GREM1_HUMAN
ID GREM1_HUMAN Reviewed; 184 AA.
AC O60565; Q52LV3; Q8N914; Q8N936;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Gremlin-1;
DE AltName: Full=Cell proliferation-inducing gene 2 protein;
DE AltName: Full=Cysteine knot superfamily 1, BMP antagonist 1;
DE AltName: Full=DAN domain family member 2;
DE AltName: Full=Down-regulated in Mos-transformed cells protein;
DE AltName: Full=Increased in high glucose protein 2 {ECO:0000303|PubMed:10744662};
DE Short=IHG-2 {ECO:0000303|PubMed:10744662};
DE Flags: Precursor;
GN Name=GREM1; Synonyms=CKTSF1B1, DAND2, DRM; ORFNames=PIG2;
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).
RX PubMed=9660951; DOI=10.1016/s1097-2765(00)80067-2;
RA Hsu D.R., Economides A.N., Wang X., Eimon P.M., Harland R.M.;
RT "The Xenopus dorsalizing factor Gremlin identifies a novel family of
RT secreted proteins that antagonize BMP activities.";
RL Mol. Cell 1:673-683(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION.
RX PubMed=10744662; DOI=10.1074/jbc.275.14.9901;
RA McMahon R., Murphy M., Clarkson M., Taal M., Mackenzie H.S., Godson C.,
RA Martin F., Brady H.R.;
RT "IHG-2, a mesangial cell gene induced by high glucose, is human gremlin.
RT Regulation by extracellular glucose concentration, cyclic mechanical
RT strain, and transforming growth factor-beta1.";
RL J. Biol. Chem. 275:9901-9904(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Small intestine;
RX PubMed=10894942; DOI=10.1159/000015568;
RA Topol L.Z., Modi W.S., Koochekpour S., Blair D.G.;
RT "DRM/GREMLIN (CKTSF1B1) maps to human chromosome 15 and is highly expressed
RT in adult and fetal brain.";
RL Cytogenet. Cell Genet. 89:79-84(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Tate G., Mitsuya T.;
RT "Human Gremlin homologue.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kim J.W.;
RT "Identification of a human cell proliferation gene.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Chondrocyte;
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).
RC TISSUE=Liver;
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 [8]
RP PROTEIN SEQUENCE OF 25-39.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [9]
RP TISSUE SPECIFICITY, AND INVOLVEMENT IN HMPS1.
RX PubMed=22561515; DOI=10.1038/ng.2263;
RA Jaeger E., Leedham S., Lewis A., Segditsas S., Becker M., Cuadrado P.R.,
RA Davis H., Kaur K., Heinimann K., Howarth K., East J., Taylor J., Thomas H.,
RA Tomlinson I.;
RT "Hereditary mixed polyposis syndrome is caused by a 40-kb upstream
RT duplication that leads to increased and ectopic expression of the BMP
RT antagonist GREM1.";
RL Nat. Genet. 44:699-703(2012).
RN [10] {ECO:0007744|PDB:5AEJ}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 72-184, FUNCTION, SUBUNIT,
RP INTERACTION WITH BMP2, AND DISULFIDE BONDS.
RX PubMed=27036124; DOI=10.1042/bcj20160254;
RA Kisonaite M., Wang X., Hyvonen M.;
RT "Structure of Gremlin-1 and analysis of its interaction with BMP-2.";
RL Biochem. J. 473:1593-1604(2016).
CC -!- FUNCTION: Cytokine that may play an important role during
CC carcinogenesis and metanephric kidney organogenesis, as a BMP
CC antagonist required for early limb outgrowth and patterning in
CC maintaining the FGF4-SHH feedback loop. Down-regulates the BMP4
CC signaling in a dose-dependent manner (By similarity). Antagonist of
CC BMP2; inhibits BMP2-mediated differentiation of osteoblasts (in vitro)
CC (PubMed:27036124). Acts as inhibitor of monocyte chemotaxis. Can
CC inhibit the growth or viability of normal cells but not transformed
CC cells when is overexpressed (By similarity).
CC {ECO:0000250|UniProtKB:O35793, ECO:0000250|UniProtKB:O70326,
CC ECO:0000269|PubMed:27036124}.
CC -!- SUBUNIT: Homodimer; can also form homooligomers (PubMed:27036124).
CC Interacts with BMP2; can form higher oligomers with BMP2
CC (PubMed:27036124). Interacts with SLIT1 and SLIT2 in a glycosylation-
CC dependent manner (By similarity). {ECO:0000250|UniProtKB:O35793,
CC ECO:0000269|PubMed:27036124}.
CC -!- INTERACTION:
CC O60565; P35968: KDR; NbExp=4; IntAct=EBI-944395, EBI-1005487;
CC O60565; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-944395, EBI-10176379;
CC O60565; Q99750: MDFI; NbExp=3; IntAct=EBI-944395, EBI-724076;
CC O60565; Q04917: YWHAH; NbExp=5; IntAct=EBI-944395, EBI-306940;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O60565-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60565-2; Sequence=VSP_013321;
CC -!- TISSUE SPECIFICITY: Highly expressed in small intestine, fetal brain
CC and colon. Expression is restricted to intestinal subepithelial
CC myofibroblasts (ISEMFs) at the crypt base. In subjects with HMPS1, by
CC contrast, GREM1 is expressed, not only in basal ISEMFs, but also at
CC very high levels in epithelial cells (predominantly colonocytes), with
CC expression extending most of the way up the sides of the crypt. Weakly
CC expressed in brain, ovary, prostate, pancreas and skeletal muscle. In
CC brain found in the region localized around the internal capsule in the
CC large subcortical nuclei, including caudate, putamen, substantia nigra,
CC thalamus and subthalamus. Predominantly expressed in normal cells
CC including neurons, astrocytes and fibroblasts.
CC {ECO:0000269|PubMed:10894942, ECO:0000269|PubMed:22561515}.
CC -!- INDUCTION: By high glucose through TGFB1-mediated pathways in mesangial
CC cell. Down-regulated in tumor cell lines. {ECO:0000269|PubMed:10744662,
CC ECO:0000269|PubMed:10894942}.
CC -!- DISEASE: Polyposis syndrome, mixed hereditary 1 (HMPS1) [MIM:601228]: A
CC disease characterized by apparent autosomal dominant inheritance of
CC multiple types of colorectal polyp, with colorectal carcinoma occurring
CC in a high proportion of affected individuals. Patients can develop
CC polyps of multiple and mixed morphologies, including serrated lesions,
CC Peutz-Jeghers polyps, juvenile polyps, conventional adenomas and
CC colorectal carcinoma in the absence of any identifiable extra-colonic
CC features. {ECO:0000269|PubMed:22561515}. Note=The disease is caused by
CC variants affecting the gene represented in this entry. HMPS1 is caused
CC by a duplication spanning the 3' end of the SCG5 gene and a region
CC upstream of the GREM1 locus. This duplication is associated with
CC increased allele-specific GREM1 expression that may cause reduced bone
CC morphogenetic protein (BMP) pathway activity. This mechanism also
CC underlies tumorigenesis in juvenile polyposis of the large bowel
CC (PubMed:22561515). {ECO:0000269|PubMed:22561515}.
CC -!- SIMILARITY: Belongs to the DAN family. {ECO:0000305}.
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DR EMBL; AF045800; AAC39725.1; -; mRNA.
DR EMBL; AF110137; AAF06677.1; -; mRNA.
DR EMBL; AF154054; AAG23891.1; -; mRNA.
DR EMBL; AB032372; BAA84462.1; -; Genomic_DNA.
DR EMBL; AY232290; AAP69985.1; -; mRNA.
DR EMBL; AK095890; BAC04643.1; -; mRNA.
DR EMBL; BC069525; AAH69525.1; -; mRNA.
DR EMBL; BC093778; AAH93778.1; -; mRNA.
DR EMBL; BC101611; AAI01612.1; -; mRNA.
DR CCDS; CCDS10029.1; -. [O60565-1]
DR CCDS; CCDS53927.1; -. [O60565-2]
DR RefSeq; NP_001178252.1; NM_001191323.1. [O60565-2]
DR RefSeq; NP_037504.1; NM_013372.6. [O60565-1]
DR PDB; 5AEJ; X-ray; 1.90 A; A/B/C/D=72-184.
DR PDBsum; 5AEJ; -.
DR AlphaFoldDB; O60565; -.
DR SMR; O60565; -.
DR BioGRID; 117754; 4.
DR IntAct; O60565; 8.
DR MINT; O60565; -.
DR STRING; 9606.ENSP00000478319; -.
DR GlyGen; O60565; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; O60565; -.
DR PhosphoSitePlus; O60565; -.
DR BioMuta; GREM1; -.
DR jPOST; O60565; -.
DR MassIVE; O60565; -.
DR MaxQB; O60565; -.
DR PaxDb; O60565; -.
DR PeptideAtlas; O60565; -.
DR PRIDE; O60565; -.
DR ProteomicsDB; 49469; -. [O60565-1]
DR ProteomicsDB; 49470; -. [O60565-2]
DR Antibodypedia; 2030; 561 antibodies from 34 providers.
DR DNASU; 26585; -.
DR Ensembl; ENST00000300177.8; ENSP00000300177.4; ENSG00000276886.4. [O60565-1]
DR Ensembl; ENST00000322805.5; ENSP00000323101.4; ENSG00000276886.4. [O60565-2]
DR Ensembl; ENST00000560830.1; ENSP00000453141.1; ENSG00000166923.12. [O60565-2]
DR Ensembl; ENST00000632478.1; ENSP00000488158.1; ENSG00000282046.3. [O60565-2]
DR Ensembl; ENST00000651081.1; ENSP00000498897.1; ENSG00000282046.3. [O60565-1]
DR Ensembl; ENST00000651154.1; ENSP00000498748.1; ENSG00000166923.12. [O60565-1]
DR Ensembl; ENST00000651986.1; ENSP00000498605.1; ENSG00000282046.3. [O60565-1]
DR Ensembl; ENST00000652365.1; ENSP00000498763.1; ENSG00000166923.12. [O60565-1]
DR GeneID; 26585; -.
DR KEGG; hsa:26585; -.
DR MANE-Select; ENST00000651154.1; ENSP00000498748.1; NM_013372.7; NP_037504.1.
DR UCSC; uc001zhe.3; human. [O60565-1]
DR CTD; 26585; -.
DR DisGeNET; 26585; -.
DR GeneCards; GREM1; -.
DR HGNC; HGNC:2001; GREM1.
DR HPA; ENSG00000166923; Tissue enhanced (gallbladder, smooth muscle).
DR MalaCards; GREM1; -.
DR MIM; 601228; phenotype.
DR MIM; 603054; gene.
DR neXtProt; NX_O60565; -.
DR OpenTargets; ENSG00000166923; -.
DR Orphanet; 157794; Hereditary mixed polyposis syndrome.
DR PharmGKB; PA26537; -.
DR VEuPathDB; HostDB:ENSG00000166923; -.
DR eggNOG; ENOG502QQ5X; Eukaryota.
DR GeneTree; ENSGT00940000154209; -.
DR HOGENOM; CLU_101024_0_0_1; -.
DR InParanoid; O60565; -.
DR OMA; MPRTRCA; -.
DR PhylomeDB; O60565; -.
DR TreeFam; TF106445; -.
DR PathwayCommons; O60565; -.
DR SignaLink; O60565; -.
DR BioGRID-ORCS; 26585; 10 hits in 1063 CRISPR screens.
DR ChiTaRS; GREM1; human.
DR GenomeRNAi; 26585; -.
DR Pharos; O60565; Tbio.
DR PRO; PR:O60565; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O60565; protein.
DR Bgee; ENSG00000166923; Expressed in stromal cell of endometrium and 95 other tissues.
DR ExpressionAtlas; O60565; baseline and differential.
DR Genevisible; O60565; HS.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0036122; F:BMP binding; IDA:UniProtKB.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0016015; F:morphogen activity; ISS:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0048018; F:receptor ligand activity; ISS:BHF-UCL.
DR GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; ISS:BHF-UCL.
DR GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; ISS:BHF-UCL.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; ISS:BHF-UCL.
DR GO; GO:0060379; P:cardiac muscle cell myoblast differentiation; IEA:Ensembl.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISS:BHF-UCL.
DR GO; GO:0000902; P:cell morphogenesis; IDA:BHF-UCL.
DR GO; GO:0007267; P:cell-cell signaling; IEA:Ensembl.
DR GO; GO:0030199; P:collagen fibril organization; IMP:BHF-UCL.
DR GO; GO:0048263; P:determination of dorsal identity; IMP:BHF-UCL.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IEA:Ensembl.
DR GO; GO:0060173; P:limb development; IMP:AgBase.
DR GO; GO:0003337; P:mesenchymal to epithelial transition involved in metanephros morphogenesis; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:AgBase.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:BHF-UCL.
DR GO; GO:0030502; P:negative regulation of bone mineralization; IMP:BHF-UCL.
DR GO; GO:1900158; P:negative regulation of bone mineralization involved in bone maturation; IMP:BHF-UCL.
DR GO; GO:0046851; P:negative regulation of bone remodeling; IMP:BHF-UCL.
DR GO; GO:1900155; P:negative regulation of bone trabecula formation; IMP:BHF-UCL.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:BHF-UCL.
DR GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IMP:AgBase.
DR GO; GO:0090027; P:negative regulation of monocyte chemotaxis; ISS:BHF-UCL.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:UniProtKB.
DR GO; GO:0033689; P:negative regulation of osteoblast proliferation; IMP:BHF-UCL.
DR GO; GO:0090291; P:negative regulation of osteoclast proliferation; IMP:BHF-UCL.
DR GO; GO:0060394; P:negative regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:1900086; P:positive regulation of peptidyl-tyrosine autophosphorylation; ISS:BHF-UCL.
DR GO; GO:0002092; P:positive regulation of receptor internalization; ISS:BHF-UCL.
DR GO; GO:2000273; P:positive regulation of signaling receptor activity; ISS:BHF-UCL.
DR GO; GO:0051973; P:positive regulation of telomerase activity; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0009954; P:proximal/distal pattern formation; IEA:Ensembl.
DR GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; IEA:Ensembl.
DR GO; GO:0038098; P:sequestering of BMP from receptor via BMP binding; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; ISS:BHF-UCL.
DR GO; GO:0060676; P:ureteric bud formation; IEA:Ensembl.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR006207; Cys_knot_C.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR004133; DAN.
DR InterPro; IPR017159; Gremlin-1/2.
DR Pfam; PF03045; DAN; 1.
DR PIRSF; PIRSF037254; Gremlin_precursor; 1.
DR SMART; SM00041; CT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytokine; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 25..184
FT /note="Gremlin-1"
FT /id="PRO_0000006714"
FT DOMAIN 94..184
FT /note="CTCK"
FT REGION 24..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..144
FT /evidence="ECO:0000269|PubMed:27036124,
FT ECO:0007744|PDB:5AEJ"
FT DISULFID 108..158
FT /evidence="ECO:0000269|PubMed:27036124,
FT ECO:0007744|PDB:5AEJ"
FT DISULFID 118..176
FT /evidence="ECO:0000269|PubMed:27036124,
FT ECO:0007744|PDB:5AEJ"
FT DISULFID 122..178
FT /evidence="ECO:0000269|PubMed:27036124,
FT ECO:0007744|PDB:5AEJ"
FT VAR_SEQ 39..79
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_013321"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:5AEJ"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:5AEJ"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:5AEJ"
FT STRAND 93..103
FT /evidence="ECO:0007829|PDB:5AEJ"
FT STRAND 111..131
FT /evidence="ECO:0007829|PDB:5AEJ"
FT STRAND 134..157
FT /evidence="ECO:0007829|PDB:5AEJ"
FT STRAND 161..180
FT /evidence="ECO:0007829|PDB:5AEJ"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:5AEJ"
SQ SEQUENCE 184 AA; 20697 MW; 4B588598DE12C47E CRC64;
MSRTAYTVGA LLLLLGTLLP AAEGKKKGSQ GAIPPPDKAQ HNDSEQTQSP QQPGSRNRGR
GQGRGTAMPG EEVLESSQEA LHVTERKYLK RDWCKTQPLK QTIHEEGCNS RTIINRFCYG
QCNSFYIPRH IRKEEGSFQS CSFCKPKKFT TMMVTLNCPE LQPPTKKKRV TRVKQCRCIS
IDLD
