ID   IBP7_MOUSE              Reviewed;         281 AA.
AC   Q61581; O88812; Q9EQW0;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2002, sequence version 3.
DT   24-JAN-2024, entry version 174.
DE   RecName: Full=Insulin-like growth factor-binding protein 7;
DE            Short=IBP-7;
DE            Short=IGF-binding protein 7;
DE            Short=IGFBP-7;
DE   AltName: Full=MAC25 protein;
DE   Flags: Precursor;
GN   Name=Igfbp7; Synonyms=Mac25;
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], AND RNA EDITING OF POSITION 94.
RC   TISSUE=Spleen;
RX   PubMed=8649839;
RA   Kato M.V., Sato H., Tsukada T., Ikawa Y., Aizawa S., Nagayoshi M.;
RT   "A follistatin-like gene, mac25, may act as a growth suppressor of
RT   osteosarcoma cells.";
RL   Oncogene 12:1361-1364(1996).
RN   [2]
RP   SEQUENCE REVISION.
RX   PubMed=10859029; DOI=10.1007/s0089400060126;
RA   Kato M.V.;
RT   "A secreted tumor-suppressor, mac25, with activin-binding activity.";
RL   Mol. Med. 6:126-135(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J;
RX   PubMed=10623583; DOI=10.1006/bbrc.1999.1937;
RA   Komatsu S., Okazaki Y., Tateno M., Kawai J., Konno H., Kusakabe M.,
RA   Yoshiki A., Muramatsu M., Held W.A., Hayashizaki Y.;
RT   "Methylation and downregulated expression of mac25/insulin-like growth
RT   factor binding protein-7 is associated with liver tumorigenesis in SV40T/t
RT   antigen transgenic mice, screened by restriction landmark genomic scanning
RT   for methylation (RLGS-M).";
RL   Biochem. Biophys. Res. Commun. 267:109-117(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-157.
RX   PubMed=11112448; DOI=10.1006/bbrc.2000.3944;
RA   Kanemitsu N., Kato M.V., Miki T., Komatsu S., Okazaki Y., Hayashizaki Y.,
RA   Sakai T.;
RT   "Characterization of the promoter of the murine mac25 gene.";
RL   Biochem. Biophys. Res. Commun. 279:251-257(2000).
RN   [5]
RP   RNA EDITING OF POSITIONS 77 AND 94.
RX   PubMed=18772245; DOI=10.1261/rna.816908;
RA   Gommans W.M., Tatalias N.E., Sie C.P., Dupuis D., Vendetti N., Smith L.,
RA   Kaushal R., Maas S.;
RT   "Screening of human SNP database identifies recoding sites of A-to-I RNA
RT   editing.";
RL   RNA 14:2074-2085(2008).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, Kidney, Lung, Spleen, and 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).
CC   -!- FUNCTION: Binds IGF-I and IGF-II with a relatively low affinity
CC       Stimulates prostacyclin (PGI2) production. Stimulates cell adhesion (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in lung, kidney, small
CC       intestine, testis and uterus and at moderate levels in liver.
CC       {ECO:0000269|PubMed:10623583}.
CC   -!- INDUCTION: By retinoic acid.
CC   -!- RNA EDITING: Modified_positions=77 {ECO:0000269|PubMed:18772245}, 94
CC       {ECO:0000269|PubMed:18772245, ECO:0000269|PubMed:8649839};
CC       Note=Partially edited. Position 77 seems to be edited at about 56% and
CC       position 94 at about 58%.;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB17228.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L75822; AAC37696.2; -; mRNA.
DR   EMBL; AB012886; BAA33569.1; -; mRNA.
DR   EMBL; AB042198; BAB17228.1; ALT_INIT; Genomic_DNA.
DR   CCDS; CCDS51529.1; -.
DR   RefSeq; NP_032074.3; NM_008048.3.
DR   AlphaFoldDB; Q61581; -.
DR   SMR; Q61581; -.
DR   BioGRID; 205897; 6.
DR   STRING; 10090.ENSMUSP00000128318; -.
DR   GlyCosmos; Q61581; 1 site, No reported glycans.
DR   GlyGen; Q61581; 1 site.
DR   PhosphoSitePlus; Q61581; -.
DR   CPTAC; non-CPTAC-3466; -.
DR   jPOST; Q61581; -.
DR   MaxQB; Q61581; -.
DR   PaxDb; 10090-ENSMUSP00000128318; -.
DR   PeptideAtlas; Q61581; -.
DR   ProteomicsDB; 267083; -.
DR   Pumba; Q61581; -.
DR   DNASU; 29817; -.
DR   Ensembl; ENSMUST00000046746.10; ENSMUSP00000045057.8; ENSMUSG00000036256.14.
DR   GeneID; 29817; -.
DR   KEGG; mmu:29817; -.
DR   AGR; MGI:1352480; -.
DR   CTD; 3490; -.
DR   MGI; MGI:1352480; Igfbp7.
DR   eggNOG; ENOG502RACD; Eukaryota.
DR   GeneTree; ENSGT00530000063555; -.
DR   InParanoid; Q61581; -.
DR   OrthoDB; 3019991at2759; -.
DR   PhylomeDB; Q61581; -.
DR   Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR   BioGRID-ORCS; 29817; 2 hits in 81 CRISPR screens.
DR   ChiTaRS; Igfbp7; mouse.
DR   PRO; PR:Q61581; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q61581; Protein.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR   GO; GO:0005520; F:insulin-like growth factor binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR   GO; GO:0048839; P:inner ear development; IDA:MGI.
DR   GO; GO:0001558; P:regulation of cell growth; IEA:InterPro.
DR   GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
DR   GO; GO:0050810; P:regulation of steroid biosynthetic process; ISO:MGI.
DR   CDD; cd00104; KAZAL_FS; 1.
DR   Gene3D; 3.30.60.30; -; 1.
DR   Gene3D; 4.10.40.20; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR000867; IGFBP-like.
DR   InterPro; IPR011390; IGFBP_rP_mac25.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   PANTHER; PTHR14186; INSULIN-LIKE GROWTH FACTOR BINDING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR14186:SF15; INSULIN-LIKE GROWTH FACTOR-BINDING PROTEIN 7; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00219; IGFBP; 1.
DR   Pfam; PF07648; Kazal_2; 1.
DR   PIRSF; PIRSF018239; IGFBP_rP_mac25; 1.
DR   SMART; SM00121; IB; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00280; KAZAL; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51323; IGFBP_N_2; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
PE   1: Evidence at protein level;
KW   Cell adhesion; Disulfide bond; Glycoprotein; Growth factor binding;
KW   Immunoglobulin domain; Phosphoprotein; Reference proteome; RNA editing;
KW   Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..281
FT                   /note="Insulin-like growth factor-binding protein 7"
FT                   /id="PRO_0000014393"
FT   DOMAIN          27..113
FT                   /note="IGFBP N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DOMAIN          98..157
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DOMAIN          159..263
FT                   /note="Ig-like C2-type"
FT   MOD_RES         238
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16270"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..56
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        34..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        39..59
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        47..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        70..86
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        80..110
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        112..130
FT                   /evidence="ECO:0000305"
FT   DISULFID        119..155
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        180..247
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VARIANT         77
FT                   /note="R -> G (in RNA edited version)"
FT   VARIANT         94
FT                   /note="K -> R (in RNA edited version)"
FT   CONFLICT        146
FT                   /note="A -> P (in Ref. 1; AAC37696)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   281 AA;  28969 MW;  A70AE6B7D2D4AB58 CRC64;
     MERPPRALLL GAAGLLLLLL PLSSSSSSDA CGPCVPASCP ALPRLGCPLG ETRDACGCCP
     VCARGEGEPC GGGAAGRGHC APGMECVKSR KRRKGKAGAA AGGPATLAVC VCKSRYPVCG
     SNGITYPSGC QLRAASLRAE SRGEKAITQV SKGTCEQGPS IVTPPKDIWN VTGAKVFLSC
     EVIGIPTPVL IWNKVKRDHS GVQRTELLPG DRENLAIQTR GGPEKHEVTG WVLVSPLSKE
     DAGEYECHAS NSQGQASAAA KITVVDALHE IPLKKGEGAQ L
//