MIA_HUMAN
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 03-AUG-2022, entry version 176.
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}.
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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.ENSP00000263369; -.
DR iPTMnet; Q16674; -.
DR PhosphoSitePlus; Q16674; -.
DR BioMuta; MIA; -.
DR DMDM; 2498559; -.
DR MassIVE; Q16674; -.
DR PaxDb; Q16674; -.
DR PeptideAtlas; Q16674; -.
DR PRIDE; Q16674; -.
DR ProteomicsDB; 61031; -. [Q16674-1]
DR Antibodypedia; 60691; 238 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 CTD; 8190; -.
DR DisGeNET; 8190; -.
DR GeneCards; MIA; -.
DR HGNC; HGNC:7076; MIA.
DR HPA; ENSG00000261857; Group enriched (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; EVKTDKW; -.
DR PhylomeDB; Q16674; -.
DR TreeFam; TF332724; -.
DR PathwayCommons; Q16674; -.
DR SignaLink; Q16674; -.
DR BioGRID-ORCS; 8190; 9 hits in 1057 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 96 other tissues.
DR ExpressionAtlas; Q16674; baseline and differential.
DR Genevisible; Q16674; HS.
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 InterPro; IPR043369; MIA.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR47312; PTHR47312; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
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
