IBP7_HUMAN
ID IBP7_HUMAN Reviewed; 282 AA.
AC Q16270; B4E1N2; B7Z9W7; Q07822; Q53YE6; Q9UCA8;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Insulin-like growth factor-binding protein 7;
DE Short=IBP-7;
DE Short=IGF-binding protein 7;
DE Short=IGFBP-7;
DE AltName: Full=IGFBP-rP1;
DE AltName: Full=MAC25 protein;
DE AltName: Full=PGI2-stimulating factor;
DE AltName: Full=Prostacyclin-stimulating factor;
DE AltName: Full=Tumor-derived adhesion factor;
DE Short=TAF;
DE Flags: Precursor;
GN Name=IGFBP7; Synonyms=MAC25, PSF;
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), VARIANT PHE-11, AND RNA EDITING OF
RP POSITION 95.
RC TISSUE=Leptomeninges;
RX PubMed=7694637;
RA Murphy M., Pykett M.J., Harnish P., Zang K.D., George D.L.;
RT "Identification and characterization of genes differentially expressed in
RT meningiomas.";
RL Cell Growth Differ. 4:715-722(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7980422; DOI=10.1042/bj3030591;
RA Yamauchi T., Umeda F., Masakado M., Isaji M., Mizushima S., Nawata H.;
RT "Purification and molecular cloning of prostacyclin-stimulating factor from
RT serum-free conditioned medium of human diploid fibroblast cells.";
RL Biochem. J. 303:591-598(1994).
RN [3]
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-11.
RG NIEHS SNPs program;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thalamus, and Trachea;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis, and Uterus;
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 27-46, AND FUNCTION.
RC TISSUE=Urinary bladder carcinoma;
RX PubMed=8117260; DOI=10.1006/bbrc.1994.1149;
RA Akaogi K., Okabe Y., Funahashi K., Yoshitake Y., Nishikawa K.,
RA Yasumitsu H., Umeda M., Miyazaki K.;
RT "Cell adhesion activity of a 30-kDa major secreted protein from human
RT bladder carcinoma cells.";
RL Biochem. Biophys. Res. Commun. 198:1046-1053(1994).
RN [9]
RP PROTEIN SEQUENCE OF 27-41.
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 [10]
RP PROTEIN SEQUENCE OF 27-36, FUNCTION, AND GLYCOSYLATION.
RX PubMed=8939990; DOI=10.1074/jbc.271.48.30322;
RA Oh Y., Nagalla S.R., Yamanaka Y., Kim H.-S., Wilson E., Rosenfeld R.G.;
RT "Synthesis and characterization of insulin-like growth factor-binding
RT protein (IGFBP)-7. Recombinant human mac25 protein specifically binds IGF-I
RT and -II.";
RL J. Biol. Chem. 271:30322-30325(1996).
RN [11]
RP POSSIBLE INTERACTION WITH CHMP3.
RX PubMed=11549700; DOI=10.1210/jcem.86.9.7845;
RA Wilson E.M., Oh Y., Hwa V., Rosenfeld R.G.;
RT "Interaction of IGF-binding protein-related protein 1 with a novel protein,
RT neuroendocrine differentiation factor, results in neuroendocrine
RT differentiation of prostate cancer cells.";
RL J. Clin. Endocrinol. Metab. 86:4504-4511(2001).
RN [12]
RP RNA EDITING OF POSITIONS 78 AND 95.
RX PubMed=18772245; DOI=10.1261/rna.816908;
RA Gommans W.M., Tatalias N.E., Sie C.P., Dupuis D., Vendetti N., Smith L.,
RA Kaushal R., Maas S.;
RT "Screening of human SNP database identifies recoding sites of A-to-I RNA
RT editing.";
RL RNA 14:2074-2085(2008).
RN [13]
RP INVOLVEMENT IN RAMSVPS.
RX PubMed=21835307; DOI=10.1016/j.ajhg.2011.07.010;
RA Abu-Safieh L., Abboud E.B., Alkuraya H., Shamseldin H., Al-Enzi S.,
RA Al-Abdi L., Hashem M., Colak D., Jarallah A., Ahmad H., Bobis S., Nemer G.,
RA Bitar F., Alkuraya F.S.;
RT "Mutation of IGFBP7 causes upregulation of BRAF/MEK/ERK pathway and
RT familial retinal arterial macroaneurysms.";
RL Am. J. Hum. Genet. 89:313-319(2011).
RN [14]
RP PHOSPHORYLATION AT SER-239.
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).
CC -!- FUNCTION: Binds IGF-I and IGF-II with a relatively low affinity.
CC Stimulates prostacyclin (PGI2) production. Stimulates cell adhesion.
CC {ECO:0000269|PubMed:8117260, ECO:0000269|PubMed:8939990}.
CC -!- SUBUNIT: May interact with VPS24/CHMP3; the relevance of such
CC interaction however remains unclear.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q16270-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16270-2; Sequence=VSP_045297;
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:8939990}.
CC -!- RNA EDITING: Modified_positions=78 {ECO:0000269|PubMed:18772245}, 95
CC {ECO:0000269|PubMed:18772245, ECO:0000269|PubMed:7694637};
CC Note=Partially edited. In the brain, position 78 is edited at about 55%
CC and position 95 at about 31%.;
CC -!- DISEASE: Retinal arterial macroaneurysm with supravalvular pulmonic
CC stenosis (RAMSVPS) [MIM:614224]: An autosomal recessive condition
CC characterized by the bilateral appearance of 'beading' along the major
CC retinal arterial trunks, with the subsequent formation of
CC macroaneurysms. Affected individuals also have supravalvular pulmonic
CC stenosis, often requiring surgical correction.
CC {ECO:0000269|PubMed:21835307}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/igfbp7/";
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DR EMBL; L19182; AAA16187.1; -; mRNA.
DR EMBL; S75725; AAB32370.1; -; mRNA.
DR EMBL; AY518539; AAR89912.1; -; Genomic_DNA.
DR EMBL; BT006654; AAP35300.1; -; mRNA.
DR EMBL; AK303915; BAG64844.1; -; mRNA.
DR EMBL; AK316082; BAH14453.1; -; mRNA.
DR EMBL; AC069307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC111197; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017201; AAH17201.1; -; mRNA.
DR EMBL; BC066339; AAH66339.1; -; mRNA.
DR CCDS; CCDS3512.1; -. [Q16270-1]
DR CCDS; CCDS58900.1; -. [Q16270-2]
DR PIR; I52825; I52825.
DR PIR; PC2030; PC2030.
DR PIR; S50031; S50031.
DR RefSeq; NP_001240764.1; NM_001253835.1. [Q16270-2]
DR RefSeq; NP_001544.1; NM_001553.2. [Q16270-1]
DR AlphaFoldDB; Q16270; -.
DR SMR; Q16270; -.
DR BioGRID; 109711; 14.
DR IntAct; Q16270; 11.
DR MINT; Q16270; -.
DR STRING; 9606.ENSP00000295666; -.
DR DrugBank; DB00030; Insulin human.
DR GlyGen; Q16270; 4 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q16270; -.
DR PhosphoSitePlus; Q16270; -.
DR BioMuta; IGFBP7; -.
DR DMDM; 23396609; -.
DR EPD; Q16270; -.
DR jPOST; Q16270; -.
DR MassIVE; Q16270; -.
DR MaxQB; Q16270; -.
DR PaxDb; Q16270; -.
DR PeptideAtlas; Q16270; -.
DR PRIDE; Q16270; -.
DR ProteomicsDB; 5772; -.
DR ProteomicsDB; 60846; -. [Q16270-1]
DR Antibodypedia; 997; 557 antibodies from 41 providers.
DR DNASU; 3490; -.
DR Ensembl; ENST00000295666.6; ENSP00000295666.4; ENSG00000163453.11. [Q16270-1]
DR Ensembl; ENST00000514062.2; ENSP00000486293.1; ENSG00000163453.11. [Q16270-2]
DR GeneID; 3490; -.
DR KEGG; hsa:3490; -.
DR MANE-Select; ENST00000295666.6; ENSP00000295666.4; NM_001553.3; NP_001544.1.
DR UCSC; uc003hcn.4; human. [Q16270-1]
DR CTD; 3490; -.
DR DisGeNET; 3490; -.
DR GeneCards; IGFBP7; -.
DR HGNC; HGNC:5476; IGFBP7.
DR HPA; ENSG00000163453; Low tissue specificity.
DR MalaCards; IGFBP7; -.
DR MIM; 602867; gene.
DR MIM; 614224; phenotype.
DR neXtProt; NX_Q16270; -.
DR OpenTargets; ENSG00000163453; -.
DR Orphanet; 284247; Familial retinal arterial macroaneurysm.
DR PharmGKB; PA29709; -.
DR VEuPathDB; HostDB:ENSG00000163453; -.
DR eggNOG; ENOG502RACD; Eukaryota.
DR GeneTree; ENSGT00530000063555; -.
DR InParanoid; Q16270; -.
DR OMA; CHATNSK; -.
DR OrthoDB; 994901at2759; -.
DR PhylomeDB; Q16270; -.
DR TreeFam; TF331645; -.
DR PathwayCommons; Q16270; -.
DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
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; Q16270; -.
DR BioGRID-ORCS; 3490; 11 hits in 1083 CRISPR screens.
DR ChiTaRS; IGFBP7; human.
DR GeneWiki; IGFBP7; -.
DR GenomeRNAi; 3490; -.
DR Pharos; Q16270; Tbio.
DR PRO; PR:Q16270; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q16270; protein.
DR Bgee; ENSG00000163453; Expressed in vena cava and 211 other tissues.
DR Genevisible; Q16270; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005520; F:insulin-like growth factor binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEA:Ensembl.
DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0001558; P:regulation of cell growth; IEA:InterPro.
DR GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
DR GO; GO:0050810; P:regulation of steroid biosynthetic process; IEA:Ensembl.
DR GO; GO:0051414; P:response to cortisol; IEA:Ensembl.
DR GO; GO:0009408; P:response to heat; IEA:Ensembl.
DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
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; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
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; 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; 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 Alternative splicing; Cell adhesion; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Growth factor binding; Immunoglobulin domain;
KW Phosphoprotein; Reference proteome; RNA editing; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:15340161,
FT ECO:0000269|PubMed:8117260, ECO:0000269|PubMed:8939990"
FT CHAIN 27..282
FT /note="Insulin-like growth factor-binding protein 7"
FT /id="PRO_0000014392"
FT DOMAIN 28..106
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 105..158
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 160..264
FT /note="Ig-like C2-type"
FT MOD_RES 239
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:8939990"
FT DISULFID 120..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 181..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 278..282
FT /note="EGAEL -> TQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045297"
FT VARIANT 11
FT /note="L -> F (in dbSNP:rs11573021)"
FT /evidence="ECO:0000269|PubMed:7694637, ECO:0000269|Ref.4"
FT /id="VAR_018959"
FT VARIANT 78
FT /note="R -> G (in RNA edited version; dbSNP:rs11555284)"
FT /id="VAR_063638"
FT VARIANT 95
FT /note="K -> R (in RNA edited version; dbSNP:rs1133243)"
FT /id="VAR_063639"
FT CONFLICT 4
FT /note="P -> A (in Ref. 1; AAA16187)"
FT /evidence="ECO:0000305"
FT CONFLICT 13
FT /note="A -> P (in Ref. 1; AAA16187)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="E -> G (in Ref. 5; BAH14453)"
FT /evidence="ECO:0000305"
FT CONFLICT 273..282
FT /note="PVKKGEGAEL -> ASEKR (in Ref. 1; AAA16187)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 282 AA; 29130 MW; 75F96EBC3B444D37 CRC64;
MERPSLRALL LGAAGLLLLL LPLSSSSSSD TCGPCEPASC PPLPPLGCLL GETRDACGCC
PMCARGEGEP CGGGGAGRGY CAPGMECVKS RKRRKGKAGA AAGGPGVSGV CVCKSRYPVC
GSDGTTYPSG CQLRAASQRA ESRGEKAITQ VSKGTCEQGP SIVTPPKDIW NVTGAQVYLS
CEVIGIPTPV LIWNKVKRGH YGVQRTELLP GDRDNLAIQT RGGPEKHEVT GWVLVSPLSK
EDAGEYECHA SNSQGQASAS AKITVVDALH EIPVKKGEGA EL
