IBPL1_HUMAN
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 03-AUG-2022, entry version 149.
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.
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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; 25.
DR STRING; 9606.ENSP00000366923; -.
DR GlyGen; Q8WX77; 1 site.
DR iPTMnet; Q8WX77; -.
DR PhosphoSitePlus; Q8WX77; -.
DR BioMuta; IGFBPL1; -.
DR DMDM; 74751604; -.
DR EPD; Q8WX77; -.
DR MassIVE; Q8WX77; -.
DR PaxDb; Q8WX77; -.
DR PeptideAtlas; Q8WX77; -.
DR PRIDE; Q8WX77; -.
DR ProteomicsDB; 74977; -.
DR Antibodypedia; 62957; 57 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 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; IAARDEC; -.
DR OrthoDB; 994901at2759; -.
DR PhylomeDB; Q8WX77; -.
DR TreeFam; TF331645; -.
DR PathwayCommons; Q8WX77; -.
DR SignaLink; Q8WX77; -.
DR BioGRID-ORCS; 347252; 30 hits in 1060 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 99 other tissues.
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 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; 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; 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 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 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
