TEN3_HUMAN
ID TEN3_HUMAN Reviewed; 2699 AA.
AC Q9P273; Q5XUL9; Q96SY2; Q9NV77; Q9NVW1; Q9NZJ2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Teneurin-3 {ECO:0000305};
DE Short=Ten-3;
DE AltName: Full=Protein Odd Oz/ten-m homolog 3 {ECO:0000303|Ref.5};
DE AltName: Full=Tenascin-M3 {ECO:0000250|UniProtKB:Q9WTS6};
DE Short=Ten-m3 {ECO:0000250|UniProtKB:Q9WTS6};
DE AltName: Full=Teneurin transmembrane protein 3 {ECO:0000250|UniProtKB:Q9WTS6};
GN Name=TENM3 {ECO:0000312|HGNC:HGNC:29944};
GN Synonyms=KIAA1455 {ECO:0000303|PubMed:10819331}, ODZ3 {ECO:0000303|Ref.5},
GN TNM3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-442, AND TISSUE SPECIFICITY.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 250-2699, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1606-2699.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2503-2583.
RA Steckler N.K., Lau J.M., Robinson D.L.;
RT "Identification of an ODZ3-like gene in Homo sapiens.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INVOLVEMENT IN MCOPCB9.
RX PubMed=22766609; DOI=10.1038/gim.2012.71;
RA Aldahmesh M.A., Mohammed J.Y., Al-Hazzaa S., Alkuraya F.S.;
RT "Homozygous null mutation in ODZ3 causes microphthalmia in humans.";
RL Genet. Med. 14:900-904(2012).
RN [7]
RP INVOLVEMENT IN MCOPS15.
RX PubMed=27103084; DOI=10.1002/ajmg.a.37667;
RA Chassaing N., Ragge N., Plaisancie J., Patat O., Genevieve D., Rivier F.,
RA Malrieu-Eliaou C., Hamel C., Kaplan J., Calvas P.;
RT "Confirmation of TENM3 involvement in autosomal recessive colobomatous
RT microphthalmia.";
RL Am. J. Med. Genet. A 170:1895-1898(2016).
RN [8]
RP INVOLVEMENT IN MCOPS15, AND VARIANT MCOPS15 619-CYS--ARG-2699 DEL.
RX PubMed=30513139; DOI=10.1002/ajmg.a.40658;
RA Stephen J., Nampoothiri S., Kuppa S., Yesodharan D., Radhakrishnan N.,
RA Gahl W.A., Malicdan M.C.V.;
RT "Novel truncating mutation in TENM3 in siblings with motor developmental
RT delay, ocular coloboma, oval cornea, without microphthalmia.";
RL Am. J. Med. Genet. A 176:2930-2933(2018).
RN [9]
RP INVOLVEMENT IN MCOPS15, AND VARIANTS MCOPS15 GLY-1349 AND TRP-2563.
RX PubMed=29753094; DOI=10.1016/j.ejmg.2018.05.004;
RA Singh B., Srivastava P., Phadke S.R.;
RT "Sequence variations in TENM3 gene causing eye anomalies with intellectual
RT disability: Expanding the phenotypic spectrum.";
RL Eur. J. Med. Genet. 62:61-64(2019).
CC -!- FUNCTION: Involved in neural development by regulating the
CC establishment of proper connectivity within the nervous system. Acts in
CC both pre- and postsynaptic neurons in the hippocampus to control the
CC assembly of a precise topographic projection: required in both CA1 and
CC subicular neurons for the precise targeting of proximal CA1 axons to
CC distal subiculum, probably by promoting homophilic cell adhesion.
CC Required for proper dendrite morphogenesis and axon targeting in the
CC vertebrate visual system, thereby playing a key role in the development
CC of the visual pathway. Regulates the formation in ipsilateral retinal
CC mapping to both the dorsal lateral geniculate nucleus (dLGN) and the
CC superior colliculus (SC). May also be involved in the differentiation
CC of the fibroblast-like cells in the superficial layer of mandibular
CC condylar cartilage into chondrocytes. {ECO:0000250|UniProtKB:Q9WTS6}.
CC -!- SUBUNIT: Homodimer; disulfide-linked; to mediate homophilic cell
CC adhesion. Heterodimer with either TENM1 or TENM2. May also form
CC heterodimer with TENM4. {ECO:0000250|UniProtKB:Q9WTS6}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9WTS6};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:Q9WTS6}. Cell
CC projection, axon {ECO:0000250|UniProtKB:Q9WTS6}.
CC -!- TISSUE SPECIFICITY: Expressed in adult and fetal brain, slightly lower
CC levels in testis and ovary, and intermediate levels in all other
CC peripheral tissues examined. Not expressed in spleen or liver.
CC Expression was high in brain, with highest levels in amygdala and
CC caudate nucleus, followed by thalamus and subthalamic nucleus.
CC {ECO:0000269|PubMed:10625539, ECO:0000269|PubMed:10819331}.
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 {ECO:0000250|UniProtKB:Q9WTS6}.
CC -!- DOMAIN: Cytoplasmic proline-rich regions could serve as docking domains
CC for intracellular SH3-containing proteins.
CC {ECO:0000250|UniProtKB:Q9WTS6}.
CC -!- DISEASE: Microphthalmia, isolated, with coloboma, 9 (MCOPCB9)
CC [MIM:615145]: A disorder of eye formation, ranging from small size of a
CC single eye to complete bilateral absence of ocular tissues. Ocular
CC abnormalities like opacities of the cornea and lens, scaring of the
CC retina and choroid, and other abnormalities may also be present. Ocular
CC colobomas are a set of malformations resulting from abnormal
CC morphogenesis of the optic cup and stalk, and the fusion of the fetal
CC fissure (optic fissure). {ECO:0000269|PubMed:22766609}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Microphthalmia, syndromic, 15 (MCOPS15) [MIM:615145]: A form
CC of microphthalmia, a disorder of eye formation, ranging from small size
CC of a single eye to complete bilateral absence of ocular tissues
CC (anophthalmia). In many cases, microphthalmia/anophthalmia occurs in
CC association with syndromes that include non-ocular abnormalities.
CC MCOPS15 is characterized by microphthalmia and/or coloboma, with
CC developmental delay in which speech appears to be more severely
CC affected than motor abilities. Additional ocular anomalies that have
CC been observed include ptosis, keyhole-shaped pupils, microcornea,
CC sclerocornea, and anterior segment dysgenesis.
CC {ECO:0000269|PubMed:27103084, ECO:0000269|PubMed:29753094,
CC ECO:0000269|PubMed:30513139}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91633.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91879.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB55138.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC131943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093601; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC109353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF195420; AAF28318.1; -; mRNA.
DR EMBL; AB040888; BAA95979.2; -; mRNA.
DR EMBL; AK001336; BAA91633.1; ALT_INIT; mRNA.
DR EMBL; AK001748; BAA91879.1; ALT_INIT; mRNA.
DR EMBL; AK027473; BAB55138.1; ALT_INIT; mRNA.
DR EMBL; AY736855; AAU84915.1; -; Genomic_DNA.
DR CCDS; CCDS47165.1; -.
DR RefSeq; NP_001073946.1; NM_001080477.3.
DR RefSeq; XP_016863882.1; XM_017008393.1.
DR AlphaFoldDB; Q9P273; -.
DR SMR; Q9P273; -.
DR BioGRID; 120836; 55.
DR IntAct; Q9P273; 25.
DR MINT; Q9P273; -.
DR STRING; 9606.ENSP00000424226; -.
DR GlyGen; Q9P273; 20 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q9P273; -.
DR PhosphoSitePlus; Q9P273; -.
DR BioMuta; TENM3; -.
DR DMDM; 118573058; -.
DR EPD; Q9P273; -.
DR jPOST; Q9P273; -.
DR MassIVE; Q9P273; -.
DR MaxQB; Q9P273; -.
DR PaxDb; Q9P273; -.
DR PeptideAtlas; Q9P273; -.
DR PRIDE; Q9P273; -.
DR ProteomicsDB; 83742; -.
DR Antibodypedia; 28699; 89 antibodies from 24 providers.
DR Ensembl; ENST00000511685.6; ENSP00000424226.1; ENSG00000218336.9.
DR GeneID; 55714; -.
DR KEGG; hsa:55714; -.
DR MANE-Select; ENST00000511685.6; ENSP00000424226.1; NM_001080477.4; NP_001073946.1.
DR UCSC; uc003ivd.2; human.
DR CTD; 55714; -.
DR DisGeNET; 55714; -.
DR GeneCards; TENM3; -.
DR HGNC; HGNC:29944; TENM3.
DR HPA; ENSG00000218336; Tissue enhanced (brain, placenta).
DR MalaCards; TENM3; -.
DR MIM; 610083; gene.
DR MIM; 615145; phenotype.
DR neXtProt; NX_Q9P273; -.
DR OpenTargets; ENSG00000218336; -.
DR Orphanet; 98938; Colobomatous microphthalmia.
DR PharmGKB; PA134961178; -.
DR VEuPathDB; HostDB:ENSG00000218336; -.
DR eggNOG; KOG4659; Eukaryota.
DR GeneTree; ENSGT01030000234566; -.
DR InParanoid; Q9P273; -.
DR OMA; RIRAIRC; -.
DR PhylomeDB; Q9P273; -.
DR TreeFam; TF316833; -.
DR PathwayCommons; Q9P273; -.
DR SignaLink; Q9P273; -.
DR BioGRID-ORCS; 55714; 15 hits in 1069 CRISPR screens.
DR ChiTaRS; TENM3; human.
DR GenomeRNAi; 55714; -.
DR Pharos; Q9P273; Tbio.
DR PRO; PR:Q9P273; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9P273; protein.
DR Bgee; ENSG00000218336; Expressed in sural nerve and 125 other tissues.
DR ExpressionAtlas; Q9P273; baseline and differential.
DR Genevisible; Q9P273; HS.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0048593; P:camera-type eye morphogenesis; IMP:UniProtKB.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
DR GO; GO:0048666; P:neuron development; IBA:GO_Central.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:1903385; P:regulation of homophilic cell adhesion; 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; IPR022385; Rhs_assc_core.
DR InterPro; IPR027691; Ten-3/4.
DR InterPro; IPR009471; Ten_N.
DR InterPro; IPR028916; Tox-GHH_dom.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR006530; YD.
DR PANTHER; PTHR11219:SF65; PTHR11219:SF65; 1.
DR Pfam; PF06484; Ten_N; 2.
DR Pfam; PF15636; Tox-GHH; 1.
DR SMART; SM00181; EGF; 8.
DR SUPFAM; SSF49464; SSF49464; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR TIGRFAMs; TIGR03696; Rhs_assc_core; 1.
DR TIGRFAMs; TIGR01643; YD_repeat_2x; 2.
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; Differentiation;
KW Disease variant; Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW Microphthalmia; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..2699
FT /note="Teneurin-3"
FT /id="PRO_0000259505"
FT TOPO_DOM 1..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..2699
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 1..309
FT /note="Teneurin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00694"
FT DOMAIN 514..545
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 546..576
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 578..610
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 611..642
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 644..677
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 678..709
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 710..739
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 740..774
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1200..1244
FT /note="NHL 1"
FT REPEAT 1270..1314
FT /note="NHL 2"
FT REPEAT 1331..1371
FT /note="NHL 3"
FT REPEAT 1402..1429
FT /note="NHL 4"
FT REPEAT 1458..1501
FT /note="NHL 5"
FT REPEAT 1511..1530
FT /note="YD 1"
FT REPEAT 1547..1567
FT /note="YD 2"
FT REPEAT 1610..1629
FT /note="YD 3"
FT REPEAT 1630..1652
FT /note="YD 4"
FT REPEAT 1823..1842
FT /note="YD 5"
FT REPEAT 1864..1882
FT /note="YD 6"
FT REPEAT 1883..1903
FT /note="YD 7"
FT REPEAT 1910..1927
FT /note="YD 8"
FT REPEAT 1928..1949
FT /note="YD 9"
FT REPEAT 1950..1967
FT /note="YD 10"
FT REPEAT 1970..1990
FT /note="YD 11"
FT REPEAT 1993..2013
FT /note="YD 12"
FT REPEAT 2021..2040
FT /note="YD 13"
FT REPEAT 2046..2063
FT /note="YD 14"
FT REPEAT 2064..2090
FT /note="YD 15"
FT REPEAT 2092..2105
FT /note="YD 16"
FT REPEAT 2106..2129
FT /note="YD 17"
FT REPEAT 2132..2152
FT /note="YD 18"
FT REPEAT 2153..2173
FT /note="YD 19"
FT REPEAT 2175..2195
FT /note="YD 20"
FT REPEAT 2207..2227
FT /note="YD 21"
FT REPEAT 2229..2249
FT /note="YD 22"
FT REPEAT 2275..2316
FT /note="YD 23"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 860
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 883
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1735
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1820
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1921
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 518..528
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 522..533
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 535..544
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 553..564
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 566..575
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 582..593
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 587..598
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 600..609
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 614..625
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 619..630
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 632..641
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 652..665
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 667..676
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 681..691
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 685..696
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 698..707
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 712..722
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 716..727
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 729..738
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 743..753
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 747..762
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 764..773
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VARIANT 385
FT /note="S -> C (in dbSNP:rs3749509)"
FT /id="VAR_053796"
FT VARIANT 619..2699
FT /note="Missing (in MCOPS15)"
FT /evidence="ECO:0000269|PubMed:30513139"
FT /id="VAR_083250"
FT VARIANT 1349
FT /note="A -> G (in MCOPS15; unknown pathological
FT significance; dbSNP:rs1243762658)"
FT /evidence="ECO:0000269|PubMed:29753094"
FT /id="VAR_083251"
FT VARIANT 2563
FT /note="R -> W (in MCOPS15; unknown pathological
FT significance; dbSNP:rs755000701)"
FT /evidence="ECO:0000269|PubMed:29753094"
FT /id="VAR_083252"
FT CONFLICT 435
FT /note="G -> K (in Ref. 2; AAF28318)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2699 AA; 300950 MW; B26701AD7D85560F CRC64;
MDVKERRPYC SLTKSRREKE RRYTNSSADN EECRVPTQKS YSSSETLKAF DHDSSRLLYG
NRVKDLVHRE ADEFTRQGQN FTLRQLGVCE PATRRGLAFC AEMGLPHRGY SISAGSDADT
ENEAVMSPEH AMRLWGRGVK SGRSSCLSSR SNSALTLTDT EHENKSDSEN EQPASNQGQS
TLQPLPPSHK QHSAQHHPSI TSLNRNSLTN RRNQSPAPPA ALPAELQTTP ESVQLQDSWV
LGSNVPLESR HFLFKTGTGT TPLFSTATPG YTMASGSVYS PPTRPLPRNT LSRSAFKFKK
SSKYCSWKCT ALCAVGVSVL LAILLSYFIA MHLFGLNWQL QQTENDTFEN GKVNSDTMPT
NTVSLPSGDN GKLGGFTQEN NTIDSGELDI GRRAIQEIPP GIFWRSQLFI DQPQFLKFNI
SLQKDALIGV YGRKGLPPSH TQYDFVELLD GSRLIAREQR SLLETERAGR QARSVSLHEA
GFIQYLDSGI WHLAFYNDGK NAEQVSFNTI VIESVVECPR NCHGNGECVS GTCHCFPGFL
GPDCSRAACP VLCSGNGQYS KGRCLCFSGW KGTECDVPTT QCIDPQCGGR GICIMGSCAC
NSGYKGESCE EADCIDPGCS NHGVCIHGEC HCSPGWGGSN CEILKTMCPD QCSGHGTYLQ
ESGSCTCDPN WTGPDCSNEI CSVDCGSHGV CMGGTCRCEE GWTGPACNQR ACHPRCAEHG
TCKDGKCECS QGWNGEHCTI EGCPGLCNSN GRCTLDQNGW HCVCQPGWRG AGCDVAMETL
CTDSKDNEGD GLIDCMDPDC CLQSSCQNQP YCRGLPDPQD IISQSLQSPS QQAAKSFYDR
ISFLIGSDST HVIPGESPFN KSLASVIRGQ VLTADGTPLI GVNVSFFHYP EYGYTITRQD
GMFDLVANGG ASLTLVFERS PFLTQYHTVW IPWNVFYVMD TLVMKKEEND IPSCDLSGFV
RPNPIIVSSP LSTFFRSSPE DSPIIPETQV LHEETTIPGT DLKLSYLSSR AAGYKSVLKI
TMTQSIIPFN LMKVHLMVAV VGRLFQKWFP ASPNLAYTFI WDKTDAYNQK VYGLSEAVVS
VGYEYESCLD LTLWEKRTAI LQGYELDASN MGGWTLDKHH VLDVQNGILY KGNGENQFIS
QQPPVVSSIM GNGRRRSISC PSCNGQADGN KLLAPVALAC GIDGSLYVGD FNYVRRIFPS
GNVTSVLELS SNPAHRYYLA TDPVTGDLYV SDTNTRRIYR PKSLTGAKDL TKNAEVVAGT
GEQCLPFDEA RCGDGGKAVE ATLMSPKGMA VDKNGLIYFV DGTMIRKVDQ NGIISTLLGS
NDLTSARPLT CDTSMHISQV RLEWPTDLAI NPMDNSIYVL DNNVVLQITE NRQVRIAAGR
PMHCQVPGVE YPVGKHAVQT TLESATAIAV SYSGVLYITE TDEKKINRIR QVTTDGEISL
VAGIPSECDC KNDANCDCYQ SGDGYAKDAK LSAPSSLAAS PDGTLYIADL GNIRIRAVSK
NKPLLNSMNF YEVASPTDQE LYIFDINGTH QYTVSLVTGD YLYNFSYSND NDITAVTDSN
GNTLRIRRDP NRMPVRVVSP DNQVIWLTIG TNGCLKSMTA QGLELVLFTY HGNSGLLATK
SDETGWTTFF DYDSEGRLTN VTFPTGVVTN LHGDMDKAIT VDIESSSREE DVSITSNLSS
IDSFYTMVQD QLRNSYQIGY DGSLRIIYAS GLDSHYQTEP HVLAGTANPT VAKRNMTLPG
ENGQNLVEWR FRKEQAQGKV NVFGRKLRVN GRNLLSVDFD RTTKTEKIYD DHRKFLLRIA
YDTSGHPTLW LPSSKLMAVN VTYSSTGQIA SIQRGTTSEK VDYDGQGRIV SRVFADGKTW
SYTYLEKSMV LLLHSQRQYI FEYDMWDRLS AITMPSVARH TMQTIRSIGY YRNIYNPPES
NASIITDYNE EGLLLQTAFL GTSRRVLFKY RRQTRLSEIL YDSTRVSFTY DETAGVLKTV
NLQSDGFICT IRYRQIGPLI DRQIFRFSED GMVNARFDYS YDNSFRVTSM QGVINETPLP
IDLYQFDDIS GKVEQFGKFG VIYYDINQII STAVMTYTKH FDAHGRIKEI QYEIFRSLMY
WITIQYDNMG RVTKREIKIG PFANTTKYAY EYDVDGQLQT VYLNEKIMWR YNYDLNGNLH
LLNPSNSARL TPLRYDLRDR ITRLGDVQYR LDEDGFLRQR GTEIFEYSSK GLLTRVYSKG
SGWTVIYRYD GLGRRVSSKT SLGQHLQFFY ADLTYPTRIT HVYNHSSSEI TSLYYDLQGH
LFAMEISSGD EFYIASDNTG TPLAVFSSNG LMLKQIQYTA YGEIYFDSNI DFQLVIGFHG
GLYDPLTKLI HFGERDYDIL AGRWTTPDIE IWKRIGKDPA PFNLYMFRNN NPASKIHDVK
DYITDVNSWL VTFGFHLHNA IPGFPVPKFD LTEPSYELVK SQQWDDIPPI FGVQQQVARQ
AKAFLSLGKM AEVQVSRRRA GGAQSWLWFA TVKSLIGKGV MLAVSQGRVQ TNVLNIANED
CIKVAAVLNN AFYLENLHFT IEGKDTHYFI KTTTPESDLG TLRLTSGRKA LENGINVTVS
QSTTVVNGRT RRFADVEMQF GALALHVRYG MTLDEEKARI LEQARQRALA RAWAREQQRV
RDGEEGARLW TEGEKRQLLS AGKVQGYDGY YVLSVEQYPE LADSANNIQF LRQSEIGRR
