGPK
     DLFPYKEYKD KFGKSNKRKG FNEGLWEIEN NPGVKFTGYQ AIQQQSSSET EGEGGNTADA
     SSEEEGDRVE EDGKGKRKNE KAGSKRKKSY TSKKSSKQSR KSPGDEDDKD CKEEENKSSS
     EGGDAGNDTR NTTSDLQKTS EGT
//