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