SEPT9_MOUSE
ID SEPT9_MOUSE Reviewed; 583 AA.
AC Q80UG5; A2A6U2; A2A6U4; A2A6U6; Q3URP2; Q80TM7; Q9QYX9;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Septin-9;
DE AltName: Full=SL3-3 integration site 1 protein;
GN Name=Septin9 {ECO:0000312|MGI:MGI:1858222};
GN Synonyms=Kiaa0991 {ECO:0000303|PubMed:12693553},
GN Sept9 {ECO:0000312|MGI:MGI:1858222}, Sint1 {ECO:0000303|PubMed:10666245};
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), AND TISSUE SPECIFICITY.
RX PubMed=10666245; DOI=10.1128/jvi.74.5.2161-2168.2000;
RA Soerensen A.B., Lund A.H., Ethelberg S., Copeland N.G., Jenkins N.A.,
RA Pedersen F.S.;
RT "Sint1, a common integration site in SL3-3-induced T-cell lymphomas,
RT harbors a putative proto-oncogene with homology to the septin gene
RT family.";
RL J. Virol. 74:2161-2168(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2), TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12039034; DOI=10.1016/s0378-1119(02)00406-7;
RA Soerensen A.B., Warming S., Fuechtbauer E.-M., Pedersen F.S.;
RT "Alternative splicing, expression, and gene structure of the septin-like
RT putative proto-oncogene Sint1.";
RL Gene 285:79-89(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Embryonic tail;
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 [4]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=129; TISSUE=Mammary gland;
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 [8]
RP PROTEIN SEQUENCE OF 548-559, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=17546647; DOI=10.1002/humu.20554;
RA Sudo K., Ito H., Iwamoto I., Morishita R., Asano T., Nagata K.;
RT "SEPT9 sequence alternations causing hereditary neuralgic amyotrophy are
RT associated with altered interactions with SEPT4/SEPT11 and resistance to
RT Rho/Rhotekin-signaling.";
RL Hum. Mutat. 28:1005-1013(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; THR-49 AND THR-143, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-62, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May
CC play a role in cytokinesis (Potential). {ECO:0000250, ECO:0000305}.
CC -!- SUBUNIT: Septins polymerize into heterooligomeric protein complexes
CC that form filaments, and associate with cellular membranes, actin
CC filaments, and microtubules. GTPase activity is required for filament
CC formation. Interacts with SEPTIN2, SEPTIN6, SEPTIN7, SEPTIN11 and
CC SEPTIN14. Interacts with RTKN and ARHGEF18 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:17546647}. Note=In an epithelial cell line,
CC concentrates at cell-cell contact areas. After TGF-beta1 treatment and
CC induction of epithelial to mesenchymal transition, colocalizes with
CC actin stress fibers.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q80UG5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80UG5-2; Sequence=VSP_012341;
CC Name=3;
CC IsoId=Q80UG5-3; Sequence=VSP_012342;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined except muscle.
CC Isoforms are differentially expressed in testes, kidney, liver, heart,
CC spleen and brain. {ECO:0000269|PubMed:10666245,
CC ECO:0000269|PubMed:12039034}.
CC -!- DEVELOPMENTAL STAGE: At 8 dpc mainly expressed in the lateral plate
CC mesoderm and the somites. Beginning at 9 dpc the lateral plate
CC expression is clearly focused in the developing fore- and hindlimb
CC buds. In the cephalic region, expressed in the first and second
CC branchial arch, in the nasal process and around the otic pit. At 9.5
CC dpc strongest expression is observed in the mesenchyme of the branchial
CC arches, the limbs, and the developing dorsal root ganglia. Weak to
CC intermediate expression is found in the neural epithelium. Expression
CC is seen in the newly formed somites in the tail bud of older embryos.
CC During formation of the digits, expression seems to outline the
CC surviving tissue bordering it towards the apoptotic webbing. Expression
CC is seen in the developing outer ear and in several areas known to be
CC regulated by intensive epithelial mesenchymal interactions, like the
CC viscera follicles and the developing mammary glands.
CC {ECO:0000269|PubMed:12039034}.
CC -!- DISEASE: Note=Putative proto-oncogene involved in T-cell
CC lymphomagenesis. May play a role in leukemogenesis.
CC -!- MISCELLANEOUS: Targeted by proviral insertion in T-cell lymphomas
CC induced by the murine retrovirus SL3-3 MuLV.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01056}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65697.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ250723; CAB59833.1; -; mRNA.
DR EMBL; AF450142; AAL50685.1; -; Genomic_DNA.
DR EMBL; AF450141; AAL50685.1; JOINED; Genomic_DNA.
DR EMBL; AK031757; BAC27538.1; -; mRNA.
DR EMBL; AK122415; BAC65697.2; ALT_INIT; mRNA.
DR EMBL; AK141312; BAE24646.1; -; mRNA.
DR EMBL; AL603868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL611935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046524; AAH46524.1; -; mRNA.
DR CCDS; CCDS25684.1; -. [Q80UG5-2]
DR CCDS; CCDS48990.1; -. [Q80UG5-1]
DR CCDS; CCDS48991.1; -. [Q80UG5-3]
DR RefSeq; NP_001106958.1; NM_001113486.1. [Q80UG5-1]
DR RefSeq; NP_001106959.1; NM_001113487.1. [Q80UG5-3]
DR RefSeq; NP_001106960.1; NM_001113488.1. [Q80UG5-2]
DR RefSeq; NP_059076.1; NM_017380.2. [Q80UG5-2]
DR RefSeq; XP_006533808.2; XM_006533745.3. [Q80UG5-2]
DR RefSeq; XP_006533809.1; XM_006533746.3. [Q80UG5-2]
DR AlphaFoldDB; Q80UG5; -.
DR SMR; Q80UG5; -.
DR BioGRID; 207494; 53.
DR IntAct; Q80UG5; 41.
DR MINT; Q80UG5; -.
DR STRING; 10090.ENSMUSP00000091435; -.
DR iPTMnet; Q80UG5; -.
DR PhosphoSitePlus; Q80UG5; -.
DR EPD; Q80UG5; -.
DR jPOST; Q80UG5; -.
DR MaxQB; Q80UG5; -.
DR PaxDb; Q80UG5; -.
DR PeptideAtlas; Q80UG5; -.
DR PRIDE; Q80UG5; -.
DR ProteomicsDB; 257120; -. [Q80UG5-1]
DR ProteomicsDB; 257121; -. [Q80UG5-2]
DR ProteomicsDB; 257122; -. [Q80UG5-3]
DR Antibodypedia; 32488; 234 antibodies from 31 providers.
DR DNASU; 53860; -.
DR Ensembl; ENSMUST00000019038; ENSMUSP00000019038; ENSMUSG00000059248. [Q80UG5-3]
DR Ensembl; ENSMUST00000093907; ENSMUSP00000091435; ENSMUSG00000059248. [Q80UG5-1]
DR Ensembl; ENSMUST00000100193; ENSMUSP00000097767; ENSMUSG00000059248. [Q80UG5-2]
DR Ensembl; ENSMUST00000106349; ENSMUSP00000101956; ENSMUSG00000059248. [Q80UG5-2]
DR GeneID; 53860; -.
DR KEGG; mmu:53860; -.
DR UCSC; uc007mnd.2; mouse. [Q80UG5-1]
DR UCSC; uc007mne.2; mouse. [Q80UG5-3]
DR CTD; 10801; -.
DR MGI; MGI:1858222; Septin9.
DR VEuPathDB; HostDB:ENSMUSG00000059248; -.
DR eggNOG; KOG1547; Eukaryota.
DR GeneTree; ENSGT00940000157195; -.
DR HOGENOM; CLU_017718_7_1_1; -.
DR InParanoid; Q80UG5; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q80UG5; -.
DR TreeFam; TF101078; -.
DR BioGRID-ORCS; 53860; 2 hits in 47 CRISPR screens.
DR ChiTaRS; Sept9; mouse.
DR PRO; PR:Q80UG5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q80UG5; protein.
DR Bgee; ENSMUSG00000059248; Expressed in ectoplacental cone and 232 other tissues.
DR ExpressionAtlas; Q80UG5; baseline and differential.
DR Genevisible; Q80UG5; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005930; C:axoneme; ISO:MGI.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0097730; C:non-motile cilium; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0031105; C:septin complex; IDA:UniProtKB.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:1902857; P:positive regulation of non-motile cilium assembly; ISO:MGI.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR030645; SEPT9.
DR InterPro; IPR016491; Septin.
DR PANTHER; PTHR18884:SF47; PTHR18884:SF47; 1.
DR Pfam; PF00735; Septin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; GTP-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..583
FT /note="Septin-9"
FT /id="PRO_0000173536"
FT DOMAIN 293..565
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..310
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 360..363
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 442..445
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT COMPBIAS 204..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 303..310
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 443..451
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 499
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 514
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHD8"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 42
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHD8"
FT MOD_RES 49
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 62
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHD8"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHD8"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHD8"
FT MOD_RES 143
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 276
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHD8"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHD8"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHD8"
FT VAR_SEQ 1..249
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10666245,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_012341"
FT VAR_SEQ 1..25
FT /note="MKKSYSGVTRTSSGRLRRLADPTGP -> MSDPAVNAQLDGIISDFE (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_012342"
SQ SEQUENCE 583 AA; 65575 MW; 174D2F1E8EA382FC CRC64;
MKKSYSGVTR TSSGRLRRLA DPTGPALKRS FEVEEIEPPN STPPRRVQTP LLRATVASSS
QKFQDLGVKN SEPAARLVDS LSQRSPKPSL RRVELAGAKA PEPMSRRTEI SIDISSKQVE
STASAAGPSR FGLKRAEVLG HKTPEPVPRR TEITIVKPQE SVLRRVETPA SKIPEGSAVP
ATDAAPKRVE IQVPKPAEAP NCPLPSQTLE NSEAPMSQLQ SRLEPRPSVA EVPYRNQEDS
EVTPSCVGDM ADNPRDAMLK QAPASRNEKA PMEFGYVGID SILEQMRRKA MKQGFEFNIM
VVGQSGLGKS TLINTLFKSK ISRKSVQPTS EERIPKTIEI KSITHDIEEK GVRMKLTVID
TPGFGDHINN ENCWQPIMKF INDQYEKYLQ EEVNINRKKR IPDTRVHCCL YFIPATGHSL
RPLDIEFMKR LSKVVNIVPV IAKADTLTLE ERVYFKQRIT ADLLSNGIDV YPQKEFDEDA
EDRLVNEKFR EMIPFAVVGS DHEYQVNGKR ILGRKTKWGT IEVENTTHCE FAYLRDLLIR
THMQNIKDIT SNIHFEAYRV KRLNEGNSAM ANGIEKEPEA QEM
