IBP7_MOUSE
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 03-AUG-2022, entry version 167.
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 GlyGen; Q61581; 1 site.
DR PhosphoSitePlus; Q61581; -.
DR CPTAC; non-CPTAC-3466; -.
DR jPOST; Q61581; -.
DR MaxQB; Q61581; -.
DR PeptideAtlas; Q61581; -.
DR PRIDE; Q61581; -.
DR ProteomicsDB; 267083; -.
DR DNASU; 29817; -.
DR Ensembl; ENSMUST00000046746; ENSMUSP00000045057; ENSMUSG00000036256.
DR GeneID; 29817; -.
DR KEGG; mmu:29817; -.
DR CTD; 3490; -.
DR MGI; MGI:1352480; Igfbp7.
DR eggNOG; ENOG502RACD; Eukaryota.
DR GeneTree; ENSGT00530000063555; -.
DR InParanoid; Q61581; -.
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 76 CRISPR screens.
DR ChiTaRS; Igfbp7; mouse.
DR PRO; PR:Q61581; -.
DR Proteomes; UP000000589; Unplaced.
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 Gene3D; 2.60.40.10; -; 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; PTHR14186; 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; SSF100895; SSF100895; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF57184; SSF57184; 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..103
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 110..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
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
