IBPL1_BOVIN
ID IBPL1_BOVIN Reviewed; 274 AA.
AC A5PKD8;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Insulin-like growth factor-binding protein-like 1;
DE Flags: Precursor;
GN Name=IGFBPL1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) 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). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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DR EMBL; BC142451; AAI42452.1; -; mRNA.
DR RefSeq; NP_001092631.1; NM_001099161.2.
DR AlphaFoldDB; A5PKD8; -.
DR SMR; A5PKD8; -.
DR STRING; 9913.ENSBTAP00000018719; -.
DR PaxDb; A5PKD8; -.
DR Ensembl; ENSBTAT00000018719; ENSBTAP00000018719; ENSBTAG00000014078.
DR GeneID; 616886; -.
DR KEGG; bta:616886; -.
DR CTD; 347252; -.
DR VEuPathDB; HostDB:ENSBTAG00000014078; -.
DR VGNC; VGNC:30090; IGFBPL1.
DR eggNOG; ENOG502QSKF; Eukaryota.
DR GeneTree; ENSGT00530000063555; -.
DR HOGENOM; CLU_075590_0_1_1; -.
DR InParanoid; A5PKD8; -.
DR OMA; IAARDEC; -.
DR OrthoDB; 994901at2759; -.
DR TreeFam; TF331645; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000014078; Expressed in Ammon's horn and 33 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005520; F:insulin-like growth factor binding; IEA:InterPro.
DR GO; GO:0071228; P:cellular response to tumor cell; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..274
FT /note="Insulin-like growth factor-binding protein-like 1"
FT /id="PRO_0000297686"
FT DOMAIN 30..105
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 91..149
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 151..255
FT /note="Ig-like C2-type"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 111..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 172..239
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 274 AA; 28673 MW; B7046C22C270F397 CRC64;
MPRSPGLFLL LLVLQPLPAL GLGLRSAGGR NPECGPCRPE RCPEPVRCPV PGIVARDECG
CCALCLGAEG ASCGGRAGAR CGPGLVCASR AAGAAPEGTG LCVCAQRGSV CGSDGRSYPS
VCALRLRARQ APRALPGHLH KARDGPCEFA PVVITPPQSV HNVTGAQVYL SCEVRAVPTP
VVTWRKVTRS PEGTQVMEEL PGDHTNIAVQ VQGGPSDHEA TAWVLINPLR KEDEGVYQCH
SANAVGEAQS HGTVTVVDRS QYRAPRFPAP DDRL