MYDGF_HUMAN
ID MYDGF_HUMAN Reviewed; 173 AA.
AC Q969H8; D6W628; O75256; O75272; Q9BTK7; Q9NP69;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Myeloid-derived growth factor {ECO:0000303|PubMed:25581518, ECO:0000312|HGNC:HGNC:16948};
DE Short=MYDGF {ECO:0000303|PubMed:25581518};
DE Flags: Precursor;
GN Name=MYDGF {ECO:0000312|HGNC:HGNC:16948};
GN Synonyms=C19orf10 {ECO:0000312|HGNC:HGNC:16948};
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Skin;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-173.
RG The European IMAGE consortium;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 32-44.
RC TISSUE=Leukemic T-cell;
RX PubMed=19892738; DOI=10.1073/pnas.0908958106;
RA Xu G., Shin S.B., Jaffrey S.R.;
RT "Global profiling of protease cleavage sites by chemoselective labeling of
RT protein N-termini.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN [6]
RP RETRACTED PAPER.
RC TISSUE=Bone marrow;
RX PubMed=11714798; DOI=10.4049/jimmunol.167.11.6338;
RA Tulin E.E., Onoda N., Nakata Y., Maeda M., Hasegawa M., Nomura H.,
RA Kitamura T.;
RT "SF20/IL-25, a novel bone marrow stroma-derived growth factor that binds to
RT mouse thymic shared antigen-1 and supports lymphoid cell proliferation.";
RL J. Immunol. 167:6338-6347(2001).
RN [7]
RP RETRACTION NOTICE OF PUBMED:11714798.
RX PubMed=12538725; DOI=10.4049/jimmunol.170.3.1593;
RA Tulin E.E., Onoda N., Nakata Y., Maeda M., Hasegawa M., Nomura H.,
RA Kitamura T.;
RL J. Immunol. 170:1593-1593(2003).
RN [8]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=17362502; DOI=10.1186/ar2145;
RA Weiler T., Du Q., Krokhin O., Ens W., Standing K., El-Gabalawy H.,
RA Wilkins J.A.;
RT "The identification and characterization of a novel protein, c19orf10, in
RT the synovium.";
RL Arthritis Res. Ther. 9:R30-R30(2007).
RN [9]
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., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=25581518; DOI=10.1038/nm.3778;
RA Korf-Klingebiel M., Reboll M.R., Klede S., Brod T., Pich A., Polten F.,
RA Napp L.C., Bauersachs J., Ganser A., Brinkmann E., Reimann I., Kempf T.,
RA Niessen H.W., Mizrahi J., Schoenfeld H.J., Iglesias A., Bobadilla M.,
RA Wang Y., Wollert K.C.;
RT "Myeloid-derived growth factor (C19orf10) mediates cardiac repair following
RT myocardial infarction.";
RL Nat. Med. 21:140-149(2015).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 172-GLU-LEU-173.
RX PubMed=29954947; DOI=10.1074/jbc.ac118.002052;
RA Bortnov V., Annis D.S., Fogerty F.J., Barretto K.T., Turton K.B.,
RA Mosher D.F.;
RT "Myeloid-derived growth factor is a resident endoplasmic reticulum
RT protein.";
RL J. Biol. Chem. 293:13166-13175(2018).
CC -!- FUNCTION: Bone marrow-derived monocyte and paracrine-acting protein
CC that promotes cardiac myocyte survival and adaptive angiogenesis for
CC cardiac protection and/or repair after myocardial infarction (MI).
CC Stimulates endothelial cell proliferation through a MAPK1/3-,
CC STAT3- and CCND1-mediated signaling pathway. Inhibits cardiac myocyte
CC apoptosis in a PI3K/AKT-dependent signaling pathway (By similarity).
CC Involved in endothelial cell proliferation and angiogenesis
CC (PubMed:25581518). {ECO:0000250|UniProtKB:Q9CPT4,
CC ECO:0000269|PubMed:25581518}.
CC -!- INTERACTION:
CC Q969H8; Q9NPJ3: ACOT13; NbExp=3; IntAct=EBI-718622, EBI-1045357;
CC Q969H8; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-718622, EBI-742054;
CC Q969H8; O00303: EIF3F; NbExp=3; IntAct=EBI-718622, EBI-711990;
CC Q969H8; P84074: HPCA; NbExp=6; IntAct=EBI-718622, EBI-12197079;
CC Q969H8; P37235: HPCAL1; NbExp=4; IntAct=EBI-718622, EBI-749311;
CC Q969H8; P80188: LCN2; NbExp=3; IntAct=EBI-718622, EBI-11911016;
CC Q969H8; O43679: LDB2; NbExp=3; IntAct=EBI-718622, EBI-2865580;
CC Q969H8; P61601: NCALD; NbExp=5; IntAct=EBI-718622, EBI-749635;
CC Q969H8; O43765: SGTA; NbExp=8; IntAct=EBI-718622, EBI-347996;
CC Q969H8; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-718622, EBI-744081;
CC Q969H8; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-718622, EBI-741480;
CC Q969H8; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-718622, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17362502,
CC ECO:0000269|PubMed:25581518}. Endoplasmic reticulum-Golgi intermediate
CC compartment {ECO:0000269|PubMed:17362502}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:29954947}. Golgi apparatus
CC {ECO:0000269|PubMed:29954947}. Note=The C-terminal RTEL motif may
CC provide retention in the endoplasmic reticulum.
CC {ECO:0000269|PubMed:25581518, ECO:0000269|PubMed:29954947}.
CC -!- TISSUE SPECIFICITY: Expressed in eosinophils (at protein level)
CC (PubMed:29954947). Expressed in bone marrow cells (PubMed:25581518).
CC Expressed in synovial tissue. Found in synovial fluid of patients with
CC arthropaties (PubMed:17362502). {ECO:0000269|PubMed:17362502,
CC ECO:0000269|PubMed:25581518, ECO:0000269|PubMed:29954947}.
CC -!- INDUCTION: Up-regulated in response to myocardial infarction (MI).
CC {ECO:0000269|PubMed:25581518}.
CC -!- SIMILARITY: Belongs to the MYDGF family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to signal lymphoid cells to proliferate
CC via thymic shared antigen 1 (PubMed:11714798). This work was later
CC retracted (PubMed:12538725). {ECO:0000305|PubMed:11714798,
CC ECO:0000305|PubMed:12538725}.
CC -!- CAUTION: It has been reported that MYDGF is secreted into blood plasma
CC and localized to the endoplasmic reticulum-Golgi intermediate
CC compartment (PubMed:17362502, PubMed:25581518). However, another report
CC shows resident localization to the endoplasmic reticulum and Golgi
CC apparatus and secretion when the two most C-terminal residues of the
CC RTEL motif are abolished (PubMed:29954947).
CC {ECO:0000269|PubMed:17362502, ECO:0000269|PubMed:25581518,
CC ECO:0000269|PubMed:29954947}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC27824.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC33800.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005594; AAC33800.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC005339; AAC27824.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471139; EAW69202.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69203.1; -; Genomic_DNA.
DR EMBL; BC003639; AAH03639.2; -; mRNA.
DR EMBL; BC010129; AAH10129.1; -; mRNA.
DR EMBL; BC014655; AAH14655.1; -; mRNA.
DR EMBL; AL365373; CAB96947.1; -; mRNA.
DR EMBL; AL365374; CAB96948.1; -; mRNA.
DR CCDS; CCDS12133.1; -.
DR RefSeq; NP_061980.1; NM_019107.3.
DR PDB; 6O6W; NMR; -; A=32-173.
DR PDB; 6SVK; X-ray; 1.60 A; A/B=32-173.
DR PDB; 6SVL; X-ray; 1.58 A; C/F/J/N/Q/R=32-173.
DR PDBsum; 6O6W; -.
DR PDBsum; 6SVK; -.
DR PDBsum; 6SVL; -.
DR AlphaFoldDB; Q969H8; -.
DR SMR; Q969H8; -.
DR BioGRID; 121028; 33.
DR IntAct; Q969H8; 21.
DR STRING; 9606.ENSP00000262947; -.
DR iPTMnet; Q969H8; -.
DR MetOSite; Q969H8; -.
DR PhosphoSitePlus; Q969H8; -.
DR SwissPalm; Q969H8; -.
DR BioMuta; MYDGF; -.
DR DMDM; 61221730; -.
DR UCD-2DPAGE; Q969H8; -.
DR EPD; Q969H8; -.
DR jPOST; Q969H8; -.
DR MassIVE; Q969H8; -.
DR MaxQB; Q969H8; -.
DR PaxDb; Q969H8; -.
DR PeptideAtlas; Q969H8; -.
DR PRIDE; Q969H8; -.
DR ProteomicsDB; 75767; -.
DR TopDownProteomics; Q969H8; -.
DR ABCD; Q969H8; 1 sequenced antibody.
DR Antibodypedia; 23698; 241 antibodies from 29 providers.
DR DNASU; 56005; -.
DR Ensembl; ENST00000262947.8; ENSP00000262947.2; ENSG00000074842.8.
DR GeneID; 56005; -.
DR KEGG; hsa:56005; -.
DR MANE-Select; ENST00000262947.8; ENSP00000262947.2; NM_019107.4; NP_061980.1.
DR UCSC; uc002may.4; human.
DR CTD; 56005; -.
DR DisGeNET; 56005; -.
DR GeneCards; MYDGF; -.
DR HGNC; HGNC:16948; MYDGF.
DR HPA; ENSG00000074842; Low tissue specificity.
DR MIM; 606746; gene.
DR neXtProt; NX_Q969H8; -.
DR OpenTargets; ENSG00000074842; -.
DR PharmGKB; PA29827; -.
DR VEuPathDB; HostDB:ENSG00000074842; -.
DR eggNOG; ENOG502RZK9; Eukaryota.
DR GeneTree; ENSGT00390000000777; -.
DR HOGENOM; CLU_132160_0_0_1; -.
DR InParanoid; Q969H8; -.
DR OMA; TKIEYAN; -.
DR OrthoDB; 1577767at2759; -.
DR PhylomeDB; Q969H8; -.
DR TreeFam; TF332795; -.
DR PathwayCommons; Q969H8; -.
DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR SignaLink; Q969H8; -.
DR BioGRID-ORCS; 56005; 15 hits in 1081 CRISPR screens.
DR ChiTaRS; MYDGF; human.
DR GenomeRNAi; 56005; -.
DR Pharos; Q969H8; Tbio.
DR PRO; PR:Q969H8; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q969H8; protein.
DR Bgee; ENSG00000074842; Expressed in stromal cell of endometrium and 204 other tissues.
DR ExpressionAtlas; Q969H8; baseline and differential.
DR Genevisible; Q969H8; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR InterPro; IPR018887; MYDGF.
DR PANTHER; PTHR31230; PTHR31230; 1.
DR Pfam; PF10572; UPF0556; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Angiogenesis; Apoptosis; Direct protein sequencing;
KW Endoplasmic reticulum; Golgi apparatus; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:19892738"
FT CHAIN 32..173
FT /note="Myeloid-derived growth factor"
FT /id="PRO_0000021008"
FT VARIANT 12
FT /note="G -> R (in dbSNP:rs2270090)"
FT /id="VAR_060183"
FT MUTAGEN 172..173
FT /note="Missing: Increased secretion."
FT /evidence="ECO:0000269|PubMed:29954947"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:6SVL"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:6SVL"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:6SVL"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:6SVL"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:6SVL"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:6SVL"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:6SVL"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:6SVL"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:6SVL"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:6SVL"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:6SVL"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:6SVL"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:6SVL"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:6SVL"
SQ SEQUENCE 173 AA; 18795 MW; DD8910DEFEA5E3FC CRC64;
MAAPSGGWNG VGASLWAALL LGAVALRPAE AVSEPTTVAF DVRPGGVVHS FSHNVGPGDK
YTCMFTYASQ GGTNEQWQMS LGTSEDHQHF TCTIWRPQGK SYLYFTQFKA EVRGAEIEYA
MAYSKAAFER ESDVPLKTEE FEVTKTAVAH RPGAFKAELS KLVIVAKASR TEL
