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SKT_MOUSE
ID   SKT_MOUSE               Reviewed;        1946 AA.
AC   A2AQ25; A2AUE9; A2AUF0; A2AUF1; Q75UV8; Q75UV9; Q80VK2; Q8BHX8; Q8BHY1;
AC   Q8CHA8; Q8R0K6;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Sickle tail protein;
DE   AltName: Full=Enhancer trap locus 4;
GN   Name=Skt {ECO:0000312|EMBL:BAD14929.1};
GN   Synonyms=Etl4 {ECO:0000312|MGI:MGI:95454},
GN   Kiaa1217 {ECO:0000312|EMBL:BAC41473.2};
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] {ECO:0000305, ECO:0000312|EMBL:BAD14929.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), FUNCTION, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=16204209; DOI=10.1534/genetics.105.048934;
RA   Semba K., Araki K., Li Z., Matsumoto K., Suzuki M., Nakagata N., Takagi K.,
RA   Takeya M., Yoshinobu K., Araki M., Imai K., Abe K., Yamamura K.;
RT   "A novel murine gene, Sickle tail, linked to the Danforth's short tail
RT   locus, is required for normal development of the intervertebral disc.";
RL   Genetics 172:445-456(2006).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:BAC41473.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
RC   TISSUE=Embryonic tail {ECO:0000312|EMBL:BAC41473.2};
RX   PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT   The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [3] {ECO:0000305, ECO:0000312|EMBL:BAC35783.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 9).
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC35783.1};
RC   TISSUE=Kidney {ECO:0000312|EMBL:BAC35121.1}, and
RC   Ovary {ECO:0000312|EMBL:BAC35783.1};
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 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   [5] {ECO:0000305, ECO:0000312|EMBL:AAH50016.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 874-1946 (ISOFORM 3).
RC   STRAIN=129/Sv X 129SvCp {ECO:0000312|EMBL:AAH50016.1}, and FVB/N;
RC   TISSUE=Colon, and Embryonic stem cell {ECO:0000312|EMBL:AAH50016.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   INTERACTION WITH CPNE4.
RX   PubMed=12522145; DOI=10.1074/jbc.m212632200;
RA   Tomsig J.L., Snyder S.L., Creutz C.E.;
RT   "Identification of targets for calcium signaling through the copine family
RT   of proteins. Characterization of a coiled-coil copine-binding motif.";
RL   J. Biol. Chem. 278:10048-10054(2003).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT SER-357.
RC   TISSUE=Brain;
RX   PubMed=16452088; DOI=10.1074/mcp.t500040-mcp200;
RA   Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A.,
RA   Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A.,
RA   Schoepfer R., Burlingame A.L.;
RT   "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT   preparations using lectin weak affinity chromatography and mass
RT   spectrometry.";
RL   Mol. Cell. Proteomics 5:923-934(2006).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA   Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in naive
RT   and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; TYR-244; SER-361;
RP   SER-365; SER-809; SER-1032; SER-1035; SER-1038; SER-1049; SER-1466;
RP   SER-1843; SER-1899; SER-1902 AND SER-1905, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC   Testis;
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: Required for normal development of intervertebral disks.
CC       {ECO:0000269|PubMed:16204209}.
CC   -!- SUBUNIT: Interacts with CPNE4 (via VWFA domain) (PubMed:12522145).
CC       {ECO:0000269|PubMed:12522145}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16204209}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=9;
CC       Name=1;
CC         IsoId=A2AQ25-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2AQ25-2; Sequence=VSP_052416, VSP_052418;
CC       Name=3 {ECO:0000269|PubMed:16204209}; Synonyms=Skt-a
CC       {ECO:0000269|PubMed:16204209};
CC         IsoId=A2AQ25-3; Sequence=VSP_052418, VSP_052421;
CC       Name=4 {ECO:0000269|PubMed:16204209}; Synonyms=Skt-b
CC       {ECO:0000269|PubMed:16204209};
CC         IsoId=A2AQ25-4; Sequence=VSP_052418, VSP_052420, VSP_052421;
CC       Name=5;
CC         IsoId=A2AQ25-5; Sequence=VSP_052416, VSP_052418, VSP_052424,
CC                                  VSP_052425, VSP_052426;
CC       Name=6;
CC         IsoId=A2AQ25-6; Sequence=VSP_052416, VSP_052418, VSP_052421,
CC                                  VSP_052425, VSP_052426;
CC       Name=7 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072};
CC         IsoId=A2AQ25-7; Sequence=VSP_052417;
CC       Name=8 {ECO:0000269|PubMed:12465718};
CC         IsoId=A2AQ25-8; Sequence=VSP_052418, VSP_052419;
CC       Name=9 {ECO:0000269|PubMed:16141072};
CC         IsoId=A2AQ25-9; Sequence=VSP_052416, VSP_052418, VSP_052420,
CC                                  VSP_052422, VSP_052423;
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in the notochord and
CC       mesonephros during embryogenesis as well as in other areas such as the
CC       epithalamus sulcus, lens vesicle, inner retinal layer, heart, hepatic
CC       primordial surface, infundibulum, surface ectoderm, hind gut and limb
CC       bud mesenchyme. In adults, expressed in a range of tissues including
CC       the nucleus pulposus, corpus callosum, kidney, cardiac muscle, Sertoli
CC       cells and hair follicles. {ECO:0000269|PubMed:16204209}.
CC   -!- DISRUPTION PHENOTYPE: Mice display a kinky-tail phenotype in about half
CC       of homozygotes with defects in the nucleus pulposus and annulus
CC       fibrosus of intertebral disks. Shortening and curving of caudal
CC       vertebrae 20-25 is apparent by the age of 2 weeks.
CC       {ECO:0000269|PubMed:16204209}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH26657.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC41473.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB125594; BAD14929.1; -; mRNA.
DR   EMBL; AB125595; BAD14930.1; -; mRNA.
DR   EMBL; AB093289; BAC41473.2; ALT_INIT; mRNA.
DR   EMBL; AK052733; BAC35121.1; -; mRNA.
DR   EMBL; AK054453; BAC35783.1; -; mRNA.
DR   EMBL; AL844538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL929100; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC026657; AAH26657.2; ALT_INIT; mRNA.
DR   EMBL; BC050016; AAH50016.1; -; mRNA.
DR   CCDS; CCDS50510.1; -. [A2AQ25-4]
DR   CCDS; CCDS50511.1; -. [A2AQ25-3]
DR   CCDS; CCDS89430.1; -. [A2AQ25-1]
DR   RefSeq; NP_001074475.1; NM_001081006.1.
DR   RefSeq; NP_001171101.2; NM_001177630.2.
DR   RefSeq; NP_084171.2; NM_029895.4. [A2AQ25-4]
DR   RefSeq; NP_835160.2; NM_178059.5. [A2AQ25-3]
DR   RefSeq; XP_006497478.1; XM_006497415.3.
DR   RefSeq; XP_006497487.1; XM_006497424.3. [A2AQ25-2]
DR   AlphaFoldDB; A2AQ25; -.
DR   SMR; A2AQ25; -.
DR   BioGRID; 228993; 19.
DR   IntAct; A2AQ25; 10.
DR   MINT; A2AQ25; -.
DR   GlyGen; A2AQ25; 1 site.
DR   iPTMnet; A2AQ25; -.
DR   PhosphoSitePlus; A2AQ25; -.
DR   MaxQB; A2AQ25; -.
DR   PaxDb; A2AQ25; -.
DR   PeptideAtlas; A2AQ25; -.
DR   PRIDE; A2AQ25; -.
DR   Antibodypedia; 1578; 33 antibodies from 15 providers.
DR   Ensembl; ENSMUST00000045555; ENSMUSP00000041431; ENSMUSG00000036617. [A2AQ25-3]
DR   Ensembl; ENSMUST00000066509; ENSMUSP00000066170; ENSMUSG00000036617. [A2AQ25-1]
DR   Ensembl; ENSMUST00000114606; ENSMUSP00000110253; ENSMUSG00000036617. [A2AQ25-6]
DR   Ensembl; ENSMUST00000114607; ENSMUSP00000110254; ENSMUSG00000036617. [A2AQ25-5]
DR   Ensembl; ENSMUST00000114608; ENSMUSP00000110255; ENSMUSG00000036617. [A2AQ25-2]
DR   Ensembl; ENSMUST00000114614; ENSMUSP00000110261; ENSMUSG00000036617. [A2AQ25-4]
DR   GeneID; 208618; -.
DR   KEGG; mmu:208618; -.
DR   UCSC; uc008imn.1; mouse. [A2AQ25-3]
DR   UCSC; uc008imo.1; mouse. [A2AQ25-4]
DR   UCSC; uc008imp.1; mouse. [A2AQ25-7]
DR   UCSC; uc008imq.1; mouse. [A2AQ25-1]
DR   UCSC; uc008ims.1; mouse. [A2AQ25-6]
DR   UCSC; uc008imt.1; mouse. [A2AQ25-9]
DR   CTD; 100144434; -.
DR   MGI; MGI:95454; Etl4.
DR   VEuPathDB; HostDB:ENSMUSG00000036617; -.
DR   eggNOG; ENOG502QQCT; Eukaryota.
DR   GeneTree; ENSGT00940000156098; -.
DR   HOGENOM; CLU_002507_2_1_1; -.
DR   InParanoid; A2AQ25; -.
DR   OrthoDB; 65773at2759; -.
DR   PhylomeDB; A2AQ25; -.
DR   TreeFam; TF332255; -.
DR   BioGRID-ORCS; 208618; 4 hits in 72 CRISPR screens.
DR   ChiTaRS; Etl4; mouse.
DR   PRO; PR:A2AQ25; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; A2AQ25; protein.
DR   Bgee; ENSMUSG00000036617; Expressed in undifferentiated genital tubercle and 259 other tissues.
DR   ExpressionAtlas; A2AQ25; baseline and differential.
DR   Genevisible; A2AQ25; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0048706; P:embryonic skeletal system development; IMP:UniProtKB.
DR   InterPro; IPR022782; AIP3-like_C.
DR   InterPro; IPR026725; Skt.
DR   PANTHER; PTHR22741:SF11; PTHR22741:SF11; 1.
DR   Pfam; PF03915; AIP3; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Developmental protein;
KW   Glycoprotein; Phosphoprotein; Reference proteome.
FT   CHAIN           1..1946
FT                   /note="Sickle tail protein"
FT                   /id="PRO_0000287898"
FT   REGION          1..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          113..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          305..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          455..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          853..875
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          891..947
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1008..1221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1482..1567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1622..1664
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1691..1946
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          557..581
FT                   /evidence="ECO:0000255"
FT   COILED          644..685
FT                   /evidence="ECO:0000255"
FT   COILED          962..990
FT                   /evidence="ECO:0000255"
FT   COILED          1469..1495
FT                   /evidence="ECO:0000255"
FT   COILED          1659..1688
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        17..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..364
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1026..1041
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1047..1061
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1063..1094
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1171..1197
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1622..1640
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1734..1780
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1801..1867
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1880..1946
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         169
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         244
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         361
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         365
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         393
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5T5P2"
FT   MOD_RES         470
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5T5P2"
FT   MOD_RES         474
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355"
FT   MOD_RES         809
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1032
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1035
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1038
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1049
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1466
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1741
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5T5P2"
FT   MOD_RES         1843
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1899
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1902
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1905
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        357
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000269|PubMed:16452088"
FT   VAR_SEQ         1..282
FT                   /note="Missing (in isoform 2, isoform 5, isoform 6 and
FT                   isoform 9)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_052416"
FT   VAR_SEQ         252..1946
FT                   /note="Missing (in isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_052417"
FT   VAR_SEQ         560..594
FT                   /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT                   5, isoform 6, isoform 8 and isoform 9)"
FT                   /evidence="ECO:0000303|PubMed:12465718,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072,
FT                   ECO:0000303|PubMed:16204209"
FT                   /id="VSP_052418"
FT   VAR_SEQ         885..1755
FT                   /note="Missing (in isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:12465718"
FT                   /id="VSP_052419"
FT   VAR_SEQ         961..971
FT                   /note="Missing (in isoform 4 and isoform 9)"
FT                   /evidence="ECO:0000303|PubMed:16141072,
FT                   ECO:0000303|PubMed:16204209"
FT                   /id="VSP_052420"
FT   VAR_SEQ         1181..1739
FT                   /note="Missing (in isoform 3, isoform 4 and isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16204209"
FT                   /id="VSP_052421"
FT   VAR_SEQ         1181..1191
FT                   /note="NLEFYHEDVRK -> VTCGSYTFTIQ (in isoform 9)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_052422"
FT   VAR_SEQ         1192..1946
FT                   /note="Missing (in isoform 9)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_052423"
FT   VAR_SEQ         1207..1739
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_052424"
FT   VAR_SEQ         1781..1784
FT                   /note="ANGS -> VVLP (in isoform 5 and isoform 6)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_052425"
FT   VAR_SEQ         1785..1946
FT                   /note="Missing (in isoform 5 and isoform 6)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_052426"
FT   CONFLICT        41
FT                   /note="R -> H (in Ref. 5; AAH50016)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        119
FT                   /note="T -> R (in Ref. 2; BAC41473)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        551
FT                   /note="T -> A (in Ref. 2; BAC41473)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        818
FT                   /note="R -> Q (in Ref. 2; BAC41473)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1946 AA;  213037 MW;  E5D411BD044DC1CB CRC64;
     MEESEGQKCE PNLPPSGDSR QMPQQGRSNL HVTSQEDAAC RRPRERLSNG NARAQVSKPA
     RNIPRRHTLG GPRSSKEILG MQPSEMDRKR EAFLEHLKQK YPHHATAIMG HQERLRDQTK
     SPKLSHSPQP PNLGDPVEHL SETSGDSLEA MSEGEVPSPF ARGSRTRASL PVVRSANQTK
     ERSLGVLYLQ YGDETKQLRM PNEVTSTDTI RALFVSAFPQ QLTMKMLESP SVAIYIKDDS
     RNVYYELNDV RNIQDRSLLK VYNKDPSHAF NHMTKAVNGD MRMQREIVYA RGDGLVAPRP
     GSVAHPPHVI PNSPPSTPVP HSLPPSPSRI PYGGSRPMAI PGNATIPRDR LSSLPVSRSI
     SPSPSAILER RDVKPDEDMS SKNLVMFRNE GFYADPYLYH EGRMSIASSH GGHPLDVPDH
     VIAYHRTAIR SASAYCSPSL QAEMHMEQSL YRQKSRKYPD SHLPTLGSKT PPASPHRVGD
     LRMIDLHPHL NTHGPPHTLQ PDRASPSRQS FKKEPGTLVY IEKPRNTSGL SSLVDLGPPL
     VEKQGFAYST TTIPKDRETR ERMQAMEKQI ASLTGLVQSA LFKGPITSSS KEASSEKMVK
     ATANRNQADG AGTAHVSAGK VLGSVEFSLP PSQPLPAGTS PIHTSLLDMR RNVAELRLQL
     QQMRQLQLQN QEILRAMMKK AELEISNKVK ETMKRLEDPV QRQRTLVEQE RQKYLHEEER
     IVKKLCELED FVEDLKKDSS STGRVVTLKD VEDGAFLLRQ VGEAVATLKG EFPTLQNKMR
     AVLRIEVEAV RFLKEEPHKL DSLLKRVRSM TDVLTMLRRH VTDGLLKGTD ASQAAQYVAM
     EKATAAEVLK HQEETAHAPG QPLHCSTGSP GDVKSEVVPL STMTVHHVQS SPVVMQPSQH
     SSALMNPAQN LPGGTRPHTA SPPAITQEVT SAQSAPGPQS PQTPVNGSSM QSLFIEEIHS
     VSAKNRAVSI EKAEKKWEEK RQNLEHYNGK EFEKLLEEAQ ANIMKSIPNL EMPPASSPVS
     KGDAAGDKLE LSEDSPNSEQ ELDKIGGKSP PPPPPPPRRS YLPGSGLTTT RSGDVVYTGR
     SMSKVSSEDP GPTPQTRATK CPPEEPASAW APSPPPVPAP SSKEEEEEEE EGDKIMAELQ
     AFQKCSFMDV NPNSHAEQSR ANSHLKDTRA GATAPPKEKK NLEFYHEDVR KSDVECENGP
     QVESQKVTAG ALRPSGPPKW ERVMVDSISD TSRTSECRAD TFTEENATPN KSLFRDSRNY
     SQKNVPKVSF SSSGLNSLEG EINKGPNVSG LQCAIPDLEN QKLNFGKTKE IGQQGQENAD
     KSHIPLPTRS AEFSIHDVKT QDQDVPVTGY GQVVLRSKVG RHANMNMNED GESTPSSPSE
     EHTATDNIAF MITKTAVQVL SSGEVHDIVS QKGQDVQTVN IDGRKETASQ HEGTEGEEPV
     VCLDKKPVII IFDEPMDIRS AYKRLSTIFE ECDEELERML TEEKIEEEEE DENEDSGVRT
     SSQMSCEQVD SRSDRMGQKA ETQSQPHVLS AELLTPGVQG VRKAEQRKLS SADSPDSGNK
     CGMVDDQFES PKKKFKFKFP KKQLAALTQA IRTGTKTGKK TLQVVVYEEE EEDGTLKQHK
     EAKRFEITRS QPEDALKTMA RRQEQLSPEG TLPASRTDEI RKSTYRTLDS LEQTIKQLEN
     TISEMSPRAL VDTSCSSNRD CGASLPHMAQ EVSPRSLLVL DEVPPAPEPP TSISPASRKG
     SSTTPQTSRM PVPMTSKNRP GSLDKASKQS KLQDPRQYRQ ANGSAKKAGG DCKPTSPSLP
     ASKIPALSPS SGKSSSLPSA SGDSSNLPNA PATKPSIAST PLSPQAGRSA HSASLIPSVS
     NGSLKFQSPP HAGKGHHHLS FALQTQNGRA APTTSSSSSP PSPASPTSLN QGARGIRTIH
     TPSLASYKAQ NGSSSKATPS TAKETS
 
 
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