ID IBPL1_HUMAN Reviewed; 278 AA. AC Q8WX77; DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 24-JAN-2024, entry version 157. DE RecName: Full=Insulin-like growth factor-binding protein-like 1; DE AltName: Full=IGFBP-related protein 10; DE AltName: Full=Insulin-like growth factor-binding-related protein 4; DE Short=IGFBP-rP4; DE Flags: Precursor; GN Name=IGFBPL1; Synonyms=IGFBPRP4; 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], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND RP FUNCTION. RC TISSUE=Testis; RX PubMed=15845387; DOI=10.1016/j.bbrc.2005.03.163; RA Cai Z., Chen H.T., Boyle B., Rupp F., Funk W.D., Dedera D.A.; RT "Identification of a novel insulin-like growth factor binding protein gene RT homologue with tumor suppressor like properties."; RL Biochem. Biophys. Res. Commun. 331:261-266(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [3] 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. CC -!- FUNCTION: IGF-binding proteins prolong the half-life of IGFs and have CC been shown to either inhibit or stimulate the growth promoting effects CC of the IGFs in cell culture. They alter the interaction of IGFs with CC their cell surface receptors (By similarity). May be a putative tumor CC suppressor protein. {ECO:0000250, ECO:0000269|PubMed:15845387}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15845387}. CC -!- TISSUE SPECIFICITY: Expressed at the highest level in both brain and CC testis, with lower levels in the prostate, bladder and lung. CC {ECO:0000269|PubMed:15845387}. CC -!- INDUCTION: Down-regulated in multiple tumors. 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; AL135785; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471071; EAW58251.1; -; Genomic_DNA. DR CCDS; CCDS35017.1; -. DR RefSeq; NP_001007564.1; NM_001007563.2. DR PDB; 7MJ6; X-ray; 1.95 A; C=14-22. DR PDB; 7MJ7; X-ray; 1.60 A; C=14-24. DR PDB; 7MJ8; X-ray; 1.79 A; C=14-25. DR PDB; 7MJ9; X-ray; 1.75 A; C=14-22. DR PDBsum; 7MJ6; -. DR PDBsum; 7MJ7; -. DR PDBsum; 7MJ8; -. DR PDBsum; 7MJ9; -. DR AlphaFoldDB; Q8WX77; -. DR SMR; Q8WX77; -. DR BioGRID; 131417; 26. DR STRING; 9606.ENSP00000366923; -. DR GlyCosmos; Q8WX77; 1 site, No reported glycans. DR GlyGen; Q8WX77; 3 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q8WX77; -. DR PhosphoSitePlus; Q8WX77; -. DR BioMuta; IGFBPL1; -. DR DMDM; 74751604; -. DR EPD; Q8WX77; -. DR MassIVE; Q8WX77; -. DR PaxDb; 9606-ENSP00000366923; -. DR PeptideAtlas; Q8WX77; -. DR ProteomicsDB; 74977; -. DR Antibodypedia; 62957; 74 antibodies from 16 providers. DR DNASU; 347252; -. DR Ensembl; ENST00000377694.2; ENSP00000366923.1; ENSG00000137142.5. DR GeneID; 347252; -. DR KEGG; hsa:347252; -. DR MANE-Select; ENST00000377694.2; ENSP00000366923.1; NM_001007563.3; NP_001007564.1. DR UCSC; uc004aaz.4; human. DR AGR; HGNC:20081; -. DR CTD; 347252; -. DR DisGeNET; 347252; -. DR GeneCards; IGFBPL1; -. DR HGNC; HGNC:20081; IGFBPL1. DR HPA; ENSG00000137142; Tissue enriched (thyroid). DR MIM; 610413; gene. DR neXtProt; NX_Q8WX77; -. DR OpenTargets; ENSG00000137142; -. DR PharmGKB; PA134937275; -. DR VEuPathDB; HostDB:ENSG00000137142; -. DR eggNOG; ENOG502QSKF; Eukaryota. DR GeneTree; ENSGT00530000063555; -. DR HOGENOM; CLU_075590_0_1_1; -. DR InParanoid; Q8WX77; -. DR OMA; WRKVTRS; -. DR OrthoDB; 3019991at2759; -. DR PhylomeDB; Q8WX77; -. DR TreeFam; TF331645; -. DR PathwayCommons; Q8WX77; -. DR SignaLink; Q8WX77; -. DR BioGRID-ORCS; 347252; 30 hits in 1138 CRISPR screens. DR ChiTaRS; IGFBPL1; human. DR GenomeRNAi; 347252; -. DR Pharos; Q8WX77; Tbio. DR PRO; PR:Q8WX77; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q8WX77; Protein. DR Bgee; ENSG00000137142; Expressed in ganglionic eminence and 100 other cell types or tissues. DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0005520; F:insulin-like growth factor binding; IEA:InterPro. DR GO; GO:0071228; P:cellular response to tumor cell; IEP:UniProtKB. DR GO; GO:0001558; P:regulation of cell growth; IEA:InterPro. DR GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central. DR CDD; cd00096; Ig; 1. 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:SF16; INSULIN-LIKE GROWTH FACTOR-BINDING PROTEIN-LIKE 1; 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 3D-structure; Disulfide bond; Glycoprotein; Immunoglobulin domain; KW Reference proteome; Secreted; Signal. FT SIGNAL 1..25 FT /evidence="ECO:0000255" FT CHAIN 26..278 FT /note="Insulin-like growth factor-binding protein-like 1" FT /id="PRO_0000297687" FT DOMAIN 34..109 FT /note="IGFBP N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DOMAIN 95..153 FT /note="Kazal-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798" FT DOMAIN 155..259 FT /note="Ig-like C2-type" FT CARBOHYD 166 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 38..63 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 41..65 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 46..66 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 52..69 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 77..91 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 85..106 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 115..151 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798" FT DISULFID 176..243 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" SQ SEQUENCE 278 AA; 29005 MW; C159031F05739B6F CRC64; MPRLSLLLPL LLLLLLPLLP PLSPSLGIRD VGGRRPKCGP CRPEGCPAPA PCPAPGISAL DECGCCARCL GAEGASCGGR AGGRCGPGLV CASQAAGAAP EGTGLCVCAQ RGTVCGSDGR SYPSVCALRL RARHTPRAHP GHLHKARDGP CEFAPVVVVP PRSVHNVTGA QVGLSCEVRA VPTPVITWRK VTKSPEGTQA LEELPGDHVN IAVQVRGGPS DHEATAWILI NPLRKEDEGV YQCHAANMVG EAESHSTVTV LDLSKYRSFH FPAPDDRM //