TEN2_HUMAN
ID TEN2_HUMAN Reviewed; 2774 AA.
AC Q9NT68; Q9ULU2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Teneurin-2;
DE Short=Ten-2;
DE AltName: Full=Protein Odd Oz/ten-m homolog 2;
DE AltName: Full=Tenascin-M2;
DE Short=Ten-m2;
DE AltName: Full=Teneurin transmembrane protein 2;
DE Contains:
DE RecName: Full=Ten-2, soluble form;
DE Contains:
DE RecName: Full=Ten-2 intracellular domain;
DE Short=Ten-2 ICD;
GN Name=TENM2; Synonyms=KIAA1127, ODZ2, TNM2;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 631-2774 (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1926-2774 (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP ALTERNATIVE SPLICING (ISOFORM 2), FUNCTION AS ADGRL1 LIGAND, INTERACTION
RP WITH ADGRL1, AND SUBCELLULAR LOCATION.
RX PubMed=21724987; DOI=10.1073/pnas.1019434108;
RA Silva J.P., Lelianova V.G., Ermolyuk Y.S., Vysokov N., Hitchen P.G.,
RA Berninghausen O., Rahman M.A., Zangrandi A., Fidalgo S., Tonevitsky A.G.,
RA Dell A., Volynski K.E., Ushkaryov Y.A.;
RT "Latrophilin 1 and its endogenous ligand Lasso/teneurin-2 form a high-
RT affinity transsynaptic receptor pair with signaling capabilities.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12113-12118(2011).
CC -!- FUNCTION: Involved in neural development, regulating the establishment
CC of proper connectivity within the nervous system. Promotes the
CC formation of filopodia and enlarged growth cone in neuronal cells.
CC Induces homophilic cell-cell adhesion (By similarity). May function as
CC a cellular signal transducer. {ECO:0000250,
CC ECO:0000269|PubMed:21724987}.
CC -!- FUNCTION: [Isoform 2]: Acts as a ligand of the ADGRL1 receptor.
CC Mediates axon guidance and heterophilic cell-cell adhesion.
CC {ECO:0000269|PubMed:21724987}.
CC -!- FUNCTION: [Ten-2 intracellular domain]: Induces gene transcription
CC inhibition. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (Probable). Heterodimer with
CC either TENM1 or TENM3. May also form heterodimer with TENM4 (By
CC similarity). Isoform 2 (C-terminal globular domain) interacts with
CC ADGRL1 isoform 2. {ECO:0000250, ECO:0000269|PubMed:21724987,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi
CC apparatus {ECO:0000250}. Synapse {ECO:0000250}. Cell projection,
CC dendritic spine {ECO:0000250}. Cell projection, filopodium
CC {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Postsynaptic
CC cell membrane {ECO:0000250}; Single-pass membrane protein
CC {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Note=Colocalizes
CC with ADGRL1 across intercellular junctions. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane. Note=Colocalizes with
CC ADGRL1 across intercellular junctions.
CC -!- SUBCELLULAR LOCATION: [Ten-2 intracellular domain]: Nucleus, PML body
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NT68-1; Sequence=Displayed;
CC Name=2; Synonyms=Lasso, LPH1-associated synaptic surface organizer;
CC IsoId=Q9NT68-2; Sequence=VSP_045019, VSP_045020, VSP_045021,
CC VSP_045022;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, followed by brain,
CC liver, kidney and fetal brain and weakly expressed in lung and testis.
CC No expression was detected in skeletal muscle, pancreas, spleen, ovary
CC and fetal liver. {ECO:0000269|PubMed:10574461}.
CC -!- DOMAIN: EGF-like domains 2 and 5 which have an odd number of cysteines
CC might enable the formation of intermolecular disulfide bonds.
CC -!- DOMAIN: Cytoplasmic proline-rich regions could serve as docking domains
CC for intracellular SH3-containing proteins.
CC -!- PTM: [Ten-2, soluble form]: Derives from the membrane form by
CC proteolytic processing. {ECO:0000250}.
CC -!- PTM: [Ten-2 intracellular domain]: Derives from the plasma membrane
CC form by proteolytic cleavage and translocates to the nucleus.
CC Homophilic binding of the C-terminal extracellular domain stimulates
CC its proteolytic cleavage and release in the cytoplasmic. Is subjected
CC to rapid degradation by the proteasome pathway (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC {ECO:0000305}.
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DR EMBL; AC008464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008601; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008642; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008705; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026689; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB032953; BAA86441.2; -; mRNA.
DR EMBL; AL137500; CAB70774.1; -; mRNA.
DR PIR; T46253; T46253.
DR RefSeq; NP_001073897.2; NM_001080428.2.
DR RefSeq; XP_016865149.1; XM_017009660.1. [Q9NT68-1]
DR PDB; 6CMX; EM; 3.10 A; A=846-2774.
DR PDB; 6VHH; EM; 2.97 A; A=846-2774.
DR PDBsum; 6CMX; -.
DR PDBsum; 6VHH; -.
DR SMR; Q9NT68; -.
DR IntAct; Q9NT68; 6.
DR STRING; 9606.ENSP00000429430; -.
DR TCDB; 9.B.87.1.20; the selenoprotein p receptor (selp-receptor) family.
DR GlyConnect; 1796; 6 N-Linked glycans (1 site).
DR GlyGen; Q9NT68; 17 sites, 6 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q9NT68; -.
DR PhosphoSitePlus; Q9NT68; -.
DR BioMuta; TENM2; -.
DR DMDM; 290457667; -.
DR EPD; Q9NT68; -.
DR jPOST; Q9NT68; -.
DR MassIVE; Q9NT68; -.
DR MaxQB; Q9NT68; -.
DR PaxDb; Q9NT68; -.
DR PeptideAtlas; Q9NT68; -.
DR PRIDE; Q9NT68; -.
DR ProteomicsDB; 82603; -. [Q9NT68-1]
DR ABCD; Q9NT68; 13 sequenced antibodies.
DR Antibodypedia; 49097; 7 antibodies from 5 providers.
DR DNASU; 57451; -.
DR Ensembl; ENST00000518659.5; ENSP00000429430.1; ENSG00000145934.16. [Q9NT68-1]
DR GeneID; 57451; -.
DR KEGG; hsa:57451; -.
DR MANE-Select; ENST00000518659.6; ENSP00000429430.1; NM_001395460.1; NP_001382389.1.
DR UCSC; uc031slx.2; human. [Q9NT68-1]
DR CTD; 57451; -.
DR DisGeNET; 57451; -.
DR GeneCards; TENM2; -.
DR HGNC; HGNC:29943; TENM2.
DR HPA; ENSG00000145934; Group enriched (brain, heart muscle).
DR MIM; 610119; gene.
DR neXtProt; NX_Q9NT68; -.
DR OpenTargets; ENSG00000145934; -.
DR VEuPathDB; HostDB:ENSG00000145934; -.
DR eggNOG; KOG1225; Eukaryota.
DR eggNOG; KOG4659; Eukaryota.
DR GeneTree; ENSGT01030000234566; -.
DR InParanoid; Q9NT68; -.
DR OMA; DSDGCPN; -.
DR OrthoDB; 7516at2759; -.
DR PhylomeDB; Q9NT68; -.
DR TreeFam; TF316833; -.
DR PathwayCommons; Q9NT68; -.
DR SignaLink; Q9NT68; -.
DR BioGRID-ORCS; 57451; 6 hits in 307 CRISPR screens.
DR ChiTaRS; TENM2; human.
DR GenomeRNAi; 57451; -.
DR Pharos; Q9NT68; Tbio.
DR PRO; PR:Q9NT68; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9NT68; protein.
DR Bgee; ENSG00000145934; Expressed in left ventricle myocardium and 155 other tissues.
DR ExpressionAtlas; Q9NT68; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050839; F:cell adhesion molecule binding; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IDA:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IDA:UniProtKB.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IDA:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0048666; P:neuron development; IBA:GO_Central.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:0098942; P:retrograde trans-synaptic signaling by trans-synaptic protein complex; IDA:SynGO.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 2.120.10.30; -; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR InterPro; IPR022385; Rhs_assc_core.
DR InterPro; IPR027689; Ten-2.
DR InterPro; IPR009471; Ten_N.
DR InterPro; IPR028916; Tox-GHH_dom.
DR InterPro; IPR006530; YD.
DR PANTHER; PTHR11219:SF8; PTHR11219:SF8; 1.
DR Pfam; PF06484; Ten_N; 1.
DR Pfam; PF15636; Tox-GHH; 1.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00179; EGF_CA; 2.
DR SUPFAM; SSF49464; SSF49464; 1.
DR SUPFAM; SSF50969; SSF50969; 1.
DR TIGRFAMs; TIGR03696; Rhs_assc_core; 1.
DR TIGRFAMs; TIGR01643; YD_repeat_2x; 1.
DR PROSITE; PS00022; EGF_1; 8.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS51361; TENEURIN_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Cell projection; Cleavage on pair of basic residues; Disulfide bond;
KW EGF-like domain; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Membrane; Nucleus; Phosphoprotein; Postsynaptic cell membrane;
KW Reference proteome; Repeat; Repressor; Signal-anchor; Synapse; Synaptosome;
KW Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..2774
FT /note="Teneurin-2"
FT /id="PRO_0000259501"
FT CHAIN 1..?
FT /note="Ten-2 intracellular domain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000421011"
FT CHAIN 529..2774
FT /note="Ten-2, soluble form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000421012"
FT TOPO_DOM 1..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..2774
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 1..375
FT /note="Teneurin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00694"
FT DOMAIN 575..603
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 598..634
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 636..668
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 669..701
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 702..735
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 738..766
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 769..797
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 808..841
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1272..1316
FT /note="NHL 1"
FT REPEAT 1342..1386
FT /note="NHL 2"
FT REPEAT 1401..1452
FT /note="NHL 3"
FT REPEAT 1474..1501
FT /note="NHL 4"
FT REPEAT 1530..1573
FT /note="NHL 5"
FT REPEAT 1583..1602
FT /note="YD 1"
FT REPEAT 1619..1639
FT /note="YD 2"
FT REPEAT 1682..1701
FT /note="YD 3"
FT REPEAT 1702..1724
FT /note="YD 4"
FT REPEAT 1895..1914
FT /note="YD 5"
FT REPEAT 1936..1954
FT /note="YD 6"
FT REPEAT 1955..1975
FT /note="YD 7"
FT REPEAT 1982..1999
FT /note="YD 8"
FT REPEAT 2000..2021
FT /note="YD 9"
FT REPEAT 2022..2039
FT /note="YD 10"
FT REPEAT 2042..2062
FT /note="YD 11"
FT REPEAT 2065..2085
FT /note="YD 12"
FT REPEAT 2093..2113
FT /note="YD 13"
FT REPEAT 2119..2136
FT /note="YD 14"
FT REPEAT 2137..2163
FT /note="YD 15"
FT REPEAT 2165..2178
FT /note="YD 16"
FT REPEAT 2179..2202
FT /note="YD 17"
FT REPEAT 2205..2225
FT /note="YD 18"
FT REPEAT 2226..2246
FT /note="YD 19"
FT REPEAT 2248..2268
FT /note="YD 20"
FT REPEAT 2280..2300
FT /note="YD 21"
FT REPEAT 2302..2322
FT /note="YD 22"
FT REPEAT 2348..2389
FT /note="YD 23"
FT REGION 111..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 528..529
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTS5"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHK6"
FT MOD_RES 155
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1K2"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1K2"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 925
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 948
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1712
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1773
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1807
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1892
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1993
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2648
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 576..586
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 580..591
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 593..602
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 611..622
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 624..633
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 640..651
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 645..656
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 658..667
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 672..683
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 677..688
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 690..699
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 710..723
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 725..734
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 739..749
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 743..754
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 756..765
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 770..780
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 774..785
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 787..796
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 810..820
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 814..829
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 831..840
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 1..121
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_045019"
FT VAR_SEQ 122..167
FT /note="GMSPEHAIRLWGRGIKSRRSSGLSSRENSALTLTDSDNENKSDDEN -> MV
FT SPPLLIISVAGTIECKPDHLLWRPGSTSPQSVSFLHGKVAMESL (in isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_045020"
FT VAR_SEQ 799..807
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_045021"
FT VAR_SEQ 1277..1283
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_045022"
FT VARIANT 728
FT /note="N -> S (in dbSNP:rs6862925)"
FT /id="VAR_060129"
FT VARIANT 1719
FT /note="V -> F (in dbSNP:rs11957063)"
FT /id="VAR_028946"
FT CONFLICT 2384
FT /note="L -> P (in Ref. 2; BAA86441)"
FT /evidence="ECO:0000305"
FT STRAND 1030..1033
FT /evidence="ECO:0007829|PDB:6VHH"
FT TURN 1044..1046
FT /evidence="ECO:0007829|PDB:6VHH"
FT TURN 1051..1054
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1055..1061
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1068..1072
FT /evidence="ECO:0007829|PDB:6VHH"
FT HELIX 1073..1075
FT /evidence="ECO:0007829|PDB:6CMX"
FT STRAND 1083..1086
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1096..1105
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1110..1115
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1121..1123
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1138..1153
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1158..1169
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1176..1178
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1186..1188
FT /evidence="ECO:0007829|PDB:6VHH"
FT TURN 1189..1192
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1193..1195
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1201..1203
FT /evidence="ECO:0007829|PDB:6VHH"
FT HELIX 1204..1206
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1210..1215
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1230..1232
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1242..1245
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1247..1249
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1251..1254
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1256..1262
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1266..1273
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1289..1293
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1295..1297
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1300..1304
FT /evidence="ECO:0007829|PDB:6VHH"
FT TURN 1305..1308
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1309..1314
FT /evidence="ECO:0007829|PDB:6VHH"
FT HELIX 1343..1345
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1359..1363
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1365..1367
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1369..1372
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1377..1380
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1382..1386
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1403..1405
FT /evidence="ECO:0007829|PDB:6VHH"
FT TURN 1424..1426
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1429..1432
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1434..1440
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1446..1451
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1476..1482
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1488..1493
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1495..1497
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1499..1504
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1508..1514
FT /evidence="ECO:0007829|PDB:6VHH"
FT TURN 1522..1524
FT /evidence="ECO:0007829|PDB:6VHH"
FT HELIX 1538..1540
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1546..1551
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1553..1555
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1557..1564
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1566..1571
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1583..1587
FT /evidence="ECO:0007829|PDB:6VHH"
FT TURN 1588..1591
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1592..1596
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1598..1600
FT /evidence="ECO:0007829|PDB:6CMX"
FT STRAND 1602..1610
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1613..1619
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1625..1629
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1635..1640
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1646..1650
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1656..1661
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1665..1671
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1676..1683
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1686..1692
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1700..1704
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1710..1714
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1720..1740
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1743..1750
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1752..1761
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1764..1771
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1776..1779
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1781..1783
FT /evidence="ECO:0007829|PDB:6CMX"
FT STRAND 1785..1793
FT /evidence="ECO:0007829|PDB:6VHH"
FT TURN 1794..1796
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1797..1809
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1811..1814
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1816..1828
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1831..1841
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1844..1852
FT /evidence="ECO:0007829|PDB:6VHH"
FT TURN 1853..1856
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1857..1862
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1868..1873
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1875..1877
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1879..1883
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1885..1887
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1891..1895
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1897..1899
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1901..1906
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1909..1915
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1917..1919
FT /evidence="ECO:0007829|PDB:6CMX"
FT STRAND 1921..1926
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1931..1935
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1942..1944
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1946..1948
FT /evidence="ECO:0007829|PDB:6CMX"
FT STRAND 1950..1955
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1957..1959
FT /evidence="ECO:0007829|PDB:6CMX"
FT STRAND 1961..1965
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1967..1969
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1971..1979
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1982..1988
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 1996..2000
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2002..2004
FT /evidence="ECO:0007829|PDB:6CMX"
FT STRAND 2006..2011
FT /evidence="ECO:0007829|PDB:6VHH"
FT TURN 2012..2015
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2016..2022
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2026..2033
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2036..2042
FT /evidence="ECO:0007829|PDB:6VHH"
FT TURN 2044..2046
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2049..2056
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2059..2068
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2071..2079
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2081..2083
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2087..2093
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2100..2107
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2115..2119
FT /evidence="ECO:0007829|PDB:6VHH"
FT TURN 2121..2123
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2126..2129
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2132..2137
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2140..2144
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2146..2154
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2156..2158
FT /evidence="ECO:0007829|PDB:6CMX"
FT STRAND 2160..2167
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2170..2179
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2185..2195
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2199..2205
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2207..2209
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2211..2216
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2219..2223
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2232..2235
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2244..2248
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2250..2252
FT /evidence="ECO:0007829|PDB:6CMX"
FT STRAND 2254..2257
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2260..2264
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2269..2273
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2276..2280
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2286..2291
FT /evidence="ECO:0007829|PDB:6VHH"
FT TURN 2292..2295
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2296..2302
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2304..2306
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2308..2313
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2318..2322
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2326..2328
FT /evidence="ECO:0007829|PDB:6CMX"
FT STRAND 2334..2337
FT /evidence="ECO:0007829|PDB:6VHH"
FT TURN 2338..2341
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2342..2348
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2350..2352
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2354..2359
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2360..2362
FT /evidence="ECO:0007829|PDB:6CMX"
FT STRAND 2364..2369
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2371..2373
FT /evidence="ECO:0007829|PDB:6CMX"
FT STRAND 2375..2380
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2381..2383
FT /evidence="ECO:0007829|PDB:6CMX"
FT STRAND 2385..2391
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2397..2401
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2403..2405
FT /evidence="ECO:0007829|PDB:6CMX"
FT HELIX 2411..2413
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2414..2417
FT /evidence="ECO:0007829|PDB:6VHH"
FT TURN 2418..2421
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2422..2425
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2428..2431
FT /evidence="ECO:0007829|PDB:6VHH"
FT TURN 2432..2435
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2436..2439
FT /evidence="ECO:0007829|PDB:6VHH"
FT HELIX 2442..2447
FT /evidence="ECO:0007829|PDB:6VHH"
FT TURN 2448..2450
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2457..2460
FT /evidence="ECO:0007829|PDB:6VHH"
FT HELIX 2461..2463
FT /evidence="ECO:0007829|PDB:6VHH"
FT HELIX 2472..2474
FT /evidence="ECO:0007829|PDB:6VHH"
FT HELIX 2480..2485
FT /evidence="ECO:0007829|PDB:6VHH"
FT HELIX 2490..2492
FT /evidence="ECO:0007829|PDB:6VHH"
FT HELIX 2509..2515
FT /evidence="ECO:0007829|PDB:6VHH"
FT TURN 2516..2518
FT /evidence="ECO:0007829|PDB:6CMX"
FT HELIX 2525..2537
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2542..2544
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2556..2558
FT /evidence="ECO:0007829|PDB:6CMX"
FT STRAND 2572..2585
FT /evidence="ECO:0007829|PDB:6VHH"
FT HELIX 2591..2600
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2611..2613
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2616..2625
FT /evidence="ECO:0007829|PDB:6VHH"
FT HELIX 2627..2634
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2637..2642
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2648..2652
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2655..2658
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2661..2664
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2666..2672
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2675..2681
FT /evidence="ECO:0007829|PDB:6VHH"
FT HELIX 2685..2687
FT /evidence="ECO:0007829|PDB:6VHH"
FT HELIX 2689..2717
FT /evidence="ECO:0007829|PDB:6VHH"
FT HELIX 2729..2735
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2736..2738
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2742..2748
FT /evidence="ECO:0007829|PDB:6VHH"
FT TURN 2750..2752
FT /evidence="ECO:0007829|PDB:6VHH"
FT HELIX 2754..2756
FT /evidence="ECO:0007829|PDB:6VHH"
FT HELIX 2760..2762
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 2763..2768
FT /evidence="ECO:0007829|PDB:6VHH"
SQ SEQUENCE 2774 AA; 307787 MW; C23DFD9BCD9D3F60 CRC64;
MDVKDRRHRS LTRGRCGKEC RYTSSSLDSE DCRVPTQKSY SSSETLKAYD HDSRMHYGNR
VTDLIHRESD EFPRQGTNFT LAELGICEPS PHRSGYCSDM GILHQGYSLS TGSDADSDTE
GGMSPEHAIR LWGRGIKSRR SSGLSSRENS ALTLTDSDNE NKSDDENGRP IPPTSSPSLL
PSAQLPSSHN PPPVSCQMPL LDSNTSHQIM DTNPDEEFSP NSYLLRACSG PQQASSSGPP
NHHSQSTLRP PLPPPHNHTL SHHHSSANSL NRNSLTNRRS QIHAPAPAPN DLATTPESVQ
LQDSWVLNSN VPLETRHFLF KTSSGSTPLF SSSSPGYPLT SGTVYTPPPR LLPRNTFSRK
AFKLKKPSKY CSWKCAALSA IAAALLLAIL LAYFIAMHLL GLNWQLQPAD GHTFNNGIRT
GLPGNDDVAT MPSGGKVPWS LKNSSIDSGE AEVGRRVTQE VPPGVFWRSQ IHISQPQFLK
FNISLGKDAL FGVYIRRGLP PSHAQYDFME RLDGKEKWSV VESPRERRSI QTLVQNEAVF
VQYLDVGLWH LAFYNDGKDK EMVSFNTVVL DSVQDCPRNC HGNGECVSGV CHCFPGFLGA
DCAKAACPVL CSGNGQYSKG TCQCYSGWKG AECDVPMNQC IDPSCGGHGS CIDGNCVCSA
GYKGEHCEEV DCLDPTCSSH GVCVNGECLC SPGWGGLNCE LARVQCPDQC SGHGTYLPDT
GLCSCDPNWM GPDCSVEVCS VDCGTHGVCI GGACRCEEGW TGAACDQRVC HPRCIEHGTC
KDGKCECREG WNGEHCTIGR QTAGTETDGC PDLCNGNGRC TLGQNSWQCV CQTGWRGPGC
NVAMETSCAD NKDNEGDGLV DCLDPDCCLQ SACQNSLLCR GSRDPLDIIQ QGQTDWPAVK
SFYDRIKLLA GKDSTHIIPG ENPFNSSLVS LIRGQVVTTD GTPLVGVNVS FVKYPKYGYT
ITRQDGTFDL IANGGASLTL HFERAPFMSQ ERTVWLPWNS FYAMDTLVMK TEENSIPSCD
LSGFVRPDPI IISSPLSTFF SAAPGQNPIV PETQVLHEEI ELPGSNVKLR YLSSRTAGYK
SLLKITMTQS TVPLNLIRVH LMVAVEGHLF QKSFQASPNL AYTFIWDKTD AYGQRVYGLS
DAVVSVGFEY ETCPSLILWE KRTALLQGFE LDPSNLGGWS LDKHHILNVK SGILHKGTGE
NQFLTQQPAI ITSIMGNGRR RSISCPSCNG LAEGNKLLAP VALAVGIDGS LYVGDFNYIR
RIFPSRNVTS ILELRNKEFK HSNNPAHKYY LAVDPVSGSL YVSDTNSRRI YRVKSLSGTK
DLAGNSEVVA GTGEQCLPFD EARCGDGGKA IDATLMSPRG IAVDKNGLMY FVDATMIRKV
DQNGIISTLL GSNDLTAVRP LSCDSSMDVA QVRLEWPTDL AVNPMDNSLY VLENNVILRI
TENHQVSIIA GRPMHCQVPG IDYSLSKLAI HSALESASAI AISHTGVLYI TETDEKKINR
LRQVTTNGEI CLLAGAASDC DCKNDVNCNC YSGDDAYATD AILNSPSSLA VAPDGTIYIA
DLGNIRIRAV SKNKPVLNAF NQYEAASPGE QELYVFNADG IHQYTVSLVT GEYLYNFTYS
TDNDVTELID NNGNSLKIRR DSSGMPRHLL MPDNQIITLT VGTNGGLKVV STQNLELGLM
TYDGNTGLLA TKSDETGWTT FYDYDHEGRL TNVTRPTGVV TSLHREMEKS ITIDIENSNR
DDDVTVITNL SSVEASYTVV QDQVRNSYQL CNNGTLRVMY ANGMGISFHS EPHVLAGTIT
PTIGRCNISL PMENGLNSIE WRLRKEQIKG KVTIFGRKLR VHGRNLLSID YDRNIRTEKI
YDDHRKFTLR IIYDQVGRPF LWLPSSGLAA VNVSYFFNGR LAGLQRGAMS ERTDIDKQGR
IVSRMFADGK VWSYSYLDKS MVLLLQSQRQ YIFEYDSSDR LLAVTMPSVA RHSMSTHTSI
GYIRNIYNPP ESNASVIFDY SDDGRILKTS FLGTGRQVFY KYGKLSKLSE IVYDSTAVTF
GYDETTGVLK MVNLQSGGFS CTIRYRKIGP LVDKQIYRFS EEGMVNARFD YTYHDNSFRI
ASIKPVISET PLPVDLYRYD EISGKVEHFG KFGVIYYDIN QIITTAVMTL SKHFDTHGRI
KEVQYEMFRS LMYWMTVQYD SMGRVIKREL KLGPYANTTK YTYDYDGDGQ LQSVAVNDRP
TWRYSYDLNG NLHLLNPGNS VRLMPLRYDL RDRITRLGDV QYKIDDDGYL CQRGSDIFEY
NSKGLLTRAY NKASGWSVQY RYDGVGRRAS YKTNLGHHLQ YFYSDLHNPT RITHVYNHSN
SEITSLYYDL QGHLFAMESS SGEEYYVASD NTGTPLAVFS INGLMIKQLQ YTAYGEIYYD
SNPDFQMVIG FHGGLYDPLT KLVHFTQRDY DVLAGRWTSP DYTMWKNVGK EPAPFNLYMF
KSNNPLSSEL DLKNYVTDVK SWLVMFGFQL SNIIPGFPRA KMYFVPPPYE LSESQASENG
QLITGVQQTT ERHNQAFMAL EGQVITKKLH ASIREKAGHW FATTTPIIGK GIMFAIKEGR
VTTGVSSIAS EDSRKVASVL NNAYYLDKMH YSIEGKDTHY FVKIGSADGD LVTLGTTIGR
KVLESGVNVT VSQPTLLVNG RTRRFTNIEF QYSTLLLSIR YGLTPDTLDE EKARVLDQAR
QRALGTAWAK EQQKARDGRE GSRLWTEGEK QQLLSTGRVQ GYEGYYVLPV EQYPELADSS
SNIQFLRQNE MGKR
