ID MIA_HUMAN Reviewed; 131 AA. AC Q16674; Q6FHV3; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 24-JAN-2024, entry version 184. DE RecName: Full=Melanoma-derived growth regulatory protein; DE AltName: Full=Melanoma inhibitory activity protein; DE Flags: Precursor; GN Name=MIA; 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] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE. RX PubMed=7923218; RA Blesch A., Bosserhoff A.-K., Apfel R., Behl C., Hessdoerfer B., Schmitt A., RA Jachimczak P., Lottspeich F., Buettner R., Bogdahn U.; RT "Cloning of a novel malignant melanoma-derived growth-regulatory protein, RT MIA."; RL Cancer Res. 54:5695-5701(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Placenta; RX PubMed=8550608; DOI=10.1074/jbc.271.1.490; RA Bosserhoff A.-K., Hein R., Bogdahn U., Buettner R.; RT "Structure and promoter analysis of the gene encoding the human melanoma- RT inhibiting protein MIA."; RL J. Biol. Chem. 271:490-495(1996). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND RP ALTERNATIVE SPLICING. RX PubMed=12230496; DOI=10.1046/j.1523-1747.2002.00501.x; RA Hau P., Wise P., Bosserhoff A.K., Blesch A., Jachimczak P., Tschertner I., RA Bogdahn U., Apfel R.; RT "Cloning and characterization of the expression pattern of a novel splice RT product MIA (splice) of malignant melanoma-derived growth-inhibiting RT activity (MIA/CD-RAP)."; RL J. Invest. Dermatol. 119:562-569(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=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 [8] RP PROTEIN SEQUENCE OF 25-39. RX PubMed=15340161; DOI=10.1110/ps.04682504; RA Zhang Z., Henzel W.J.; RT "Signal peptide prediction based on analysis of experimentally verified RT cleavage sites."; RL Protein Sci. 13:2819-2824(2004). RN [9] RP INTERACTION WITH FASLG. RX PubMed=19807924; DOI=10.1186/1471-2172-10-53; RA Voss M., Lettau M., Janssen O.; RT "Identification of SH3 domain interaction partners of human FasL (CD178) by RT phage display screening."; RL BMC Immunol. 10:53-53(2009). RN [10] RP INTERACTION WITH TMIGD2. RX PubMed=22419821; DOI=10.1091/mbc.e11-11-0934; RA Rahimi N., Rezazadeh K., Mahoney J.E., Hartsough E., Meyer R.D.; RT "Identification of IGPR-1 as a novel adhesion molecule involved in RT angiogenesis."; RL Mol. Biol. Cell 23:1646-1656(2012). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.39 ANGSTROMS) OF 25-131. RX PubMed=11331761; DOI=10.1073/pnas.091601698; RA Lougheed J.C., Holton J.M., Alber T., Bazan J.F., Handel T.M.; RT "Structure of melanoma inhibitory activity protein, a member of a recently RT identified family of secreted proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 98:5515-5520(2001). CC -!- FUNCTION: Elicits growth inhibition on melanoma cells in vitro as well CC as some other neuroectodermal tumors, including gliomas. CC -!- SUBUNIT: Interacts with FASLG. Interacts with TMIGD2. CC {ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:22419821}. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q16674-1; Sequence=Displayed; CC Name=2; Synonyms=MIA-splice; CC IsoId=Q16674-2; Sequence=VSP_044450; CC -!- TISSUE SPECIFICITY: All malignant melanoma cell lines tested and CC infrequently in glioma cell lines. CC -!- PTM: May possess two intramolecular disulfide bonds. CC -!- SIMILARITY: Belongs to the MIA/OTOR 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; X75450; CAA53203.1; -; mRNA. DR EMBL; X84707; CAA59195.1; -; Genomic_DNA. DR EMBL; BT007044; AAP35693.1; -; mRNA. DR EMBL; CR541648; CAG46449.1; -; mRNA. DR EMBL; CH471126; EAW56997.1; -; Genomic_DNA. DR EMBL; BC005910; AAH05910.1; -; mRNA. DR CCDS; CCDS12566.1; -. [Q16674-1] DR PIR; I38019; I38019. DR RefSeq; NP_001189482.1; NM_001202553.1. [Q16674-1] DR RefSeq; NP_006524.1; NM_006533.3. [Q16674-1] DR PDB; 1HJD; NMR; -; A=31-131. DR PDB; 1I1J; X-ray; 1.39 A; A/B=25-131. DR PDB; 1K0X; NMR; -; A=25-131. DR PDB; 5IXB; X-ray; 1.39 A; A/B=25-131. DR PDBsum; 1HJD; -. DR PDBsum; 1I1J; -. DR PDBsum; 1K0X; -. DR PDBsum; 5IXB; -. DR AlphaFoldDB; Q16674; -. DR BMRB; Q16674; -. DR SMR; Q16674; -. DR BioGRID; 113834; 3. DR IntAct; Q16674; 1. DR STRING; 9606.ENSP00000470129; -. DR iPTMnet; Q16674; -. DR PhosphoSitePlus; Q16674; -. DR BioMuta; MIA; -. DR DMDM; 2498559; -. DR MassIVE; Q16674; -. DR PaxDb; 9606-ENSP00000263369; -. DR PeptideAtlas; Q16674; -. DR ProteomicsDB; 61031; -. [Q16674-1] DR Antibodypedia; 60691; 269 antibodies from 33 providers. DR DNASU; 8190; -. DR Ensembl; ENST00000263369.4; ENSP00000263369.2; ENSG00000261857.7. [Q16674-1] DR Ensembl; ENST00000594436.5; ENSP00000470129.1; ENSG00000261857.7. [Q16674-1] DR Ensembl; ENST00000597784.5; ENSP00000469499.1; ENSG00000261857.7. [Q16674-1] DR GeneID; 8190; -. DR KEGG; hsa:8190; -. DR MANE-Select; ENST00000263369.4; ENSP00000263369.2; NM_006533.4; NP_006524.1. DR UCSC; uc002opb.5; human. [Q16674-1] DR AGR; HGNC:7076; -. DR CTD; 8190; -. DR DisGeNET; 8190; -. DR GeneCards; MIA; -. DR HGNC; HGNC:7076; MIA. DR HPA; ENSG00000261857; Tissue enhanced (breast, pituitary gland, salivary gland, stomach). DR MIM; 601340; gene. DR neXtProt; NX_Q16674; -. DR OpenTargets; ENSG00000261857; -. DR PharmGKB; PA30800; -. DR VEuPathDB; HostDB:ENSG00000261857; -. DR eggNOG; ENOG502S2XN; Eukaryota. DR GeneTree; ENSGT00950000182767; -. DR HOGENOM; CLU_158739_0_0_1; -. DR InParanoid; Q16674; -. DR OMA; AECSHPI; -. DR OrthoDB; 5342070at2759; -. DR PhylomeDB; Q16674; -. DR TreeFam; TF332724; -. DR PathwayCommons; Q16674; -. DR SignaLink; Q16674; -. DR BioGRID-ORCS; 8190; 10 hits in 1135 CRISPR screens. DR EvolutionaryTrace; Q16674; -. DR GeneWiki; Melanoma_inhibitory_activity; -. DR GenomeRNAi; 8190; -. DR Pharos; Q16674; Tbio. DR PRO; PR:Q16674; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q16674; Protein. DR Bgee; ENSG00000261857; Expressed in tibial nerve and 98 other cell types or tissues. DR ExpressionAtlas; Q16674; baseline and differential. DR GO; GO:0005615; C:extracellular space; TAS:ProtInc. DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW. DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central. DR CDD; cd11890; MIA; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR043369; MIA. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR47312; MELANOMA-DERIVED GROWTH REGULATORY PROTEIN; 1. DR PANTHER; PTHR47312:SF1; MELANOMA-DERIVED GROWTH REGULATORY PROTEIN; 1. DR Pfam; PF07653; SH3_2; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q16674; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Direct protein sequencing; KW Disulfide bond; Growth factor; Reference proteome; Secreted; SH3 domain; KW Signal. FT SIGNAL 1..24 FT /evidence="ECO:0000269|PubMed:15340161" FT CHAIN 25..131 FT /note="Melanoma-derived growth regulatory protein" FT /id="PRO_0000019028" FT DOMAIN 43..113 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DISULFID 36..41 FT DISULFID 59..130 FT VAR_SEQ 43..131 FT /note="HPISMAVALQDYMAPDCRFLTIHRGQVVYVFSKLKGRGRLFWGGSVQGDYYG FT DLAARLGYFPSSIVREDQTLKPGKVDVKTDKWDFYCQ -> RSGRLLWRSGCSPGLFPQ FT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12230496" FT /id="VSP_044450" FT STRAND 32..38 FT /evidence="ECO:0007829|PDB:1I1J" FT STRAND 45..52 FT /evidence="ECO:0007829|PDB:1I1J" FT STRAND 57..61 FT /evidence="ECO:0007829|PDB:1HJD" FT STRAND 69..76 FT /evidence="ECO:0007829|PDB:1I1J" FT HELIX 78..80 FT /evidence="ECO:0007829|PDB:1I1J" FT STRAND 83..89 FT /evidence="ECO:0007829|PDB:1I1J" FT STRAND 101..104 FT /evidence="ECO:0007829|PDB:1I1J" FT HELIX 105..107 FT /evidence="ECO:0007829|PDB:1I1J" FT STRAND 108..113 FT /evidence="ECO:0007829|PDB:1I1J" FT STRAND 119..122 FT /evidence="ECO:0007829|PDB:1I1J" FT HELIX 125..128 FT /evidence="ECO:0007829|PDB:5IXB" SQ SEQUENCE 131 AA; 14509 MW; 4D3BB30BD6008BDC CRC64; MARSLVCLGV IILLSAFSGP GVRGGPMPKL ADRKLCADQE CSHPISMAVA LQDYMAPDCR FLTIHRGQVV YVFSKLKGRG RLFWGGSVQG DYYGDLAARL GYFPSSIVRE DQTLKPGKVD VKTDKWDFYC Q //