TEN2_MOUSE
ID TEN2_MOUSE Reviewed; 2764 AA.
AC Q9WTS5; Q5NBW7; Q5NBW8; Q80TJ0; Q9JLC0; Q9QYZ1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 145.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=10225957; DOI=10.1083/jcb.145.3.563;
RA Oohashi T., Zhou X.-H., Feng K., Richter B., Moergelin M., Perez M.T.,
RA Su W.D., Chiquet-Ehrismann R., Rauch U., Faessler R.;
RT "Mouse ten-m/Odz is a new family of dimeric type II transmembrane proteins
RT expressed in many tissues.";
RL J. Cell Biol. 145:563-577(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 572-799.
RX PubMed=10588872; DOI=10.1006/dbio.1999.9503;
RA Rubin B.P., Tucker R.P., Martin D., Chiquet-Ehrismann R.;
RT "Teneurins: a novel family of neuronal cell surface proteins in
RT vertebrates, homologous to the Drosophila pair-rule gene product Ten-m.";
RL Dev. Biol. 216:195-209(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1835-2764.
RX PubMed=10625539; DOI=10.1006/dbio.1999.9532;
RA Ben-Zur T., Feige E., Motro B., Wides R.;
RT "The mammalian Odz gene family: homologs of a Drosophila pair-rule gene
RT with expression implying distinct yet overlapping developmental roles.";
RL Dev. Biol. 217:107-120(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2512-2764.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [6]
RP HOMODIMERIZATION, AND HETERODIMERIZATION.
RX PubMed=12000766; DOI=10.1074/jbc.m203722200;
RA Feng K., Zhou X.H., Oohashi T., Morgelin M., Lustig A., Hirakawa S.,
RA Ninomiya Y., Engel J., Rauch U., Fassler R.;
RT "All four members of the Ten-m/Odz family of transmembrane proteins form
RT dimers.";
RL J. Biol. Chem. 277:26128-26135(2002).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12915301; DOI=10.1016/s1567-133x(03)00087-5;
RA Zhou X.H., Brandau O., Feng K., Oohashi T., Ninomiya Y., Rauch U.,
RA Fassler R.;
RT "The murine Ten-m/Odz genes show distinct but overlapping expression
RT patterns during development and in adult brain.";
RL Gene Expr. Patterns 3:397-405(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in neural development, regulating the establishment
CC of proper connectivity within the nervous system. Acts as a ligand of
CC the ADGRL1 receptor. Promotes the formation of filopodia and enlarged
CC growth cone in neuronal cells. Mediates axon guidance and homophilic
CC and heterophilic cell-cell adhesion. May function as a cellular signal
CC transducer (By similarity). {ECO:0000250}.
CC -!- FUNCTION: [Ten-2 intracellular domain]: Induces gene transcription
CC inhibition. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Heterodimer with either TENM1 or
CC TENM3. May also form heterodimer with TENM4.
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: [Ten-2 intracellular domain]: Nucleus, PML body
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the cortex, CA1, CA2, CA3, dentate
CC gyrus and granular layer of the hippocampus. Expressed in the Purkinje
CC cells and molecular layer of the cerebellum.
CC {ECO:0000269|PubMed:12915301}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the midbrain and spinal cord at 12.5
CC dpc. {ECO:0000269|PubMed:12915301}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB025411; BAA77397.1; -; mRNA.
DR EMBL; AL713956; CAI35933.1; -; Genomic_DNA.
DR EMBL; AL645912; CAI35933.1; JOINED; Genomic_DNA.
DR EMBL; AL713915; CAI35933.1; JOINED; Genomic_DNA.
DR EMBL; AL713919; CAI35933.1; JOINED; Genomic_DNA.
DR EMBL; BX000433; CAI35933.1; JOINED; Genomic_DNA.
DR EMBL; BX539311; CAI35933.1; JOINED; Genomic_DNA.
DR EMBL; AL713956; CAI35934.1; -; Genomic_DNA.
DR EMBL; AL645912; CAI35934.1; JOINED; Genomic_DNA.
DR EMBL; AL713915; CAI35934.1; JOINED; Genomic_DNA.
DR EMBL; AL713919; CAI35934.1; JOINED; Genomic_DNA.
DR EMBL; BX539311; CAI35934.1; JOINED; Genomic_DNA.
DR EMBL; BX000433; CAI35934.1; JOINED; Genomic_DNA.
DR EMBL; BX539311; CAI36037.1; -; Genomic_DNA.
DR EMBL; AL645912; CAI36037.1; JOINED; Genomic_DNA.
DR EMBL; AL713915; CAI36037.1; JOINED; Genomic_DNA.
DR EMBL; AL713919; CAI36037.1; JOINED; Genomic_DNA.
DR EMBL; AL713956; CAI36037.1; JOINED; Genomic_DNA.
DR EMBL; BX000433; CAI36037.1; JOINED; Genomic_DNA.
DR EMBL; BX539311; CAI36038.1; -; Genomic_DNA.
DR EMBL; AL645912; CAI36038.1; JOINED; Genomic_DNA.
DR EMBL; AL713915; CAI36038.1; JOINED; Genomic_DNA.
DR EMBL; AL713919; CAI36038.1; JOINED; Genomic_DNA.
DR EMBL; AL713956; CAI36038.1; JOINED; Genomic_DNA.
DR EMBL; BX000433; CAI36038.1; JOINED; Genomic_DNA.
DR EMBL; AL713919; CAI35941.1; -; Genomic_DNA.
DR EMBL; AL645912; CAI35941.1; JOINED; Genomic_DNA.
DR EMBL; AL713915; CAI35941.1; JOINED; Genomic_DNA.
DR EMBL; AL713956; CAI35941.1; JOINED; Genomic_DNA.
DR EMBL; BX000433; CAI35941.1; JOINED; Genomic_DNA.
DR EMBL; BX539311; CAI35941.1; JOINED; Genomic_DNA.
DR EMBL; AL713919; CAI35942.1; -; Genomic_DNA.
DR EMBL; AL645912; CAI35942.1; JOINED; Genomic_DNA.
DR EMBL; AL713915; CAI35942.1; JOINED; Genomic_DNA.
DR EMBL; AL713956; CAI35942.1; JOINED; Genomic_DNA.
DR EMBL; BX539311; CAI35942.1; JOINED; Genomic_DNA.
DR EMBL; BX000433; CAI35942.1; JOINED; Genomic_DNA.
DR EMBL; AL713915; CAI35944.1; -; Genomic_DNA.
DR EMBL; AL645912; CAI35944.1; JOINED; Genomic_DNA.
DR EMBL; AL713919; CAI35944.1; JOINED; Genomic_DNA.
DR EMBL; AL713956; CAI35944.1; JOINED; Genomic_DNA.
DR EMBL; BX000433; CAI35944.1; JOINED; Genomic_DNA.
DR EMBL; BX539311; CAI35944.1; JOINED; Genomic_DNA.
DR EMBL; AL713915; CAI35945.1; -; Genomic_DNA.
DR EMBL; BX539311; CAI35945.1; JOINED; Genomic_DNA.
DR EMBL; BX000433; CAI35945.1; JOINED; Genomic_DNA.
DR EMBL; AL713956; CAI35945.1; JOINED; Genomic_DNA.
DR EMBL; AL713919; CAI35945.1; JOINED; Genomic_DNA.
DR EMBL; AL645912; CAI35945.1; JOINED; Genomic_DNA.
DR EMBL; BX000433; CAI35946.1; -; Genomic_DNA.
DR EMBL; AL645912; CAI35946.1; JOINED; Genomic_DNA.
DR EMBL; AL713915; CAI35946.1; JOINED; Genomic_DNA.
DR EMBL; AL713919; CAI35946.1; JOINED; Genomic_DNA.
DR EMBL; AL713956; CAI35946.1; JOINED; Genomic_DNA.
DR EMBL; BX539311; CAI35946.1; JOINED; Genomic_DNA.
DR EMBL; BX000433; CAI35947.1; -; Genomic_DNA.
DR EMBL; AL645912; CAI35947.1; JOINED; Genomic_DNA.
DR EMBL; AL713919; CAI35947.1; JOINED; Genomic_DNA.
DR EMBL; AL713956; CAI35947.1; JOINED; Genomic_DNA.
DR EMBL; AL713915; CAI35947.1; JOINED; Genomic_DNA.
DR EMBL; BX539311; CAI35947.1; JOINED; Genomic_DNA.
DR EMBL; AL645912; CAI35083.1; -; Genomic_DNA.
DR EMBL; AL713915; CAI35083.1; JOINED; Genomic_DNA.
DR EMBL; AL713919; CAI35083.1; JOINED; Genomic_DNA.
DR EMBL; AL713956; CAI35083.1; JOINED; Genomic_DNA.
DR EMBL; BX000433; CAI35083.1; JOINED; Genomic_DNA.
DR EMBL; BX539311; CAI35083.1; JOINED; Genomic_DNA.
DR EMBL; AL645912; CAI35084.1; -; Genomic_DNA.
DR EMBL; AL713915; CAI35084.1; JOINED; Genomic_DNA.
DR EMBL; AL713919; CAI35084.1; JOINED; Genomic_DNA.
DR EMBL; AL713956; CAI35084.1; JOINED; Genomic_DNA.
DR EMBL; BX000433; CAI35084.1; JOINED; Genomic_DNA.
DR EMBL; BX539311; CAI35084.1; JOINED; Genomic_DNA.
DR EMBL; AJ245710; CAB57282.1; -; mRNA.
DR EMBL; AF195419; AAF28317.1; -; mRNA.
DR EMBL; AK122455; BAC65737.1; -; mRNA.
DR CCDS; CCDS24546.1; -.
DR SMR; Q9WTS5; -.
DR IntAct; Q9WTS5; 3.
DR MINT; Q9WTS5; -.
DR STRING; 10090.ENSMUSP00000052014; -.
DR GlyConnect; 2756; 10 N-Linked glycans (6 sites).
DR GlyGen; Q9WTS5; 15 sites, 10 N-linked glycans (6 sites).
DR iPTMnet; Q9WTS5; -.
DR PhosphoSitePlus; Q9WTS5; -.
DR EPD; Q9WTS5; -.
DR MaxQB; Q9WTS5; -.
DR PaxDb; Q9WTS5; -.
DR PRIDE; Q9WTS5; -.
DR ProteomicsDB; 263034; -.
DR MGI; MGI:1345184; Tenm2.
DR eggNOG; KOG1225; Eukaryota.
DR eggNOG; KOG4659; Eukaryota.
DR InParanoid; Q9WTS5; -.
DR PhylomeDB; Q9WTS5; -.
DR TreeFam; TF316833; -.
DR ChiTaRS; Tenm2; mouse.
DR PRO; PR:Q9WTS5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9WTS5; protein.
DR GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; ISS: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:0098890; C:extrinsic component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
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; ISS:MGI.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS: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:0050839; F:cell adhesion molecule binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; ISS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISS: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; ISS: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; ISO:MGI.
DR Gene3D; 2.120.10.30; -; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR000742; EGF-like_dom.
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 SUPFAM; SSF49464; SSF49464; 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; 4.
DR PROSITE; PS51361; TENEURIN_N; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Cell projection;
KW Cleavage on pair of basic residues; Disulfide bond; EGF-like domain;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Membrane; Nucleus;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Repeat;
KW Repressor; Synapse; Synaptosome; Transcription; Transcription regulation;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..2764
FT /note="Teneurin-2"
FT /id="PRO_0000259502"
FT CHAIN 1..?
FT /note="Ten-2 intracellular domain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000421013"
FT CHAIN 529..2764
FT /note="Ten-2, soluble form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000421014"
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..2764
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 737..765
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 768..796
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 798..831
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1262..1306
FT /note="NHL 1"
FT REPEAT 1332..1376
FT /note="NHL 2"
FT REPEAT 1391..1442
FT /note="NHL 3"
FT REPEAT 1464..1491
FT /note="NHL 4"
FT REPEAT 1520..1563
FT /note="NHL 5"
FT REPEAT 1573..1592
FT /note="YD 1"
FT REPEAT 1609..1629
FT /note="YD 2"
FT REPEAT 1672..1691
FT /note="YD 3"
FT REPEAT 1692..1714
FT /note="YD 4"
FT REPEAT 1885..1904
FT /note="YD 5"
FT REPEAT 1926..1944
FT /note="YD 6"
FT REPEAT 1945..1965
FT /note="YD 7"
FT REPEAT 1972..1989
FT /note="YD 8"
FT REPEAT 1990..2011
FT /note="YD 9"
FT REPEAT 2012..2029
FT /note="YD 10"
FT REPEAT 2032..2052
FT /note="YD 11"
FT REPEAT 2055..2075
FT /note="YD 12"
FT REPEAT 2083..2103
FT /note="YD 13"
FT REPEAT 2109..2126
FT /note="YD 14"
FT REPEAT 2127..2153
FT /note="YD 15"
FT REPEAT 2155..2168
FT /note="YD 16"
FT REPEAT 2169..2192
FT /note="YD 17"
FT REPEAT 2195..2215
FT /note="YD 18"
FT REPEAT 2216..2236
FT /note="YD 19"
FT REPEAT 2238..2258
FT /note="YD 20"
FT REPEAT 2270..2290
FT /note="YD 21"
FT REPEAT 2292..2312
FT /note="YD 22"
FT REPEAT 2338..2379
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 168..191
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:0007744|PubMed:21183079"
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 915
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 938
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1606
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1739
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1763
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1797
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1882
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1983
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2638
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 738..748
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 742..753
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 755..764
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 769..779
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 773..784
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 786..795
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 800..810
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 804..819
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 821..830
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 736
FT /note="V -> VE (in Ref. 2; CAI35934/CAI36038/CAI35942/
FT CAI35945/CAI35947/CAI35084 and 3; CAB57282)"
FT /evidence="ECO:0000305"
FT CONFLICT 2369
FT /note="Y -> F (in Ref. 2; CAI35083/CAI35084/CAI35933/
FT CAI35934/CAI35941/CAI35942/CAI35944/CAI35945/CAI35946/
FT CAI35947/CAI36037/CAI36038 and 4; AAF28317)"
FT /evidence="ECO:0000305"
FT CONFLICT 2690
FT /note="G -> R (in Ref. 2; CAI35083/CAI35084/CAI35933/
FT CAI35934/CAI35941/CAI35942/CAI35944/CAI35945/CAI35946/
FT CAI35947/CAI36037/CAI36038 and 5; BAC65737)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2764 AA; 306468 MW; 73BA3D916D0F0344 CRC64;
MDVKDRRHRS LTRGRCGKEC RYTSSSLDSE DCRVPTQKSY SSSETLKAYD HDSRMHYGNR
VTDLVHRESD EFSRQGTNFT LAELGICEPS PHRSGYCSDM GILHQGYSLS TGSDADSDTE
GGMSPEHAIR LWGRGIKSRR SSGLSSRENS ALTLTDSDNE NKSDDDNGRP IPPTSSSSLL
PSAQLPSSHN PPPVSCQMPL LDSNTSHQIM DTNPDEEFSP NSYLLRACSG PQQASSSGPP
NHHSQSTLRP PLPPPHNHTL SHHHSSANSL NRNSLTNRRS QIHAPAPAPN DLATTPESVQ
LQDSWVLNSN VPLETRHFLF KTSSGSTPLF SSSSPGYPLT SGTVYTPPPR LLPRNTFSRK
AFKLKKPSKY CSWKCAALSA IAAALLLAIL LAYFIAMHLL GLNWQLQPAD GHTFNNGVRT
GLPGNDDVAT VPSGGKVPWS LKNSSIDSGE AEVGRRVTQE VPPGVFWRSQ IHISQPQFLK
FNISLGKDAL FGVYIRRGLP PSHAQYDFME RLDGKEKWSV VESPRERRSI QTLVQNEAVF
VQYLDVGLWH LAFYNDGKDK EMVSFNTVVL DSVQDCPRNC HGNGECVSGL CHCFPGFLGA
DCAKAACPVL CSGNGQYSKG TCQCYSGWKG AECDVPMNQC IDPSCGGHGS CIDGNCVCAA
GYKGEHCEEV DCLDPTCSSH GVCVNGECLC SPGWGGLNCE LARVQCPDQC SGHGTYLPDS
GLCSCDPNWM GPDCSVVCSV DCGTHGVCIG GACRCEEGWT GAACDQRVCH PRCIEHGTCK
DGKCECREGW NGEHCTIDGC PDLCNGNGRC TLGQNSWQCV CQTGWRGPGC NVAMETSCAD
NKDNEGDGLV DCLDPDCCLQ SACQNSLLCR GSRDPLDIIQ QGQTDWPAVK SFYDRIKLLA
GKDSTHIIPG DNPFNSSLVS LIRGQVVTMD GTPLVGVNVS FVKYPKYGYT ITRQDGTFDL
IANGGSALTL HFERAPFMSQ ERTVWLPWNS FYAMDTLVMK TEENSIPSCD LSGFVRPDPI
IISSPLSTFF SASPASNPIV PETQVLHEEI ELPGTNVKLR YLSSRTAGYK SLLKITMTQS
TVPLNLIRVH LMVAVEGHLF QKSFQASPNL AYTFIWDKTD AYGQRVYGLS DAVVSVGFEY
ETCPSLILWE KRTALLQGFE LDPSNLGGWS LDKHHTLNVK SGILHKGTGE NQFLTQQPAI
ITSIMGNGRR RSISCPSCNG LAEGNKLLAP VALAVGIDGS LFVGDFNYIR RIFPSRNVTS
ILELRNKEFK HSNSPGHKYY LAVDPVTGSL YVSDTNSRRI YRVKSLSGAK DLAGNSEVVA
GTGEQCLPFD EARCGDGGKA VDATLMSPRG IAVDKNGLMY FVDATMIRKV DQNGIISTLL
GSNDLTAVRP LSCDSSMDVA QVRLEWPTDL AVNPMDNSLY VLENNVILRI TENHQVSIIA
GRPMHCQVPG IDYSLSKLAI HSALESASAI AISHTGVLYI TETDEKKINR LRQVTTNGEI
CLLAGAASDC DCKNDVNCIC YSGDDAYATD AILNSPSSLA VAPDGTIYIA DLGNIRIRAV
SKNKPVLNAF NQYEAASPGE QELYVFNADG IHQYTVSLVT GEYLYNFTYS ADNDVTELID
NNGNSLKIRR DSSGMPRHLL MPDNQIITLT VGTNGGLKAV STQNLELGLM TYDGNTGLLA
TKSDETGWTT FYDYDHEGRL TNVTRPTGVV TSLHREMEKS ITIDIENSNR DDDVTVITNL
SSVEASYTVV QDQVRNSYQL CNNGTLRVMY ANGMAVSFHS EPHVLAGTIT PTIGRCNISL
PMENGLNSIE WRLRKEQIKG KVTIFGRKLR VHGRNLLSID YDRNIRTEKI YDDHRKFTLR
IIYDQVGRPF LWLPSSGLAA VNVSYFFNGR LAGLQRGAMS ERTDIDKQGR IVSRMFADGK
VWSYSYLDKS MVLLLQSQRQ YIFEYDSSDR LHAVTMPSVA RHSMSTHTSI GYIRNIYNPP
ESNASVIFDY SDDGRILKTS FLGTGRQVFY KYGKLSKLSE IVYDSTAVTF GYDETTGVLK
MVNLQSGGFS CTIRYRKVGP LVDKQIYRFS EEGMINARFD YTYHDNSFRI ASIKPVISET
PLPVDLYRYD EISGKVEHFG KFGVIYYDIN QIITTAVMTL SKHFDTHGRI KEVQYEMFRS
LMYWMTVQYD SMGRVIKREL KLGPYANTTK YTYDYDGDGQ LQSVAVNDRP TWRYSYDLNG
NLHLLNPGNS ARLMPLRYDL RDRITRLGDV QYKIDDDGYL CQRGSDIFEY NSKGLLTRAY
NKASGWSVQY RYDGVGRRAS YKTNLGHHLQ YFYSDLHNPT RITHVYNHSN SEITSLYYDL
QGHLFAMESS SGEEYYVASD NTGTPLAVYS INGLMIKQLQ YTAYGEIYYD SNPDFQMVIG
FHGGLYDPLT KLVHFTQRDY DVLAGRWTSP DYTMWRNVGK EPAPFNLYMF KNNNPLSNEL
DLKNYVTDVK SWLVMFGFQL SNIIPGFPRA KMYFVPPPYE LSESQASENG QLITGVQQTT
ERHNQAFLAL EGQVITKKLH ASIREKAGHW FATTTPIIGK GIMFAIKEGR VTTGVSSIAS
EDSRKVASVL NNAYYLDKMH YSIEGKDTHY FVKIGAADGD LVTLGTTIGR KVLESGVNVT
VSQPTLLVNG RTRRFTNIEF QYSTLLLSIR YGLTPDTLDE EKARVLDQAG QRALGTAWAK
EQQKARDGRE GSRLWTEGEK QQLLSTGRVQ GYEGYYVLPV EQYPELADSS SNIQFLRQNE
MGKR
