NRG2_HUMAN
ID NRG2_HUMAN Reviewed; 850 AA.
AC O14511;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Pro-neuregulin-2, membrane-bound isoform;
DE Short=Pro-NRG2;
DE Contains:
DE RecName: Full=Neuregulin-2;
DE Short=NRG-2;
DE AltName: Full=Divergent of neuregulin-1;
DE Short=DON-1;
DE AltName: Full=Neural- and thymus-derived activator for ERBB kinases;
DE Short=NTAK;
DE Flags: Precursor;
GN Name=NRG2; Synonyms=NTAK;
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=Neuroblastoma;
RX PubMed=9348101; DOI=10.1093/oxfordjournals.jbchem.a021806;
RA Higashiyama S., Horikawa M., Yamada K., Ichino N., Nakano N., Nakagawa T.,
RA Miyagawa J., Matsushita N., Nagatsu T., Taniguchi N., Ishiguro H.;
RT "A novel brain-derived member of the epidermal growth factor family that
RT interacts with ErbB3 and ErbB4.";
RL J. Biochem. 122:675-680(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS DON-1B AND DON-1R).
RC TISSUE=Fetal brain;
RX PubMed=9199335; DOI=10.1128/mcb.17.7.4007;
RA Busfield S.J., Michnick D.A., Chickering T.W., Revett T.L., Ma J.,
RA Woolf E.A., Comrack C.A., Dussault B.J., Woolf J., Goodearl A.D.J.,
RA Gearing D.P.;
RT "Characterization of a neuregulin-related gene, Don-1, that is highly
RT expressed in restricted regions of the cerebellum and hippocampus.";
RL Mol. Cell. Biol. 17:4007-4014(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS 1; 2;
RP 3; 4; 5 AND 6).
RC TISSUE=Fetal brain, and Lung;
RX PubMed=10369162; DOI=10.1007/s004390050961;
RA Ring H.Z., Chang H., Guilbot A., Brice A., LeGuern E., Francke U.;
RT "The human neuregulin 2 (NRG2) gene: cloning, mapping and evaluation as a
RT candidate for the autosomal recessive form of Charcot-Marie-Tooth disease
RT linked to 5q.";
RL Hum. Genet. 104:326-332(1999).
RN [4]
RP INTERACTION WITH ERBB4.
RX PubMed=10867024; DOI=10.1074/jbc.c901015199;
RA Sweeney C., Lai C., Riese D.J. II, Diamonti A.J., Cantley L.C.,
RA Carraway K.L. III;
RT "Ligand discrimination in signaling through an ErbB4 receptor homodimer.";
RL J. Biol. Chem. 275:19803-19807(2000).
CC -!- FUNCTION: Direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors.
CC Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in
CC ligand-stimulated tyrosine phosphorylation and activation of the ERBB
CC receptors. May also promote the heterodimerization with the EGF
CC receptor.
CC -!- SUBUNIT: Interacts with ERBB3 and ERBB4. {ECO:0000269|PubMed:10867024}.
CC -!- SUBCELLULAR LOCATION: [Pro-neuregulin-2, membrane-bound isoform]: Cell
CC membrane {ECO:0000250}; Single-pass type I membrane protein
CC {ECO:0000250}. Note=Does not seem to be active. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Neuregulin-2]: Secreted {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=O14511-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14511-2; Sequence=VSP_003453;
CC Name=3;
CC IsoId=O14511-3; Sequence=VSP_003455;
CC Name=4;
CC IsoId=O14511-4; Sequence=VSP_003454;
CC Name=5;
CC IsoId=O14511-5; Sequence=VSP_003458, VSP_003459;
CC Name=6;
CC IsoId=O14511-6; Sequence=VSP_003456, VSP_003457;
CC Name=DON-1B;
CC IsoId=O14511-7; Sequence=VSP_003452, VSP_003455;
CC Name=DON-1R;
CC IsoId=O14511-8; Sequence=VSP_003451;
CC -!- TISSUE SPECIFICITY: Restricted to the cerebellum in the adult.
CC -!- DOMAIN: The cytoplasmic domain may be involved in the regulation of
CC trafficking and proteolytic processing. Regulation of the proteolytic
CC processing involves initial intracellular domain dimerization (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: ERBB receptor binding is elicited entirely by the EGF-like
CC domain. {ECO:0000250}.
CC -!- PTM: Proteolytic cleavage close to the plasma membrane on the external
CC face leads to the release of the soluble growth factor form.
CC {ECO:0000250}.
CC -!- PTM: Extensive glycosylation precedes the proteolytic cleavage.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the neuregulin family. {ECO:0000305}.
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DR EMBL; AB005060; BAA23417.1; -; mRNA.
DR EMBL; AF119162; AAF28848.1; -; Genomic_DNA.
DR EMBL; AF119151; AAF28848.1; JOINED; Genomic_DNA.
DR EMBL; AF119152; AAF28848.1; JOINED; Genomic_DNA.
DR EMBL; AF119153; AAF28848.1; JOINED; Genomic_DNA.
DR EMBL; AF119154; AAF28848.1; JOINED; Genomic_DNA.
DR EMBL; AF119155; AAF28848.1; JOINED; Genomic_DNA.
DR EMBL; AF119158; AAF28848.1; JOINED; Genomic_DNA.
DR EMBL; AF119159; AAF28848.1; JOINED; Genomic_DNA.
DR EMBL; AF119160; AAF28848.1; JOINED; Genomic_DNA.
DR EMBL; AF119161; AAF28848.1; JOINED; Genomic_DNA.
DR EMBL; AF119162; AAF28849.1; -; Genomic_DNA.
DR EMBL; AF119151; AAF28849.1; JOINED; Genomic_DNA.
DR EMBL; AF119152; AAF28849.1; JOINED; Genomic_DNA.
DR EMBL; AF119153; AAF28849.1; JOINED; Genomic_DNA.
DR EMBL; AF119154; AAF28849.1; JOINED; Genomic_DNA.
DR EMBL; AF119156; AAF28849.1; JOINED; Genomic_DNA.
DR EMBL; AF119158; AAF28849.1; JOINED; Genomic_DNA.
DR EMBL; AF119159; AAF28849.1; JOINED; Genomic_DNA.
DR EMBL; AF119160; AAF28849.1; JOINED; Genomic_DNA.
DR EMBL; AF119161; AAF28849.1; JOINED; Genomic_DNA.
DR EMBL; AF119162; AAF28850.1; -; Genomic_DNA.
DR EMBL; AF119151; AAF28850.1; JOINED; Genomic_DNA.
DR EMBL; AF119152; AAF28850.1; JOINED; Genomic_DNA.
DR EMBL; AF119153; AAF28850.1; JOINED; Genomic_DNA.
DR EMBL; AF119154; AAF28850.1; JOINED; Genomic_DNA.
DR EMBL; AF119155; AAF28850.1; JOINED; Genomic_DNA.
DR EMBL; AF119157; AAF28850.1; JOINED; Genomic_DNA.
DR EMBL; AF119158; AAF28850.1; JOINED; Genomic_DNA.
DR EMBL; AF119159; AAF28850.1; JOINED; Genomic_DNA.
DR EMBL; AF119160; AAF28850.1; JOINED; Genomic_DNA.
DR EMBL; AF119161; AAF28850.1; JOINED; Genomic_DNA.
DR EMBL; AF119162; AAF28851.1; -; Genomic_DNA.
DR EMBL; AF119151; AAF28851.1; JOINED; Genomic_DNA.
DR EMBL; AF119152; AAF28851.1; JOINED; Genomic_DNA.
DR EMBL; AF119153; AAF28851.1; JOINED; Genomic_DNA.
DR EMBL; AF119154; AAF28851.1; JOINED; Genomic_DNA.
DR EMBL; AF119156; AAF28851.1; JOINED; Genomic_DNA.
DR EMBL; AF119157; AAF28851.1; JOINED; Genomic_DNA.
DR EMBL; AF119158; AAF28851.1; JOINED; Genomic_DNA.
DR EMBL; AF119159; AAF28851.1; JOINED; Genomic_DNA.
DR EMBL; AF119160; AAF28851.1; JOINED; Genomic_DNA.
DR EMBL; AF119161; AAF28851.1; JOINED; Genomic_DNA.
DR EMBL; AF119158; AAF28852.1; -; Genomic_DNA.
DR EMBL; AF119151; AAF28852.1; JOINED; Genomic_DNA.
DR EMBL; AF119152; AAF28852.1; JOINED; Genomic_DNA.
DR EMBL; AF119153; AAF28852.1; JOINED; Genomic_DNA.
DR EMBL; AF119154; AAF28852.1; JOINED; Genomic_DNA.
DR EMBL; AF119155; AAF28852.1; JOINED; Genomic_DNA.
DR EMBL; AF119156; AAF28852.1; JOINED; Genomic_DNA.
DR EMBL; AF119157; AAF28853.1; -; Genomic_DNA.
DR EMBL; AF119151; AAF28853.1; JOINED; Genomic_DNA.
DR EMBL; AF119152; AAF28853.1; JOINED; Genomic_DNA.
DR EMBL; AF119153; AAF28853.1; JOINED; Genomic_DNA.
DR EMBL; AF119154; AAF28853.1; JOINED; Genomic_DNA.
DR EMBL; AF119155; AAF28853.1; JOINED; Genomic_DNA.
DR EMBL; AF119156; AAF28853.1; JOINED; Genomic_DNA.
DR CCDS; CCDS4217.1; -. [O14511-1]
DR PIR; JC5700; JC5700.
DR RefSeq; NP_001171864.1; NM_001184935.1.
DR RefSeq; NP_004874.1; NM_004883.2. [O14511-1]
DR RefSeq; NP_053584.1; NM_013981.3. [O14511-2]
DR RefSeq; NP_053585.1; NM_013982.2. [O14511-3]
DR RefSeq; NP_053586.1; NM_013983.2. [O14511-4]
DR RefSeq; XP_006714873.1; XM_006714810.3. [O14511-6]
DR AlphaFoldDB; O14511; -.
DR BioGRID; 114917; 5.
DR STRING; 9606.ENSP00000354910; -.
DR GlyGen; O14511; 5 sites.
DR iPTMnet; O14511; -.
DR PhosphoSitePlus; O14511; -.
DR BioMuta; NRG2; -.
DR EPD; O14511; -.
DR MassIVE; O14511; -.
DR PaxDb; O14511; -.
DR PeptideAtlas; O14511; -.
DR PRIDE; O14511; -.
DR ProteomicsDB; 48047; -. [O14511-1]
DR ProteomicsDB; 48048; -. [O14511-2]
DR ProteomicsDB; 48049; -. [O14511-3]
DR ProteomicsDB; 48050; -. [O14511-4]
DR ProteomicsDB; 48051; -. [O14511-5]
DR ProteomicsDB; 48052; -. [O14511-6]
DR ProteomicsDB; 48053; -. [O14511-7]
DR ProteomicsDB; 48054; -. [O14511-8]
DR Antibodypedia; 26820; 199 antibodies from 25 providers.
DR DNASU; 9542; -.
DR Ensembl; ENST00000289409.8; ENSP00000289409.4; ENSG00000158458.21. [O14511-2]
DR Ensembl; ENST00000289422.11; ENSP00000289422.7; ENSG00000158458.21. [O14511-3]
DR Ensembl; ENST00000340391.8; ENSP00000342660.3; ENSG00000158458.21. [O14511-8]
DR Ensembl; ENST00000358522.7; ENSP00000351323.3; ENSG00000158458.21. [O14511-4]
DR Ensembl; ENST00000361474.6; ENSP00000354910.1; ENSG00000158458.21. [O14511-1]
DR Ensembl; ENST00000378238.5; ENSP00000367483.4; ENSG00000158458.21. [O14511-5]
DR GeneID; 9542; -.
DR KEGG; hsa:9542; -.
DR MANE-Select; ENST00000361474.6; ENSP00000354910.1; NM_004883.3; NP_004874.1.
DR UCSC; uc003lev.3; human. [O14511-1]
DR CTD; 9542; -.
DR DisGeNET; 9542; -.
DR GeneCards; NRG2; -.
DR HGNC; HGNC:7998; NRG2.
DR HPA; ENSG00000158458; Low tissue specificity.
DR MIM; 603818; gene.
DR neXtProt; NX_O14511; -.
DR OpenTargets; ENSG00000158458; -.
DR PharmGKB; PA31777; -.
DR VEuPathDB; HostDB:ENSG00000158458; -.
DR eggNOG; ENOG502QRNM; Eukaryota.
DR GeneTree; ENSGT00940000158778; -.
DR HOGENOM; CLU_023628_0_0_1; -.
DR InParanoid; O14511; -.
DR OMA; QMADYMS; -.
DR OrthoDB; 313400at2759; -.
DR PhylomeDB; O14511; -.
DR TreeFam; TF332469; -.
DR PathwayCommons; O14511; -.
DR Reactome; R-HSA-1227986; Signaling by ERBB2.
DR Reactome; R-HSA-1236394; Signaling by ERBB4.
DR Reactome; R-HSA-1250196; SHC1 events in ERBB2 signaling.
DR Reactome; R-HSA-1250342; PI3K events in ERBB4 signaling.
DR Reactome; R-HSA-1250347; SHC1 events in ERBB4 signaling.
DR Reactome; R-HSA-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-1306955; GRB7 events in ERBB2 signaling.
DR Reactome; R-HSA-1358803; Downregulation of ERBB2:ERBB3 signaling.
DR Reactome; R-HSA-1963640; GRB2 events in ERBB2 signaling.
DR Reactome; R-HSA-1963642; PI3K events in ERBB2 signaling.
DR Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-6785631; ERBB2 Regulates Cell Motility.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-HSA-8847993; ERBB2 Activates PTK6 Signaling.
DR Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-HSA-9664565; Signaling by ERBB2 KD Mutants.
DR Reactome; R-HSA-9665686; Signaling by ERBB2 TMD/JMD mutants.
DR SignaLink; O14511; -.
DR SIGNOR; O14511; -.
DR BioGRID-ORCS; 9542; 19 hits in 1066 CRISPR screens.
DR ChiTaRS; NRG2; human.
DR GeneWiki; NRG2; -.
DR GenomeRNAi; 9542; -.
DR Pharos; O14511; Tbio.
DR PRO; PR:O14511; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O14511; protein.
DR Bgee; ENSG00000158458; Expressed in buccal mucosa cell and 137 other tissues.
DR ExpressionAtlas; O14511; baseline and differential.
DR Genevisible; O14511; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0048513; P:animal organ development; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR000742; EGF-like_dom.
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; IPR003598; Ig_sub2.
DR InterPro; IPR040180; Neuregulin.
DR InterPro; IPR002154; Neuregulin_C.
DR PANTHER; PTHR11100; PTHR11100; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF02158; Neuregulin; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; EGF-like domain;
KW Glycoprotein; Growth factor; Immunoglobulin domain; Membrane;
KW Reference proteome; Secreted; Transmembrane; Transmembrane helix.
FT PROPEP 1..111
FT /evidence="ECO:0000250"
FT /id="PRO_0000019472"
FT CHAIN 112..850
FT /note="Pro-neuregulin-2, membrane-bound isoform"
FT /id="PRO_0000019473"
FT CHAIN 112..404
FT /note="Neuregulin-2"
FT /id="PRO_0000019474"
FT TOPO_DOM 112..405
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical; Note=Internal signal sequence"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..850
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 237..332
FT /note="Ig-like C2-type"
FT DOMAIN 341..382
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..665
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 257..311
FT /evidence="ECO:0000250"
FT DISULFID 345..359
FT /evidence="ECO:0000250"
FT DISULFID 353..370
FT /evidence="ECO:0000250"
FT DISULFID 372..381
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..241
FT /note="Missing (in isoform DON-1B)"
FT /evidence="ECO:0000303|PubMed:9199335"
FT /id="VSP_003452"
FT VAR_SEQ 1..233
FT /note="MRQVCCSALPPPPLEKGRCSSYSDSSSSSSERSSSSSSSSSESGSSSRSSSN
FT NSSISRPAAPPEPRPQQQPQPRSPAARRAAARSRAAAAGGMRRDPAPGFSMLLFGVSLA
FT CYSPSLKSVQDQAYKAPVVVEGKVQGLVPAGGSSSNSTREPPASGRVALVKVLDKWPLR
FT SGGLQREQVISVGSCVPLERNQRYIFFLEPTEQPLVFKTAFAPLDTNGKNLKKEVGKIL
FT CTDC -> MSESRRRGRGRGKKHPEGRKREREPDPGEK (in isoform DON-1R)"
FT /evidence="ECO:0000303|PubMed:9199335"
FT /id="VSP_003451"
FT VAR_SEQ 374..397
FT /note="NGFFGQRCLEKLPLRLYMPDPKQK -> VGYTGDRCQQFAMVNFSKHLGFEL
FT KE (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_003454"
FT VAR_SEQ 374..396
FT /note="NGFFGQRCLEKLPLRLYMPDPKQ -> VGYTGDRCQQFAMVNFS (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_003453"
FT VAR_SEQ 397..426
FT /note="KAEELYQKRVLTITGICVALLVVGIVCVVA -> SVLWDTPGTGVSSSQWST
FT SPKPRSCTRRGS (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_003458"
FT VAR_SEQ 397..422
FT /note="KAEELYQKRVLTITGICVALLVVGIV -> SVLWDTPGTGVSSSQWSTSPST
FT LDLN (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_003456"
FT VAR_SEQ 397
FT /note="K -> KHLGFELKE (in isoform 3 and isoform DON-1B)"
FT /evidence="ECO:0000303|PubMed:9199335"
FT /id="VSP_003455"
FT VAR_SEQ 423..850
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_003457"
FT VAR_SEQ 427..850
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_003459"
SQ SEQUENCE 850 AA; 91679 MW; 7124C089435FD2F4 CRC64;
MRQVCCSALP PPPLEKGRCS SYSDSSSSSS ERSSSSSSSS SESGSSSRSS SNNSSISRPA
APPEPRPQQQ PQPRSPAARR AAARSRAAAA GGMRRDPAPG FSMLLFGVSL ACYSPSLKSV
QDQAYKAPVV VEGKVQGLVP AGGSSSNSTR EPPASGRVAL VKVLDKWPLR SGGLQREQVI
SVGSCVPLER NQRYIFFLEP TEQPLVFKTA FAPLDTNGKN LKKEVGKILC TDCATRPKLK
KMKSQTGQVG EKQSLKCEAA AGNPQPSYRW FKDGKELNRS RDIRIKYGNG RKNSRLQFNK
VKVEDAGEYV CEAENILGKD TVRGRLYVNS VSTTLSSWSG HARKCNETAK SYCVNGGVCY
YIEGINQLSC KCPNGFFGQR CLEKLPLRLY MPDPKQKAEE LYQKRVLTIT GICVALLVVG
IVCVVAYCKT KKQRKQMHNH LRQNMCPAHQ NRSLANGPSH PRLDPEEIQM ADYISKNVPA
TDHVIRRETE TTFSGSHSCS PSHHCSTATP TSSHRHESHT WSLERSESLT SDSQSGIMLS
SVGTSKCNSP ACVEARARRA AAYNLEERRR ATAPPYHDSV DSLRDSPHSE RYVSALTTPA
RLSPVDFHYS LATQVPTFEI TSPNSAHAVS LPPAAPISYR LAEQQPLLRH PAPPGPGPGP
GPGPGPGADM QRSYDSYYYP AAGPGPRRGT CALGGSLGSL PASPFRIPED DEYETTQECA
PPPPPRPRAR GASRRTSAGP RRWRRSRLNG LAAQRARAAR DSLSLSSGSG GGSASASDDD
ADDADGALAA ESTPFLGLRG AHDALRSDSP PLCPAADSRT YYSLDSHSTR ASSRHSRGPP
PRAKQDSAPL
