TEN4_MOUSE
ID TEN4_MOUSE Reviewed; 2771 AA.
AC Q3UHK6; O70465; Q3TSI0; Q3UH52; Q80TF5; Q9WTS7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Teneurin-4;
DE Short=Ten-4;
DE AltName: Full=Downstream of CHOP4;
DE AltName: Full=Protein Odd Oz/ten-m homolog 4;
DE AltName: Full=Tenascin-M4;
DE Short=Ten-m4;
DE AltName: Full=Teneurin transmembrane protein 4;
GN Name=Tenm4; Synonyms=Doc4, Kiaa1302, Odz4, Tnm4;
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] (ISOFORM 2).
RC STRAIN=NIH Swiss;
RX PubMed=9649432; DOI=10.1093/emboj/17.13.3619;
RA Wang X.-Z., Kuroda M., Sok J., Batchvarova N., Kimmel R., Chung P.,
RA Zinszner H., Ron D.;
RT "Identification of novel stress-induced genes downstream of chop.";
RL EMBO J. 17:3619-3630(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Muellerian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1574-2771.
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 [5]
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 [6]
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 [7]
RP FUNCTION IN GASTRULATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=15489520; DOI=10.1534/genetics.104.034967;
RA Lossie A.C., Nakamura H., Thomas S.E., Justice M.J.;
RT "Mutation of l7Rn3 shows that Odz4 is required for mouse gastrulation.";
RL Genetics 169:285-299(2005).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1707 AND ASN-2190.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND THR-178, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Brown adipose tissue;
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).
RN [10]
RP FUNCTION IN OLIGODENDROCYTE DIFFERENTIATION, SUBCELLULAR LOCATION,
RP DISRUPTION PHENOTYPE, INDUCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=22915103; DOI=10.1523/jneurosci.2045-11.2012;
RA Suzuki N., Fukushi M., Kosaki K., Doyle A.D., de Vega S., Yoshizaki K.,
RA Akazawa C., Arikawa-Hirasawa E., Yamada Y.;
RT "Teneurin-4 is a novel regulator of oligodendrocyte differentiation and
RT myelination of small-diameter axons in the CNS.";
RL J. Neurosci. 32:11586-11599(2012).
CC -!- FUNCTION: Involved in neural development, regulating the establishment
CC of proper connectivity within the nervous system. Plays a role in the
CC establishment of the anterior-posterior axis during gastrulation.
CC Regulates the differentiation and cellular process formation of
CC oligodendrocytes and myelination of small-diameter axons in the central
CC nervous system (CNS). Promotes activation of focal adhesion kinase. May
CC function as a cellular signal transducer. {ECO:0000269|PubMed:15489520,
CC ECO:0000269|PubMed:22915103}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. May also form heterodimer with
CC either TENM1 or TENM2 or TENM3.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6N022};
CC Single-pass membrane protein {ECO:0000255}. Cell projection
CC {ECO:0000269|PubMed:22915103}. Nucleus {ECO:0000269|PubMed:22915103}.
CC Cytoplasm {ECO:0000269|PubMed:22915103}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional mRNAs also exist. Tissue-specific expression of
CC isoforms was observed throughout embryogenesis and in the brain and
CC ovary adult tissues.;
CC Name=1;
CC IsoId=Q3UHK6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UHK6-2; Sequence=VSP_021405, VSP_021407, VSP_021408;
CC Name=3;
CC IsoId=Q3UHK6-3; Sequence=VSP_021404, VSP_021405, VSP_021406;
CC Name=4;
CC IsoId=Q3UHK6-4; Sequence=VSP_021404;
CC -!- TISSUE SPECIFICITY: Expressed in brain and spinal cord (at protein
CC level). Expressed in neurons and oligodendrocytes of the spinal cord.
CC Expressed weakly in kidney, lung and spleen. Expressed in the cortex,
CC CA1, CA2 and CA3 of the hippocampus. Expressed in the white matter,
CC Purkinje cells and molecular layer of the cerebellum.
CC {ECO:0000269|PubMed:12915301, ECO:0000269|PubMed:15489520,
CC ECO:0000269|PubMed:22915103}.
CC -!- DEVELOPMENTAL STAGE: Expressed in spinal cord at 18 dpc (at protein
CC level). Expressed in the epiblast and extraembryonic regions as early
CC as 6.5 dpc. Expressed in the neural plate and extraembryonic tissues at
CC 7.5 dpc. Expressed in the forebrain, mid/hindbrain junction, somites
CC and tail bud at 8.5 dpc. Expressed in the tail bud and limbs at 11.5
CC dpc. Expressed in the diencephalon and midbrain at 12.5 dpc.
CC {ECO:0000269|PubMed:12915301, ECO:0000269|PubMed:15489520,
CC ECO:0000269|PubMed:22915103}.
CC -!- INDUCTION: Up-regulated during oligodendrocyte differentiation.
CC {ECO:0000269|PubMed:22915103}.
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 -!- DISRUPTION PHENOTYPE: Mice show tremors and hypomyelination in the
CC central nervous system (CNS), particularly in the spinal cord, but not
CC in the sciatic nerve of the peripheral nervous system (PNS).
CC Differentiation of oligodendrocytes is prevented in the spinal cord.
CC {ECO:0000269|PubMed:22915103}.
CC -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC {ECO:0000305}.
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DR EMBL; AF059485; AAC31807.1; -; mRNA.
DR EMBL; AB025413; BAA77399.1; -; mRNA.
DR EMBL; AK147579; BAE28005.1; -; mRNA.
DR EMBL; AK147329; BAE27851.1; -; mRNA.
DR EMBL; AK162046; BAE36695.1; -; mRNA.
DR EMBL; AK122490; BAC65772.1; -; mRNA.
DR CCDS; CCDS40024.1; -. [Q3UHK6-4]
DR CCDS; CCDS80753.1; -. [Q3UHK6-3]
DR CCDS; CCDS80754.1; -. [Q3UHK6-2]
DR PIR; T14271; T14271.
DR RefSeq; NP_001297689.1; NM_001310760.1. [Q3UHK6-3]
DR RefSeq; NP_001297691.1; NM_001310762.1. [Q3UHK6-2]
DR RefSeq; NP_035988.2; NM_011858.4. [Q3UHK6-4]
DR RefSeq; XP_017177717.1; XM_017322228.1.
DR SMR; Q3UHK6; -.
DR BioGRID; 204827; 3.
DR IntAct; Q3UHK6; 5.
DR MINT; Q3UHK6; -.
DR STRING; 10090.ENSMUSP00000102783; -.
DR GlyConnect; 2432; 3 N-Linked glycans (4 sites). [Q3UHK6-2]
DR GlyGen; Q3UHK6; 12 sites.
DR iPTMnet; Q3UHK6; -.
DR PhosphoSitePlus; Q3UHK6; -.
DR SwissPalm; Q3UHK6; -.
DR jPOST; Q3UHK6; -.
DR MaxQB; Q3UHK6; -.
DR PaxDb; Q3UHK6; -.
DR PeptideAtlas; Q3UHK6; -.
DR PRIDE; Q3UHK6; -.
DR ProteomicsDB; 258993; -. [Q3UHK6-1]
DR ProteomicsDB; 258994; -. [Q3UHK6-2]
DR ProteomicsDB; 258995; -. [Q3UHK6-3]
DR ProteomicsDB; 258996; -. [Q3UHK6-4]
DR Antibodypedia; 67208; 12 antibodies from 6 providers.
DR DNASU; 23966; -.
DR Ensembl; ENSMUST00000107162; ENSMUSP00000102780; ENSMUSG00000048078. [Q3UHK6-2]
DR Ensembl; ENSMUST00000107165; ENSMUSP00000102783; ENSMUSG00000048078. [Q3UHK6-3]
DR Ensembl; ENSMUST00000107166; ENSMUSP00000102784; ENSMUSG00000048078. [Q3UHK6-4]
DR GeneID; 23966; -.
DR KEGG; mmu:23966; -.
DR UCSC; uc009iio.1; mouse. [Q3UHK6-4]
DR UCSC; uc009iip.1; mouse. [Q3UHK6-3]
DR UCSC; uc009iiq.1; mouse. [Q3UHK6-2]
DR CTD; 26011; -.
DR MGI; MGI:2447063; Tenm4.
DR VEuPathDB; HostDB:ENSMUSG00000048078; -.
DR eggNOG; KOG4659; Eukaryota.
DR GeneTree; ENSGT01030000234566; -.
DR HOGENOM; CLU_000229_0_0_1; -.
DR InParanoid; Q3UHK6; -.
DR OMA; HWTQSAP; -.
DR PhylomeDB; Q3UHK6; -.
DR TreeFam; TF316833; -.
DR BioGRID-ORCS; 23966; 0 hits in 56 CRISPR screens.
DR ChiTaRS; Tenm4; mouse.
DR PRO; PR:Q3UHK6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3UHK6; protein.
DR Bgee; ENSMUSG00000048078; Expressed in floor plate of midbrain and 222 other tissues.
DR ExpressionAtlas; Q3UHK6; baseline and differential.
DR Genevisible; Q3UHK6; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0060912; P:cardiac cell fate specification; IMP:MGI.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IMP:MGI.
DR GO; GO:0032289; P:central nervous system myelin formation; IMP:UniProtKB.
DR GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0048666; P:neuron development; ISS:UniProtKB.
DR GO; GO:2000543; P:positive regulation of gastrulation; IMP:UniProtKB.
DR GO; GO:0031643; P:positive regulation of myelination; IMP:UniProtKB.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0031641; P:regulation of myelination; ISS:UniProtKB.
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; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR022385; Rhs_assc_core.
DR InterPro; IPR031325; RHS_repeat.
DR InterPro; IPR027691; Ten-3/4.
DR InterPro; IPR009471; Ten_N.
DR InterPro; IPR028916; Tox-GHH_dom.
DR InterPro; IPR006530; YD.
DR PANTHER; PTHR11219:SF65; PTHR11219:SF65; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF05593; RHS_repeat; 1.
DR Pfam; PF06484; Ten_N; 2.
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; 5.
DR PROSITE; PS51361; TENEURIN_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cytoplasm;
KW Developmental protein; Differentiation; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..2771
FT /note="Teneurin-4"
FT /id="PRO_0000259509"
FT TOPO_DOM 1..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..2771
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 1..341
FT /note="Teneurin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00694"
FT DOMAIN 564..595
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 596..626
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 628..660
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 661..692
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 694..727
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 728..759
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 760..789
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 790..833
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1218..1261
FT /note="NHL 1"
FT REPEAT 1266..1310
FT /note="NHL 2"
FT REPEAT 1336..1380
FT /note="NHL 3"
FT REPEAT 1395..1446
FT /note="NHL 4"
FT REPEAT 1525..1568
FT /note="NHL 5"
FT REPEAT 1578..1597
FT /note="YD 1"
FT REPEAT 1614..1634
FT /note="YD 2"
FT REPEAT 1677..1696
FT /note="YD 3"
FT REPEAT 1697..1719
FT /note="YD 4"
FT REPEAT 1889..1908
FT /note="YD 5"
FT REPEAT 1930..1948
FT /note="YD 6"
FT REPEAT 1949..1969
FT /note="YD 7"
FT REPEAT 1976..1993
FT /note="YD 8"
FT REPEAT 1994..2015
FT /note="YD 9"
FT REPEAT 2016..2033
FT /note="YD 10"
FT REPEAT 2036..2056
FT /note="YD 11"
FT REPEAT 2059..2079
FT /note="YD 12"
FT REPEAT 2087..2106
FT /note="YD 13"
FT REPEAT 2112..2129
FT /note="YD 14"
FT REPEAT 2130..2156
FT /note="YD 15"
FT REPEAT 2158..2171
FT /note="YD 16"
FT REPEAT 2172..2195
FT /note="YD 17"
FT REPEAT 2198..2218
FT /note="YD 18"
FT REPEAT 2219..2239
FT /note="YD 19"
FT REPEAT 2241..2261
FT /note="YD 20"
FT REPEAT 2273..2293
FT /note="YD 21"
FT REPEAT 2295..2315
FT /note="YD 22"
FT REPEAT 2341..2382
FT /note="YD 23"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 942
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1611
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1707
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 1743
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1801
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1886
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1987
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 2330
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 568..578
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 572..583
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 585..594
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 603..614
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 616..625
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 632..643
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 637..648
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 650..659
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 664..675
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 669..680
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 682..691
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 702..715
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 717..726
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 731..741
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 735..746
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 748..757
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 762..772
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 766..777
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 779..788
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 802..812
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 806..821
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 823..832
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 1
FT /note="M -> MEPDHSALSAARAQFVDVEEREPEAM (in isoform 3 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021404"
FT VAR_SEQ 164
FT /note="T -> TGAPLHCSSASSTPIEQSPSPPPSPPANESQRRLLGNGVAQPTPDSD
FT SEEEFVPNSFLVKSGSASLGVAAN (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9649432"
FT /id="VSP_021405"
FT VAR_SEQ 251..283
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021406"
FT VAR_SEQ 791..799
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9649432"
FT /id="VSP_021407"
FT VAR_SEQ 1269..1275
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9649432"
FT /id="VSP_021408"
FT CONFLICT 136..137
FT /note="TR -> EK (in Ref. 3; BAE36695)"
FT /evidence="ECO:0000305"
FT CONFLICT 152..164
FT /note="LTLTDTEHENTET -> EKSGSASLGVAAN (in Ref. 3;
FT BAE36695)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="L -> V (in Ref. 1; AAC31807)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="N -> K (in Ref. 1; AAC31807)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="L -> V (in Ref. 1; AAC31807)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="L -> W (in Ref. 1; AAC31807)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="L -> F (in Ref. 1; AAC31807)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="H -> R (in Ref. 1; AAC31807)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="L -> F (in Ref. 1; AAC31807)"
FT /evidence="ECO:0000305"
FT CONFLICT 422..429
FT /note="KPSSLFPE -> RVAALSVL (in Ref. 3; BAE36695)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="F -> L (in Ref. 1; AAC31807)"
FT /evidence="ECO:0000305"
FT CONFLICT 780
FT /note="S -> T (in Ref. 1; AAC31807)"
FT /evidence="ECO:0000305"
FT CONFLICT 895
FT /note="S -> P (in Ref. 2; BAA77399)"
FT /evidence="ECO:0000305"
FT CONFLICT 1013
FT /note="C -> R (in Ref. 1; AAC31807)"
FT /evidence="ECO:0000305"
FT CONFLICT 1039
FT /note="E -> G (in Ref. 3; BAE28005)"
FT /evidence="ECO:0000305"
FT CONFLICT 1077
FT /note="L -> V (in Ref. 1; AAC31807)"
FT /evidence="ECO:0000305"
FT CONFLICT 1133
FT /note="L -> F (in Ref. 2; BAA77399)"
FT /evidence="ECO:0000305"
FT CONFLICT 1457
FT /note="H -> Q (in Ref. 1; AAC31807)"
FT /evidence="ECO:0000305"
FT CONFLICT 1743
FT /note="N -> H (in Ref. 1; AAC31807)"
FT /evidence="ECO:0000305"
FT CONFLICT 1746
FT /note="A -> G (in Ref. 1; AAC31807)"
FT /evidence="ECO:0000305"
FT CONFLICT 1831
FT /note="R -> P (in Ref. 1; AAC31807)"
FT /evidence="ECO:0000305"
FT CONFLICT 1875
FT /note="L -> F (in Ref. 1; AAC31807)"
FT /evidence="ECO:0000305"
FT CONFLICT 1952
FT /note="N -> D (in Ref. 3; BAE28005)"
FT /evidence="ECO:0000305"
FT CONFLICT 2144
FT /note="T -> S (in Ref. 1; AAC31807)"
FT /evidence="ECO:0000305"
FT CONFLICT 2160
FT /note="I -> T (in Ref. 1; AAC31807)"
FT /evidence="ECO:0000305"
FT CONFLICT 2256
FT /note="K -> R (in Ref. 3; BAE28005)"
FT /evidence="ECO:0000305"
FT CONFLICT 2262
FT /note="F -> S (in Ref. 1; AAC31807)"
FT /evidence="ECO:0000305"
FT CONFLICT 2330
FT /note="N -> S (in Ref. 1; AAC31807)"
FT /evidence="ECO:0000305"
FT CONFLICT 2657
FT /note="V -> M (in Ref. 1; AAC31807, 2; BAA77399 and 4;
FT BAC65772)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2771 AA; 308425 MW; 15EF31E25A171FD0 CRC64;
MDVKERKPYR SLTRRRDAER RYTSSSADSE EGKGPQKSYS SSETLKAYDQ DARLAYGSRV
KDMVPQEAEE FCRTGTNFTL RELGLGEMTP PHGTLYRTDI GLPHCGYSMG ASSDADLEAD
TVLSPEHPVR LWGRSTRSGR SSCLSSRANS NLTLTDTEHE NTETDHPSSL QNHPRLRTPP
PPLPHAHTPN QHHAASINSL NRGNFTPRSN PSPAPTDHSL SGEPPAGSAQ EPTHAQDNWL
LNSNIPLETR NLGKQPFLGT LQDNLIEMDI LSASRHDGAY SDGHFLFKPG GTSPLFCTTS
PGYPLTSSTV YSPPPRPLPR STFSRPAFNL KKPSKYCNWK CAALSAILIS ATLVILLAYF
VAMHLFGLNW HLQPMEGQMQ MYEITEDTAS SWPVPTDVSL YPSGGTGLET PDRKGKGAAE
GKPSSLFPED SFIDSGEIDV GRRASQKIPP GTFWRSQVFI DHPVHLKFNV SLGKAALVGI
YGRKGLPPSH TQFDFVELLD GRRLLTQEAR SLEGPQRQSR GPVPPSSHET GFIQYLDSGI
WHLAFYNDGK ESEVVSFLTT AIESVDNCPS NCYGNGDCIS GTCHCFLGFL GPDCGRASCP
VLCSGNGQYM KGRCLCHSGW KGAECDVPTN QCIDVACSSH GTCIMGTCIC NPGYKGESCE
EVDCMDPTCS SRGVCVRGEC HCSVGWGGTN CETPRATCLD QCSGHGTFLP DTGLCNCDPS
WTGHDCSIEI CAADCGGHGV CVGGTCRCED GWMGAACDQR ACHPRCAEHG TCRDGKCECS
PGWNGEHCTI AHYLDRVVKE GCPGLCNGNG RCTLDLNGWH CVCQLGWRGT GCDTSMETGC
GDGKDNDGDG LVDCMDPDCC LQPLCHVNPL CLGSPDPLDI IQETQAPVSQ QNLNSFYDRI
KFLVGRDSTH SIPGENPFDG GHACVIRGQV MTSDGTPLVG VNISFINNPL FGYTISRQDG
SFDLVTNGGI SIILRFERAP FITQEHTLWL PWDRFFVMET IVMRHEENEI PSCDLSNFAR
PNPVVSPSPL TSFASSCAEK GPIVPEIQAL QEEIVIAGCK MRLSYLSSRT PGYKSVLRIS
LTHPTIPFNL MKVHLMVAVE GRLFRKWFAA APDLSYYFIW DKTDVYNQKV FGLSEAFVSV
GYEYESCPDL ILWEKRTAVL QGYEIDASKL GGWSLDKHHA LNIQSGILHK GNGENQFVSQ
QPPVIGSIMG NGRRRSISCP SCNGLADGNK LLAPVALTCG SDGSLYVGDF NYIRRIFPSG
NVTNILEMRN KDFRHSHSPA HKYYLATDPM SGAVFLSDTN SRRVFKVKST TVVKDLVKNS
EVVAGTGDQC LPFDDTRCGD GGKATEATLT NPRGITVDKF GLIYFVDGTM IRRVDQNGII
STLLGSNDLT SARPLSCDSV MEISQVRLEW PTDLAINPMD NSLYVLDNNV VLQISENHQV
RIVAGRPMHC QVPGIDHFLL SKVAIHATLE SATALAVSHN GVLYIAETDE KKINRIRQVT
TSGEISLVAG APSGCDCKND ANCDCFSGDD GYAKDAKLNT PSSLAVCADG ELYVADLGNI
RIRFIRKNKP FLNTQNMYEL SSPIDQELYL FDTSGKHLYT QSLPTGDYLY NFTYTGDGDI
THITDNNGNM VNVRRDSTGM PLWLVVPDGQ VYWVTMGTNS ALRSVTTQGH ELAMMTYHGN
SGLLATKSNE NGWTTFYEYD SFGRLTNVTF PTGQVSSFRS DTDSSVHVQV ETSSKDDVTI
TTNLSASGAF YTLLQDQVRN SYYIGADGSL RLLLANGMEV ALQTEPHLLA GTVNPTVGKR
NVTLPIDNGL NLVEWRQRKE QARGQVTVFG RRLRVHNRNL LSLDFDRVTR TEKIYDDHRK
FTLRILYDQA GRPSLWSPSS RLNGVNVTYS PGGHIAGIQR GIMSERMEYD QAGRITSRIF
ADGKMWSYTY LEKSMVLHLH SQRQYIFEFD KNDRLSSVTM PNVARQTLET IRSVGYYRNI
YQPPEGNASV IQDFTEDGHL LHTFYLGTGR RVIYKYGKLS KLAETLYDTT KVSFTYDETA
GMLKTVNLQN EGFTCTIRYR QIGPLIDRQI FRFTEEGMVN ARFDYNYDNS FRVTSMQAVI
NETPLPIDLY RYDDVSGKTE QFGKFGVIYY DINQIITTAV MTHTKHFDAY GRMKEVQYEI
FRSLMYWMTV QYDNMGRVVK KELKVGPYAN TTRYSYEYDA DGQLQTVSIN DKPLWRYSYD
LNGNLHLLSP GNSARLTPLR YDLRDRITRL GDVQYKMDED GFLRQRGGDV FEYNSAGLLI
KAYNRASGWS VRYRYDGLGR RVSSKSSHSH HLQFFYADLT NPTKVTHLYN HSSSEITSLY
YDLQGHLFAM ELSSGDEFYI ACDNIGTPLA VFSGTGLMIK QILYTAYGEI YMDTNPNFQI
IIGYHGGLYD PLTKLVHMGR RDYDVLAGRW TSPDHELWKR LSSNSIVPFH LYMFKNNNPI
SNSQDIKCFM TDVNSWLLTF GFQLHNVIPG YPKPDTDAME PSYELVHTQM KTQEWDNSKS
ILGVQCEVQK QLKAFVTLER FDQLYGSTIT SCQQAPETKK FASSGSIFGK GVKFALKDGR
VTTDIISVAN EDGRRIAAIL NNAHYLENLH FTIDGVDTHY FVKPGPSEGD LAILGLSGGR
RTLENGVNVT VSQINTVLSG RTRRYTDIQL QYRALCLNTR YGTTVDEEKV RVLELARQRA
VRQAWAREQQ RLREGEEGLR AWTDGEKQQV LNTGRVQGYD GFFVTSVEQY PELSDSANNI
HFMRQSEMGR R
