GenomeNet

Database: UniProt
Entry: Q9NT68
LinkDB: Q9NT68
Original site: Q9NT68 
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   10-APR-2019, entry version 137.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA   Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA   Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA   Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA   Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA   Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA   Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA   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
RP   TISSUE 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
RT   from 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.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., 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,
RP   INTERACTION 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.,
RA   Tonevitsky A.G., 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
CC       establishment of proper connectivity within the nervous system.
CC       Promotes the formation of filopodia and enlarged growth cone in
CC       neuronal cells. Induces homophilic cell-cell adhesion (By
CC       similarity). May function as a cellular signal transducer.
CC       {ECO:0000250, 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
CC       membrane protein {ECO:0000250}. Endoplasmic reticulum
CC       {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell junction,
CC       synapse {ECO:0000250}. Cell projection, dendritic spine
CC       {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell
CC       projection, growth cone {ECO:0000250}. Cell junction, synapse,
CC       postsynaptic cell membrane {ECO:0000250}; Single-pass membrane
CC       protein {ECO:0000250}. Cell junction, synapse, synaptosome
CC       {ECO:0000250}. Note=Colocalizes with ADGRL1 across intercellular
CC       junctions. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane. Note=Colocalizes
CC       with ADGRL1 across intercellular junctions.
CC   -!- SUBCELLULAR LOCATION: Ten-2 intracellular domain: Nucleus, PML
CC       body {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
CC       organizer;
CC         IsoId=Q9NT68-2; Sequence=VSP_045019, VSP_045020, VSP_045021,
CC                                  VSP_045022;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart, followed by brain,
CC       liver, kidney and fetal brain and weakly expressed in lung and
CC       testis. No expression was detected in skeletal muscle, pancreas,
CC       spleen, ovary and fetal liver. {ECO:0000269|PubMed:10574461}.
CC   -!- DOMAIN: EGF-like domains 2 and 5 which have an odd number of
CC       cysteines might enable the formation of intermolecular disulfide
CC       bonds.
CC   -!- DOMAIN: Cytoplasmic proline-rich regions could serve as docking
CC       domains 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
CC       stimulates its proteolytic cleavage and release in the
CC       cytoplasmic. Is subjected to rapid degradation by the proteasome
CC       pathway (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC       {ECO:0000305}.
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   UniGene; Hs.631957; -.
DR   PDB; 6CMX; EM; 3.10 A; A=846-2774.
DR   PDBsum; 6CMX; -.
DR   ProteinModelPortal; Q9NT68; -.
DR   SMR; Q9NT68; -.
DR   IntAct; Q9NT68; 2.
DR   STRING; 9606.ENSP00000429430; -.
DR   GlyConnect; 1796; -.
DR   iPTMnet; Q9NT68; -.
DR   PhosphoSitePlus; Q9NT68; -.
DR   BioMuta; TENM2; -.
DR   DMDM; 290457667; -.
DR   EPD; Q9NT68; -.
DR   jPOST; Q9NT68; -.
DR   MaxQB; Q9NT68; -.
DR   PaxDb; Q9NT68; -.
DR   PeptideAtlas; Q9NT68; -.
DR   PRIDE; Q9NT68; -.
DR   ProteomicsDB; 82603; -.
DR   Ensembl; ENST00000518659; ENSP00000429430; ENSG00000145934. [Q9NT68-1]
DR   GeneID; 57451; -.
DR   KEGG; hsa:57451; -.
DR   UCSC; uc031slx.2; human. [Q9NT68-1]
DR   CTD; 57451; -.
DR   DisGeNET; 57451; -.
DR   EuPathDB; HostDB:ENSG00000145934.15; -.
DR   GeneCards; TENM2; -.
DR   HGNC; HGNC:29943; TENM2.
DR   HPA; HPA038018; -.
DR   HPA; HPA038420; -.
DR   HPA; HPA068691; -.
DR   MIM; 610119; gene.
DR   neXtProt; NX_Q9NT68; -.
DR   OpenTargets; ENSG00000145934; -.
DR   eggNOG; KOG1225; Eukaryota.
DR   eggNOG; KOG4659; Eukaryota.
DR   eggNOG; ENOG410XQQD; LUCA.
DR   GeneTree; ENSGT00950000182725; -.
DR   HOGENOM; HOG000231701; -.
DR   HOVERGEN; HBG080306; -.
DR   InParanoid; Q9NT68; -.
DR   OMA; LIKVHLM; -.
DR   OrthoDB; 7516at2759; -.
DR   PhylomeDB; Q9NT68; -.
DR   TreeFam; TF316833; -.
DR   ChiTaRS; TENM2; human.
DR   GenomeRNAi; 57451; -.
DR   PRO; PR:Q9NT68; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   Bgee; ENSG00000145934; Expressed in 153 organ(s), highest expression level in left ventricle myocardium.
DR   ExpressionAtlas; Q9NT68; baseline and differential.
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; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR011044; Quino_amine_DH_bsu.
DR   InterPro; IPR022385; Rhs_assc_core.
DR   InterPro; IPR027689; Ten-2/3.
DR   InterPro; IPR009471; Ten_N.
DR   InterPro; IPR028916; Tox-GHH_dom.
DR   InterPro; IPR006530; YD.
DR   PANTHER; PTHR11219:SF64; PTHR11219:SF64; 2.
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 junction;
KW   Cell membrane; Cell projection; Cleavage on pair of basic residues;
KW   Complete proteome; Disulfide bond; EGF-like domain;
KW   Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Membrane;
KW   Nucleus; Phosphoprotein; Polymorphism; Postsynaptic cell membrane;
KW   Reference proteome; Repeat; Repressor; Signal-anchor; Synapse;
KW   Synaptosome; Transcription; Transcription regulation; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   2774       Teneurin-2.
FT                                /FTId=PRO_0000259501.
FT   CHAIN         1      ?       Ten-2 intracellular domain.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000421011.
FT   CHAIN       529   2774       Ten-2, soluble form. {ECO:0000250}.
FT                                /FTId=PRO_0000421012.
FT   TOPO_DOM      1    379       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    380    400       Helical. {ECO:0000255}.
FT   TOPO_DOM    401   2774       Extracellular. {ECO:0000255}.
FT   DOMAIN        1    375       Teneurin N-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00694}.
FT   DOMAIN      575    603       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      598    634       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      636    668       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      669    701       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      702    735       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      738    766       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      769    797       EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      808    841       EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT     1272   1316       NHL 1.
FT   REPEAT     1342   1386       NHL 2.
FT   REPEAT     1401   1452       NHL 3.
FT   REPEAT     1474   1501       NHL 4.
FT   REPEAT     1530   1573       NHL 5.
FT   REPEAT     1583   1602       YD 1.
FT   REPEAT     1619   1639       YD 2.
FT   REPEAT     1682   1701       YD 3.
FT   REPEAT     1702   1724       YD 4.
FT   REPEAT     1895   1914       YD 5.
FT   REPEAT     1936   1954       YD 6.
FT   REPEAT     1955   1975       YD 7.
FT   REPEAT     1982   1999       YD 8.
FT   REPEAT     2000   2021       YD 9.
FT   REPEAT     2022   2039       YD 10.
FT   REPEAT     2042   2062       YD 11.
FT   REPEAT     2065   2085       YD 12.
FT   REPEAT     2093   2113       YD 13.
FT   REPEAT     2119   2136       YD 14.
FT   REPEAT     2137   2163       YD 15.
FT   REPEAT     2165   2178       YD 16.
FT   REPEAT     2179   2202       YD 17.
FT   REPEAT     2205   2225       YD 18.
FT   REPEAT     2226   2246       YD 19.
FT   REPEAT     2248   2268       YD 20.
FT   REPEAT     2280   2300       YD 21.
FT   REPEAT     2302   2322       YD 22.
FT   REPEAT     2348   2389       YD 23.
FT   COMPBIAS    331    334       Poly-Ser.
FT   SITE        528    529       Cleavage. {ECO:0000250}.
FT   MOD_RES      90     90       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9WTS5}.
FT   MOD_RES     124    124       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q3UHK6}.
FT   MOD_RES     155    155       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9R1K2}.
FT   MOD_RES     157    157       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9R1K2}.
FT   CARBOHYD    443    443       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    482    482       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    925    925       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    948    948       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1267   1267       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1616   1616       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1712   1712       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1749   1749       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1773   1773       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1807   1807       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1892   1892       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1993   1993       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2197   2197       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2337   2337       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2648   2648       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    576    586       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    580    591       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    593    602       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    611    622       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    624    633       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    640    651       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    645    656       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    658    667       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    672    683       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    677    688       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    690    699       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    710    723       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    725    734       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    739    749       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    743    754       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    756    765       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    770    780       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    774    785       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    787    796       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    810    820       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    814    829       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    831    840       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   VAR_SEQ       1    121       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_045019.
FT   VAR_SEQ     122    167       GMSPEHAIRLWGRGIKSRRSSGLSSRENSALTLTDSDNENK
FT                                SDDEN -> MVSPPLLIISVAGTIECKPDHLLWRPGSTSPQ
FT                                SVSFLHGKVAMESL (in isoform 2).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_045020.
FT   VAR_SEQ     799    807       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_045021.
FT   VAR_SEQ    1277   1283       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_045022.
FT   VARIANT     728    728       N -> S (in dbSNP:rs6862925).
FT                                /FTId=VAR_060129.
FT   VARIANT    1719   1719       V -> F (in dbSNP:rs11957063).
FT                                /FTId=VAR_028946.
FT   CONFLICT   2384   2384       L -> P (in Ref. 2; BAA86441).
FT                                {ECO:0000305}.
FT   STRAND     1030   1033       {ECO:0000244|PDB:6CMX}.
FT   TURN       1044   1046       {ECO:0000244|PDB:6CMX}.
FT   TURN       1051   1054       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1055   1061       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1068   1072       {ECO:0000244|PDB:6CMX}.
FT   HELIX      1073   1075       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1083   1088       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1098   1100       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1103   1107       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1118   1123       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1138   1147       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1160   1167       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1176   1178       {ECO:0000244|PDB:6CMX}.
FT   TURN       1189   1191       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1583   1587       {ECO:0000244|PDB:6CMX}.
FT   TURN       1588   1591       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1592   1596       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1598   1600       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1602   1607       {ECO:0000244|PDB:6CMX}.
FT   TURN       1608   1610       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1613   1619       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1625   1630       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1633   1637       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1648   1650       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1656   1660       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1663   1666       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1669   1671       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1673   1679       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1681   1686       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1689   1691       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1728   1730       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1737   1739       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1745   1750       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1752   1763       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1781   1783       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1785   1788       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1803   1809       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1818   1828       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1831   1841       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1844   1852       {ECO:0000244|PDB:6CMX}.
FT   TURN       1853   1855       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1860   1862       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1868   1870       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1875   1877       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1883   1885       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1897   1899       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1903   1906       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1909   1915       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1917   1919       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1921   1929       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1933   1935       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1942   1944       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1946   1948       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1950   1955       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1957   1959       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1961   1965       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1974   1979       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1982   1987       {ECO:0000244|PDB:6CMX}.
FT   STRAND     1996   2000       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2002   2004       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2006   2011       {ECO:0000244|PDB:6CMX}.
FT   TURN       2012   2015       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2016   2022       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2028   2033       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2036   2042       {ECO:0000244|PDB:6CMX}.
FT   TURN       2044   2046       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2048   2056       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2062   2076       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2081   2084       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2087   2093       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2100   2103       {ECO:0000244|PDB:6CMX}.
FT   TURN       2121   2124       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2126   2129       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2132   2137       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2140   2144       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2149   2154       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2156   2158       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2160   2164       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2174   2180       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2183   2191       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2193   2195       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2199   2205       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2211   2218       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2220   2223       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2250   2252       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2255   2257       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2289   2294       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2297   2302       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2304   2306       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2308   2313       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2318   2320       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2326   2328       {ECO:0000244|PDB:6CMX}.
FT   TURN       2338   2341       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2345   2348       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2354   2358       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2360   2362       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2365   2369       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2371   2373       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2375   2379       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2381   2383       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2385   2387       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2390   2392       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2395   2399       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2403   2405       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2413   2416       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2418   2420       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2423   2425       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2432   2436       {ECO:0000244|PDB:6CMX}.
FT   HELIX      2445   2448       {ECO:0000244|PDB:6CMX}.
FT   HELIX      2461   2463       {ECO:0000244|PDB:6CMX}.
FT   HELIX      2472   2474       {ECO:0000244|PDB:6CMX}.
FT   HELIX      2479   2485       {ECO:0000244|PDB:6CMX}.
FT   TURN       2490   2493       {ECO:0000244|PDB:6CMX}.
FT   HELIX      2509   2515       {ECO:0000244|PDB:6CMX}.
FT   TURN       2516   2518       {ECO:0000244|PDB:6CMX}.
FT   HELIX      2525   2537       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2556   2558       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2575   2582       {ECO:0000244|PDB:6CMX}.
FT   HELIX      2591   2600       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2611   2613       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2616   2618       {ECO:0000244|PDB:6CMX}.
FT   HELIX      2686   2716       {ECO:0000244|PDB:6CMX}.
FT   TURN       2727   2729       {ECO:0000244|PDB:6CMX}.
FT   HELIX      2730   2735       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2736   2738       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2744   2748       {ECO:0000244|PDB:6CMX}.
FT   TURN       2750   2752       {ECO:0000244|PDB:6CMX}.
FT   TURN       2755   2758       {ECO:0000244|PDB:6CMX}.
FT   STRAND     2762   2765       {ECO:0000244|PDB:6CMX}.
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
//
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