IBP4_HUMAN
ID IBP4_HUMAN Reviewed; 258 AA.
AC P22692; A0N9W2; B4E351; Q5U012; Q9UCL6;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Insulin-like growth factor-binding protein 4;
DE Short=IBP-4;
DE Short=IGF-binding protein 4;
DE Short=IGFBP-4;
DE Flags: Precursor;
GN Name=IGFBP4; Synonyms=IBP4;
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] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=1704481; DOI=10.1210/mend-4-10-1451;
RA Shimasaki S., Uchiyama F., Shimonaka M., Ling N.;
RT "Molecular cloning of the cDNAs encoding a novel insulin-like growth
RT factor-binding protein from rat and human.";
RL Mol. Endocrinol. 4:1451-1458(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1707125; DOI=10.1210/mend-4-12-1806;
RA Latour D., Mohan S., Linkhart T.A., Baylink D.J., Strong D.D.;
RT "Inhibitory insulin-like growth factor-binding protein: cloning, complete
RT sequence, and physiological regulation.";
RL Mol. Endocrinol. 4:1806-1814(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 22-41.
RC TISSUE=Osteosarcoma;
RX PubMed=1709161; DOI=10.1016/s0021-9258(18)31549-7;
RA Kiefer M.C., Masiarz F.R., Bauer D.M., Zapf J.;
RT "Identification and molecular cloning of two new 30-kDa insulin-like growth
RT factor binding proteins isolated from adult human serum.";
RL J. Biol. Chem. 266:9043-9049(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=9048882; DOI=10.1016/s0167-4781(96)00220-5;
RA Qin X., Morales S., Lee K.-W., Boonyaratanakornkit V., Baylink D.J.,
RA Mohan S., Strong D.D.;
RT "Structural and functional analysis of the 5'-flanking region of the human
RT insulin-like growth factor binding protein (IGFBP)-4 gene.";
RL Biochim. Biophys. Acta 1350:136-140(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9615225; DOI=10.1006/geno.1998.5283;
RA Zazzi H., Nikoshkov A., Hall K., Luthman H.;
RT "Structure and transcription regulation of the human insulin-like growth
RT factor binding protein 4 gene (IGFBP4).";
RL Genomics 49:401-410(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [10]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [12]
RP PROTEIN SEQUENCE OF 22-53.
RC TISSUE=Colon;
RX PubMed=1709585;
RA Culouscou J.-M., Shoyab M.;
RT "Purification of a colon cancer cell growth inhibitor and its
RT identification as an insulin-like growth factor binding protein.";
RL Cancer Res. 51:2813-2819(1991).
RN [13]
RP PROTEIN SEQUENCE OF 22-42, AND INDUCTION.
RC TISSUE=Osteosarcoma;
RX PubMed=1726835;
RA Mohan S., Baylink D.J.;
RT "Evidence that the inhibition of TE85 human bone cell proliferation by
RT agents which stimulate cAMP production may in part be mediated by changes
RT in the IGF-II regulatory system.";
RL Growth Regul. 1:110-118(1991).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP PHOSPHORYLATION AT SER-255.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 24-103 IN COMPLEX WITH IGF1, AND
RP DISULFIDE BONDS.
RX PubMed=15642270; DOI=10.1016/j.str.2004.11.009;
RA Siwanowicz I., Popowicz G.M., Wisniewska M., Huber R., Kuenkele K.-P.,
RA Lang K., Engh R.A., Holak T.A.;
RT "Structural basis for the regulation of insulin-like growth factors by IGF
RT binding proteins.";
RL Structure 13:155-167(2005).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 22-253 IN COMPLEX WITH IGF1, AND
RP DISULFIDE BONDS.
RX PubMed=16924115; DOI=10.1073/pnas.0605652103;
RA Sitar T., Popowicz G.M., Siwanowicz I., Huber R., Holak T.A.;
RT "Structural basis for the inhibition of insulin-like growth factors by
RT insulin-like growth factor-binding proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13028-13033(2006).
CC -!- FUNCTION: IGF-binding proteins prolong the half-life of the IGFs and
CC have been shown to either inhibit or stimulate the growth promoting
CC effects of the IGFs on cell culture. They alter the interaction of IGFs
CC with their cell surface receptors.
CC -!- SUBUNIT: Binds IGF2 more than IGF1. {ECO:0000269|PubMed:15642270,
CC ECO:0000269|PubMed:16924115}.
CC -!- INTERACTION:
CC P22692; P54252: ATXN3; NbExp=3; IntAct=EBI-2831948, EBI-946046;
CC P22692; P46379-2: BAG6; NbExp=3; IntAct=EBI-2831948, EBI-10988864;
CC P22692; G5E9A7: DMWD; NbExp=3; IntAct=EBI-2831948, EBI-10976677;
CC P22692; P22607: FGFR3; NbExp=3; IntAct=EBI-2831948, EBI-348399;
CC P22692; P28799: GRN; NbExp=3; IntAct=EBI-2831948, EBI-747754;
CC P22692; P06396: GSN; NbExp=3; IntAct=EBI-2831948, EBI-351506;
CC P22692; P42858: HTT; NbExp=6; IntAct=EBI-2831948, EBI-466029;
CC P22692; P05019: IGF1; NbExp=7; IntAct=EBI-2831948, EBI-7902275;
CC P22692; P01344-3: IGF2; NbExp=4; IntAct=EBI-2831948, EBI-13334485;
CC P22692; O60333-2: KIF1B; NbExp=3; IntAct=EBI-2831948, EBI-10975473;
CC P22692; O14901: KLF11; NbExp=3; IntAct=EBI-2831948, EBI-948266;
CC P22692; D3DTS7: PMP22; NbExp=3; IntAct=EBI-2831948, EBI-25882629;
CC P22692; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2831948, EBI-5235340;
CC P22692; O14656: TOR1A; NbExp=3; IntAct=EBI-2831948, EBI-524257;
CC P22692; O76024: WFS1; NbExp=3; IntAct=EBI-2831948, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P22692-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P22692-2; Sequence=VSP_057034;
CC -!- INDUCTION: By forskolin and N6,O2'dibutyryl adenosine 3',5'-cyclic
CC monophosphate, but not by 1,9 dideoxyforskolin.
CC {ECO:0000269|PubMed:1726835}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/igfbp4/";
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DR EMBL; M38177; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M62403; AAB06189.1; -; mRNA.
DR EMBL; U20982; AAA62670.1; -; Genomic_DNA.
DR EMBL; Y12508; CAA73110.1; -; Genomic_DNA.
DR EMBL; AK304572; BAG65363.1; -; mRNA.
DR EMBL; BT019891; AAV38694.1; -; mRNA.
DR EMBL; BT019892; AAV38695.1; -; mRNA.
DR EMBL; AY442346; AAR05443.1; -; Genomic_DNA.
DR EMBL; AC018629; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471152; EAW60664.1; -; Genomic_DNA.
DR EMBL; BC016041; AAH16041.1; -; mRNA.
DR CCDS; CCDS11367.1; -. [P22692-1]
DR PIR; G01662; B37252.
DR RefSeq; NP_001543.2; NM_001552.2. [P22692-1]
DR PDB; 1WQJ; X-ray; 1.60 A; B=24-103.
DR PDB; 2DSP; X-ray; 2.50 A; B=22-113.
DR PDB; 2DSQ; X-ray; 2.80 A; A/B=22-113.
DR PDB; 2DSR; X-ray; 2.10 A; B=24-103, G=172-253.
DR PDBsum; 1WQJ; -.
DR PDBsum; 2DSP; -.
DR PDBsum; 2DSQ; -.
DR PDBsum; 2DSR; -.
DR AlphaFoldDB; P22692; -.
DR SMR; P22692; -.
DR BioGRID; 109708; 34.
DR DIP; DIP-48432N; -.
DR IntAct; P22692; 23.
DR MINT; P22692; -.
DR STRING; 9606.ENSP00000269593; -.
DR BindingDB; P22692; -.
DR ChEMBL; CHEMBL2310; -.
DR DrugBank; DB01277; Mecasermin.
DR MEROPS; I31.952; -.
DR GlyGen; P22692; 1 site.
DR iPTMnet; P22692; -.
DR PhosphoSitePlus; P22692; -.
DR BioMuta; IGFBP4; -.
DR DMDM; 124065; -.
DR EPD; P22692; -.
DR jPOST; P22692; -.
DR MassIVE; P22692; -.
DR MaxQB; P22692; -.
DR PaxDb; P22692; -.
DR PeptideAtlas; P22692; -.
DR PRIDE; P22692; -.
DR ProteomicsDB; 54018; -. [P22692-1]
DR ProteomicsDB; 5879; -.
DR Antibodypedia; 16491; 655 antibodies from 39 providers.
DR DNASU; 3487; -.
DR Ensembl; ENST00000269593.5; ENSP00000269593.4; ENSG00000141753.7. [P22692-1]
DR GeneID; 3487; -.
DR KEGG; hsa:3487; -.
DR MANE-Select; ENST00000269593.5; ENSP00000269593.4; NM_001552.3; NP_001543.2.
DR UCSC; uc002hus.4; human. [P22692-1]
DR CTD; 3487; -.
DR DisGeNET; 3487; -.
DR GeneCards; IGFBP4; -.
DR HGNC; HGNC:5473; IGFBP4.
DR HPA; ENSG00000141753; Low tissue specificity.
DR MIM; 146733; gene.
DR neXtProt; NX_P22692; -.
DR OpenTargets; ENSG00000141753; -.
DR PharmGKB; PA29706; -.
DR VEuPathDB; HostDB:ENSG00000141753; -.
DR eggNOG; ENOG502QTC8; Eukaryota.
DR GeneTree; ENSGT00940000159647; -.
DR HOGENOM; CLU_070833_3_0_1; -.
DR InParanoid; P22692; -.
DR OMA; KAPQGCA; -.
DR PhylomeDB; P22692; -.
DR TreeFam; TF331211; -.
DR BioCyc; MetaCyc:ENSG00000141753-MON; -.
DR PathwayCommons; P22692; -.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; P22692; -.
DR BioGRID-ORCS; 3487; 7 hits in 1074 CRISPR screens.
DR ChiTaRS; IGFBP4; human.
DR EvolutionaryTrace; P22692; -.
DR GeneWiki; IGFBP4; -.
DR GenomeRNAi; 3487; -.
DR Pharos; P22692; Tchem.
DR PRO; PR:P22692; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P22692; protein.
DR Bgee; ENSG00000141753; Expressed in stromal cell of endometrium and 186 other tissues.
DR ExpressionAtlas; P22692; baseline and differential.
DR Genevisible; P22692; HS.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0031994; F:insulin-like growth factor I binding; IBA:GO_Central.
DR GO; GO:0031995; F:insulin-like growth factor II binding; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; TAS:ParkinsonsUK-UCL.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:ParkinsonsUK-UCL.
DR GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
DR GO; GO:0010906; P:regulation of glucose metabolic process; IEA:Ensembl.
DR GO; GO:0043567; P:regulation of insulin-like growth factor receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0044342; P:type B pancreatic cell proliferation; IEA:Ensembl.
DR CDD; cd00191; TY; 1.
DR Gene3D; 4.10.800.10; -; 1.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR022327; IGFBP-4.
DR InterPro; IPR000867; IGFBP-like.
DR InterPro; IPR022321; IGFBP_1-6_chordata.
DR InterPro; IPR017891; Insulin_GF-bd_Cys-rich_CS.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR PANTHER; PTHR11551:SF7; PTHR11551:SF7; 1.
DR Pfam; PF00219; IGFBP; 1.
DR Pfam; PF00086; Thyroglobulin_1; 1.
DR PRINTS; PR01976; IGFBPFAMILY.
DR PRINTS; PR01980; IGFBPFAMILY4.
DR SMART; SM00121; IB; 1.
DR SMART; SM00211; TY; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR SUPFAM; SSF57610; SSF57610; 1.
DR PROSITE; PS00222; IGFBP_N_1; 1.
DR PROSITE; PS51323; IGFBP_N_2; 1.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Growth factor binding; Phosphoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:1709161,
FT ECO:0000269|PubMed:1709585, ECO:0000269|PubMed:1726835"
FT CHAIN 22..258
FT /note="Insulin-like growth factor-binding protein 4"
FT /id="PRO_0000014382"
FT DOMAIN 23..103
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 171..249
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REGION 149..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 255
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:1709161"
FT DISULFID 27..53
FT /evidence="ECO:0000269|PubMed:15642270,
FT ECO:0000269|PubMed:16924115"
FT DISULFID 30..55
FT /evidence="ECO:0000269|PubMed:15642270,
FT ECO:0000269|PubMed:16924115"
FT DISULFID 38..59
FT /evidence="ECO:0000269|PubMed:15642270,
FT ECO:0000269|PubMed:16924115"
FT DISULFID 44..56
FT /evidence="ECO:0000269|PubMed:15642270,
FT ECO:0000269|PubMed:16924115"
FT DISULFID 67..80
FT /evidence="ECO:0000269|PubMed:15642270,
FT ECO:0000269|PubMed:16924115"
FT DISULFID 74..100
FT /evidence="ECO:0000269|PubMed:15642270,
FT ECO:0000269|PubMed:16924115"
FT DISULFID 131..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:15642270, ECO:0000269|PubMed:16924115"
FT DISULFID 174..204
FT /evidence="ECO:0000269|PubMed:15642270,
FT ECO:0000269|PubMed:16924115"
FT DISULFID 215..226
FT /evidence="ECO:0000269|PubMed:15642270,
FT ECO:0000269|PubMed:16924115"
FT DISULFID 228..249
FT /evidence="ECO:0000269|PubMed:15642270,
FT ECO:0000269|PubMed:16924115"
FT VAR_SEQ 1..100
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057034"
FT VARIANT 42
FT /note="V -> G (in dbSNP:rs599199)"
FT /id="VAR_011906"
FT CONFLICT 51
FT /note="P -> A (in Ref. 2; M38177, 4; AAA62670 and 12; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="G -> E (in Ref. 7; AAV38694)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="I -> F (in Ref. 2; M38177 and 4; AAA62670)"
FT /evidence="ECO:0000305"
FT HELIX 32..36
FT /evidence="ECO:0007829|PDB:1WQJ"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:1WQJ"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:1WQJ"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:2DSQ"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1WQJ"
FT HELIX 89..94
FT /evidence="ECO:0007829|PDB:1WQJ"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:1WQJ"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:2DSP"
FT HELIX 173..186
FT /evidence="ECO:0007829|PDB:2DSR"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:2DSR"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:2DSR"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:2DSR"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:2DSR"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:2DSR"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:2DSR"
SQ SEQUENCE 258 AA; 27934 MW; 5E8F4638D99F0A94 CRC64;
MLPLCLVAAL LLAAGPGPSL GDEAIHCPPC SEEKLARCRP PVGCEELVRE PGCGCCATCA
LGLGMPCGVY TPRCGSGLRC YPPRGVEKPL HTLMHGQGVC MELAEIEAIQ ESLQPSDKDE
GDHPNNSFSP CSAHDRRCLQ KHFAKIRDRS TSGGKMKVNG APREDARPVP QGSCQSELHR
ALERLAASQS RTHEDLYIIP IPNCDRNGNF HPKQCHPALD GQRGKCWCVD RKTGVKLPGG
LEPKGELDCH QLADSFRE
