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 27-MAR-2024, entry version 144. 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}. 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; 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; 9. DR IntAct; Q3UHK6; 5. DR MINT; Q3UHK6; -. DR STRING; 10090.ENSMUSP00000102783; -. DR GlyConnect; 2432; 3 N-Linked glycans (4 sites). [Q3UHK6-2] DR GlyCosmos; Q3UHK6; 12 sites, No reported glycans. DR GlyGen; Q3UHK6; 14 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q3UHK6; -. DR PhosphoSitePlus; Q3UHK6; -. DR SwissPalm; Q3UHK6; -. DR jPOST; Q3UHK6; -. DR MaxQB; Q3UHK6; -. DR PaxDb; 10090-ENSMUSP00000102783; -. DR PeptideAtlas; Q3UHK6; -. DR ProteomicsDB; 258993; -. [Q3UHK6-1] DR ProteomicsDB; 258994; -. [Q3UHK6-2] DR ProteomicsDB; 258995; -. [Q3UHK6-3] DR ProteomicsDB; 258996; -. [Q3UHK6-4] DR Antibodypedia; 67208; 27 antibodies from 7 providers. DR DNASU; 23966; -. DR Ensembl; ENSMUST00000107162.8; ENSMUSP00000102780.2; ENSMUSG00000048078.17. [Q3UHK6-2] DR Ensembl; ENSMUST00000107165.8; ENSMUSP00000102783.2; ENSMUSG00000048078.17. [Q3UHK6-3] DR Ensembl; ENSMUST00000107166.8; ENSMUSP00000102784.2; ENSMUSG00000048078.17. [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 AGR; MGI:2447063; -. 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 59 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 223 other cell types or tissues. DR ExpressionAtlas; Q3UHK6; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. 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 CDD; cd00054; EGF_CA; 2. DR Gene3D; 2.10.25.10; Laminin; 6. DR Gene3D; 2.180.10.10; RHS repeat-associated core; 2. DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 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; IPR009471; Ten_N. DR InterPro; IPR028916; Tox-GHH_dom. DR InterPro; IPR006530; YD. DR NCBIfam; TIGR03696; Rhs_assc_core; 1. DR NCBIfam; TIGR01643; YD_repeat_2x; 1. DR PANTHER; PTHR11219; TENEURIN AND N-ACETYLGLUCOSAMINE-1-PHOSPHODIESTER ALPHA-N-ACETYLGLUCOSAMINIDASE; 1. DR PANTHER; PTHR11219:SF9; TENEURIN-4; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF05593; RHS_repeat; 2. DR Pfam; PF06484; Ten_N; 2. DR Pfam; PF15636; Tox-GHH; 1. DR SMART; SM00181; EGF; 8. DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1. DR SUPFAM; SSF57196; EGF/Laminin; 1. DR SUPFAM; SSF101898; NHL repeat; 1. DR SUPFAM; SSF69322; Tricorn protease domain 2; 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. DR Genevisible; Q3UHK6; MM. 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 //