WNT2B_HUMAN
ID WNT2B_HUMAN Reviewed; 391 AA.
AC Q93097; O14903; Q5TEH9; Q5TEI2; Q9HDC1; Q9HDC2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Protein Wnt-2b;
DE AltName: Full=Protein Wnt-13 {ECO:0000303|PubMed:8761309};
DE Flags: Precursor;
GN Name=WNT2B; Synonyms=WNT13;
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), AND TISSUE SPECIFICITY.
RX PubMed=8761309;
RA Katoh M., Hirai M., Sugimura T., Terada M.;
RT "Cloning, expression and chromosomal localization of Wnt-13, a novel member
RT of the Wnt gene family.";
RL Oncogene 13:873-876(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX PubMed=10944466; DOI=10.1006/bbrc.2000.3252;
RA Katoh M., Kirikoshi H., Saitoh T., Sagara N., Koike J.;
RT "Alternative splicing of the WNT-2B/WNT-13 gene.";
RL Biochem. Biophys. Res. Commun. 275:209-216(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 243-359.
RX PubMed=9441749; DOI=10.1006/geno.1997.5041;
RA Bergstein I., Eisenberg L.M., Bhalerao J., Jenkins N.A., Copeland N.G.,
RA Osborne M.P., Bowcock A.M., Brown A.M.C.;
RT "Isolation of two novel WNT genes, WNT14 and WNT15, one of which (WNT15) is
RT closely linked to WNT3 on human chromosome 17q21.";
RL Genomics 46:450-458(1997).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-117 AND ASN-283.
RC TISSUE=Milk;
RX PubMed=18780401; DOI=10.1002/pmic.200701057;
RA Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
RT "Identification of N-linked glycoproteins in human milk by hydrophilic
RT interaction liquid chromatography and mass spectrometry.";
RL Proteomics 8:3833-3847(2008).
RN [9]
RP INTERACTION WITH AFM, AND SUBCELLULAR LOCATION.
RX PubMed=26902720; DOI=10.7554/elife.11621;
RA Mihara E., Hirai H., Yamamoto H., Tamura-Kawakami K., Matano M.,
RA Kikuchi A., Sato T., Takagi J.;
RT "Active and water-soluble form of lipidated Wnt protein is maintained by a
RT serum glycoprotein afamin/alpha-albumin.";
RL Elife 5:0-0(2016).
RN [10]
RP INVOLVEMENT IN DIAR9, VARIANTS DIAR9 69-ARG--THR-391 DEL AND
RP 105-ARG--THR-391 DEL, AND CHARACTERIZATION OF VARIANT DIAR9 69-ARG--THR-391
RP DEL.
RX PubMed=29909964; DOI=10.1016/j.ajhg.2018.05.007;
RA O'Connell A.E., Zhou F., Shah M.S., Murphy Q., Rickner H., Kelsen J.,
RA Boyle J., Doyle J.J., Gangwani B., Thiagarajah J.R., Kamin D.S.,
RA Goldsmith J.D., Richmond C., Breault D.T., Agrawal P.B.;
RT "Neonatal-Onset Chronic Diarrhea Caused by Homozygous Nonsense WNT2B
RT Mutations.";
RL Am. J. Hum. Genet. 103:131-137(2018).
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors. Functions in the canonical Wnt/beta-catenin
CC signaling pathway. Plays a redundant role in embryonic lung
CC development. {ECO:0000250|UniProtKB:O70283}.
CC -!- SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents
CC oligomerization and is required for prolonged biological activity
CC (PubMed:26902720). The complex with AFM may represent the physiological
CC form in body fluids (PubMed:26902720). Interacts with FZD4 and FZD5 (By
CC similarity). {ECO:0000250|UniProtKB:Q98SN7,
CC ECO:0000269|PubMed:26902720}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:26902720}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q93097-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q93097-2; Sequence=VSP_006794;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in adult heart, brain,
CC placenta, lung, prostate, testis, ovary, small intestine and colon. In
CC the adult brain, it is mainly found in the caudate nucleus, subthalamic
CC nucleus and thalamus. Also detected in fetal brain, lung and kidney.
CC Isoform 2 is expressed in fetal brain, fetal lung, fetal kidney,
CC caudate nucleus, testis and cancer cell lines.
CC {ECO:0000269|PubMed:10944466, ECO:0000269|PubMed:8761309}.
CC -!- PTM: Palmitoleoylation is required for efficient binding to frizzled
CC receptors. Depalmitoleoylation leads to Wnt signaling pathway
CC inhibition. {ECO:0000250|UniProtKB:P27467,
CC ECO:0000250|UniProtKB:P56704}.
CC -!- DISEASE: Diarrhea 9 (DIAR9) [MIM:618168]: An autosomal recessive form
CC of chronic diarrhea characterized by neonatal-onset of osmotic diarrhea
CC that is not substrate specific, abnormal crypt and villus architecture,
CC and significant fat malabsorption evidenced by high levels of fecal
CC fat. {ECO:0000269|PubMed:29909964}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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DR EMBL; Z71621; CAA96283.1; -; mRNA.
DR EMBL; AB045116; BAB11984.1; -; mRNA.
DR EMBL; AB045117; BAB11985.1; -; mRNA.
DR EMBL; AK312696; BAG35575.1; -; mRNA.
DR EMBL; AL354760; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL109932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471122; EAW56519.1; -; Genomic_DNA.
DR EMBL; BC141825; AAI41826.1; -; mRNA.
DR EMBL; AF028701; AAC39552.1; -; mRNA.
DR CCDS; CCDS846.1; -. [Q93097-2]
DR CCDS; CCDS847.1; -. [Q93097-1]
DR PIR; T09612; T09612.
DR RefSeq; NP_001278809.1; NM_001291880.1.
DR RefSeq; NP_004176.2; NM_004185.4. [Q93097-2]
DR RefSeq; NP_078613.1; NM_024494.2. [Q93097-1]
DR AlphaFoldDB; Q93097; -.
DR SMR; Q93097; -.
DR BioGRID; 113319; 5.
DR IntAct; Q93097; 1.
DR STRING; 9606.ENSP00000358698; -.
DR GlyGen; Q93097; 2 sites.
DR iPTMnet; Q93097; -.
DR PhosphoSitePlus; Q93097; -.
DR BioMuta; WNT2B; -.
DR DMDM; 14424481; -.
DR MassIVE; Q93097; -.
DR PaxDb; Q93097; -.
DR PeptideAtlas; Q93097; -.
DR PRIDE; Q93097; -.
DR ProteomicsDB; 75722; -. [Q93097-1]
DR ProteomicsDB; 75723; -. [Q93097-2]
DR Antibodypedia; 20129; 247 antibodies from 30 providers.
DR DNASU; 7482; -.
DR Ensembl; ENST00000369684.5; ENSP00000358698.4; ENSG00000134245.18. [Q93097-1]
DR Ensembl; ENST00000369686.9; ENSP00000358700.4; ENSG00000134245.18. [Q93097-2]
DR GeneID; 7482; -.
DR KEGG; hsa:7482; -.
DR MANE-Select; ENST00000369684.5; ENSP00000358698.4; NM_024494.3; NP_078613.1.
DR UCSC; uc001eca.4; human. [Q93097-1]
DR CTD; 7482; -.
DR DisGeNET; 7482; -.
DR GeneCards; WNT2B; -.
DR HGNC; HGNC:12781; WNT2B.
DR HPA; ENSG00000134245; Low tissue specificity.
DR MalaCards; WNT2B; -.
DR MIM; 601968; gene.
DR MIM; 618168; phenotype.
DR neXtProt; NX_Q93097; -.
DR OpenTargets; ENSG00000134245; -.
DR PharmGKB; PA37382; -.
DR VEuPathDB; HostDB:ENSG00000134245; -.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000159166; -.
DR HOGENOM; CLU_033039_1_0_1; -.
DR InParanoid; Q93097; -.
DR OMA; IHYGIRF; -.
DR OrthoDB; 745245at2759; -.
DR PhylomeDB; Q93097; -.
DR TreeFam; TF105310; -.
DR PathwayCommons; Q93097; -.
DR Reactome; R-HSA-3238698; WNT ligand biogenesis and trafficking.
DR Reactome; R-HSA-373080; Class B/2 (Secretin family receptors).
DR SignaLink; Q93097; -.
DR SIGNOR; Q93097; -.
DR BioGRID-ORCS; 7482; 15 hits in 1069 CRISPR screens.
DR ChiTaRS; WNT2B; human.
DR GeneWiki; WNT2B; -.
DR GenomeRNAi; 7482; -.
DR Pharos; Q93097; Tbio.
DR PRO; PR:Q93097; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q93097; protein.
DR Bgee; ENSG00000134245; Expressed in germinal epithelium of ovary and 147 other tissues.
DR ExpressionAtlas; Q93097; baseline and differential.
DR Genevisible; Q93097; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0005109; F:frizzled binding; IBA:GO_Central.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
DR GO; GO:0002062; P:chondrocyte differentiation; IEP:UniProtKB.
DR GO; GO:0061303; P:cornea development in camera-type eye; ISS:BHF-UCL.
DR GO; GO:0021871; P:forebrain regionalization; IEP:UniProtKB.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IDA:BHF-UCL.
DR GO; GO:0061072; P:iris morphogenesis; ISS:BHF-UCL.
DR GO; GO:0002088; P:lens development in camera-type eye; ISS:BHF-UCL.
DR GO; GO:0060492; P:lung induction; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEP:UniProtKB.
DR GO; GO:0060638; P:mesenchymal-epithelial cell signaling; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR009140; Wnt2.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01842; WNT2PROTEIN.
DR PRINTS; PR01349; WNTPROTEIN.
DR SMART; SM00097; WNT1; 1.
DR PROSITE; PS00246; WNT1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Disease variant;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Lipoprotein;
KW Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT CHAIN ?..391
FT /note="Protein Wnt-2b"
FT /id="PRO_0000041413"
FT LIPID 243
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18780401"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18780401"
FT DISULFID 107..118
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 158..166
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 168..188
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 237..251
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 239..246
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 309..340
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 325..335
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 339..379
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 355..370
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 357..367
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 362..363
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT VAR_SEQ 1..61
FT /note="MLRPGGAEEAAQLPLRRASAPVPVPSPAAPDGSRASARLGLACLLLLLLLTL
FT PARVDTSWW -> MLDGLGVVAISIFGIQLKTEGSLRTAVPGIPTQSAFNKCLQR (in
FT isoform 1)"
FT /evidence="ECO:0000303|PubMed:10944466,
FT ECO:0000303|PubMed:8761309"
FT /id="VSP_006794"
FT VARIANT 69..391
FT /note="Missing (in DIAR9; diminished staining for the
FT intestinal stem cell marker OLFM4; enteroid cultures
FT generated from patient intestinal epithelium cannot be
FT expanded and do not survive multiple passages; shows a 10-
FT fold increase in LEF1 mRNA and a 100-fold reduction in TLR4
FT expression compared to controls indicating alterations in
FT canonical Wnt signaling and microbial pattern-recognition
FT signaling)"
FT /evidence="ECO:0000269|PubMed:29909964"
FT /id="VAR_081727"
FT VARIANT 105..391
FT /note="Missing (in DIAR9)"
FT /evidence="ECO:0000269|PubMed:29909964"
FT /id="VAR_081728"
FT CONFLICT 151
FT /note="V -> I (in Ref. 1; CAA96283)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="D -> T (in Ref. 1; CAA96283)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="L -> V (in Ref. 1; CAA96283)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="A -> T (in Ref. 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="T -> S (in Ref. 1; CAA96283)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 391 AA; 43770 MW; BD7BB7F795FB33B1 CRC64;
MLRPGGAEEA AQLPLRRASA PVPVPSPAAP DGSRASARLG LACLLLLLLL TLPARVDTSW
WYIGALGARV ICDNIPGLVS RQRQLCQRYP DIMRSVGEGA REWIRECQHQ FRHHRWNCTT
LDRDHTVFGR VMLRSSREAA FVYAISSAGV VHAITRACSQ GELSVCSCDP YTRGRHHDQR
GDFDWGGCSD NIHYGVRFAK AFVDAKEKRL KDARALMNLH NNRCGRTAVR RFLKLECKCH
GVSGSCTLRT CWRALSDFRR TGDYLRRRYD GAVQVMATQD GANFTAARQG YRRATRTDLV
YFDNSPDYCV LDKAAGSLGT AGRVCSKTSK GTDGCEIMCC GRGYDTTRVT RVTQCECKFH
WCCAVRCKEC RNTVDVHTCK APKKAEWLDQ T
