PODXL_HUMAN
ID PODXL_HUMAN Reviewed; 558 AA.
AC O00592; A6NHX8; Q52LZ7; Q53ER6;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Podocalyxin;
DE AltName: Full=GCTM-2 antigen;
DE AltName: Full=Gp200;
DE AltName: Full=Podocalyxin-like protein 1;
DE Short=PC;
DE Short=PCLP-1;
DE Flags: Precursor;
GN Name=PODXL; Synonyms=PCLP, PCLP1;
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 [MRNA] (ISOFORM 2), AND VARIANT LEU-194.
RX PubMed=9188463; DOI=10.1074/jbc.272.25.15708;
RA Kershaw D.B., Beck S.G., Wharram B.L., Wiggins J.E., Goyal M., Thomas P.E.,
RA Wiggins R.C.;
RT "Molecular cloning and characterization of human podocalyxin-like protein.
RT Orthologous relationship to rabbit PCLP1 and rat podocalyxin.";
RL J. Biol. Chem. 272:15708-15714(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ILE-358.
RC TISSUE=Heart;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 120-310 (ISOFORM 1).
RA Suzuki Y., Yamashita R., Shirota M., Sakakibara Y., Chiba J., Nakai K.,
RA Sugano S.;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PROTEIN SEQUENCE OF 399-411 AND 445-372.
RX PubMed=12504081; DOI=10.1016/s0006-291x(02)02844-9;
RA Schopperle W.M., Kershaw D.B., DeWolf W.C.;
RT "Human embryonal carcinoma tumor antigen, Gp200/GCTM-2, is podocalyxin.";
RL Biochem. Biophys. Res. Commun. 300:285-290(2003).
RN [9]
RP FUNCTION, INTERACTION WITH EZR, AND SUBCELLULAR LOCATION.
RX PubMed=17616675; DOI=10.1158/0008-5472.can-06-3575;
RA Sizemore S., Cicek M., Sizemore N., Ng K.P., Casey G.;
RT "Podocalyxin increases the aggressive phenotype of breast and prostate
RT cancer cells in vitro through its interaction with ezrin.";
RL Cancer Res. 67:6183-6191(2007).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18456258; DOI=10.1016/j.yexcr.2008.03.009;
RA Larrucea S., Butta N., Arias-Salgado E.G., Alonso-Martin S., Ayuso M.S.,
RA Parrilla R.;
RT "Expression of podocalyxin enhances the adherence, migration, and
RT intercellular communication of cells.";
RL Exp. Cell Res. 314:2004-2015(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529 AND THR-556, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Involved in the regulation of both adhesion and cell
CC morphology and cancer progression. Functions as an anti-adhesive
CC molecule that maintains an open filtration pathway between neighboring
CC foot processes in the podocyte by charge repulsion. Acts as a pro-
CC adhesive molecule, enhancing the adherence of cells to immobilized
CC ligands, increasing the rate of migration and cell-cell contacts in an
CC integrin-dependent manner. Induces the formation of apical actin-
CC dependent microvilli. Involved in the formation of a preapical plasma
CC membrane subdomain to set up initial epithelial polarization and the
CC apical lumen formation during renal tubulogenesis. Plays a role in
CC cancer development and aggressiveness by inducing cell migration and
CC invasion through its interaction with the actin-binding protein EZR.
CC Affects EZR-dependent signaling events, leading to increased activities
CC of the MAPK and PI3K pathways in cancer cells.
CC {ECO:0000269|PubMed:17616675, ECO:0000269|PubMed:18456258}.
CC -!- SUBUNIT: Monomer; when associated with the membrane raft. Oligomer;
CC when integrated in the apical membrane. Interacts (via the C-terminal
CC PDZ-binding motif DTHL) with SLC9A3R1 (via the PDZ domains); the
CC interaction is not detected in glomerular epithelium cells, take place
CC early in the secretory pathway and is necessary for its apical membrane
CC sorting. Found in a complex with EZR, PODXL and SLC9A3R2. Associates
CC with the actin cytoskeleton through complex formation with EZR and
CC SLC9A3R2. Interacts (via the C-terminal PDZ-binding motif DTHL) with
CC SLC9A3R2 (via the PDZ 1 domain); interaction is detected in glomerular
CC epithelium cells (By similarity). Interacts with EZR. {ECO:0000250,
CC ECO:0000269|PubMed:17616675}.
CC -!- INTERACTION:
CC O00592; P46940: IQGAP1; NbExp=4; IntAct=EBI-6897823, EBI-297509;
CC O00592-2; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-12407415, EBI-744081;
CC O00592-2; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-12407415, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane. Cell projection,
CC lamellipodium. Cell projection, filopodium. Cell projection, ruffle.
CC Cell projection, microvillus {ECO:0000250}. Membrane raft
CC {ECO:0000250}. Membrane {ECO:0000305}; Single-pass type I membrane
CC protein {ECO:0000305}. Note=In single attached epithelial cells is
CC restricted to a preapical pole on the free plasma membrane whereas
CC other apical and basolateral proteins are not yet polarized.
CC Colocalizes with SLC9A3R2 at the apical plasma membrane during
CC epithelial polarization. Colocalizes with SLC9A3R1 at the trans-Golgi
CC network (transiently) and at the apical plasma membrane. Its
CC association with the membrane raft is transient. Colocalizes with actin
CC filaments, EZR and SLC9A3R1 in a punctate pattern at the apical cell
CC surface where microvilli form. Colocalizes with EZR and SLC9A3R2 at the
CC apical cell membrane of glomerular epithelium cells (By similarity).
CC Forms granular, punctuated pattern, forming patches, preferentially
CC adopting a polar distribution, located on the migrating poles of the
CC cell or forming clusters along the terminal ends of filipodia
CC establishing contact with the endothelial cells. Colocalizes with the
CC submembrane actin of lamellipodia, particularly associated with
CC ruffles. Colocalizes with vinculin at protrusions of cells. Colocalizes
CC with ITGB1. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, RAB11A and
CC RAB8A in apical membrane initiation sites (AMIS) during the generation
CC of apical surface and luminogenesis (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00592-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00592-2; Sequence=VSP_037220;
CC -!- TISSUE SPECIFICITY: Glomerular epithelium cell (podocyte).
CC -!- DOMAIN: Both the O-glycan-rich domain of the extracellular domain and
CC the C-terminus PDZ-binding motif (DTHL) in the cytoplasmic tail harbor
CC an apical sorting signal. The cytoplasmic domain is necessary for the
CC apical membrane targeting and renal tubulogenesis. The cytoplasmic C-
CC terminus PDZ-binding motif (DTHL) is essential for interaction with
CC SLC9A3R1 and for targeting SLC9A3R1 to the apical cell membrane. The
CC extracellular domain is necessary for microvillus formation (By
CC similarity). The large highly anionic extracellular domain allows to
CC maintain open filtration pathways between neighboring podocyte foot
CC processes. {ECO:0000250}.
CC -!- PTM: N- and O-linked glycosylated. Sialoglycoprotein (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the podocalyxin family. {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; U97519; AAB61574.1; -; mRNA.
DR EMBL; AK223573; BAD97293.1; -; mRNA.
DR EMBL; AC008264; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236950; EAL24080.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83786.1; -; Genomic_DNA.
DR EMBL; BC093730; AAH93730.1; -; mRNA.
DR EMBL; BC112035; AAI12036.1; -; mRNA.
DR EMBL; BP234810; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS34755.1; -. [O00592-1]
DR CCDS; CCDS47714.1; -. [O00592-2]
DR RefSeq; NP_001018121.1; NM_001018111.2. [O00592-1]
DR RefSeq; NP_005388.2; NM_005397.3. [O00592-2]
DR AlphaFoldDB; O00592; -.
DR BioGRID; 111416; 65.
DR CORUM; O00592; -.
DR DIP; DIP-58638N; -.
DR IntAct; O00592; 20.
DR STRING; 9606.ENSP00000367817; -.
DR TCDB; 8.A.187.1.1; the podocalyxin (podxl) family.
DR GlyConnect; 1617; 22 N-Linked glycans (2 sites).
DR GlyGen; O00592; 14 sites, 21 N-linked glycans (2 sites), 7 O-linked glycans (8 sites).
DR iPTMnet; O00592; -.
DR PhosphoSitePlus; O00592; -.
DR SwissPalm; O00592; -.
DR BioMuta; PODXL; -.
DR EPD; O00592; -.
DR jPOST; O00592; -.
DR MassIVE; O00592; -.
DR MaxQB; O00592; -.
DR PaxDb; O00592; -.
DR PeptideAtlas; O00592; -.
DR PRIDE; O00592; -.
DR ProteomicsDB; 47992; -. [O00592-1]
DR ProteomicsDB; 47993; -. [O00592-2]
DR ABCD; O00592; 2 sequenced antibodies.
DR Antibodypedia; 971; 1211 antibodies from 45 providers.
DR DNASU; 5420; -.
DR Ensembl; ENST00000322985.9; ENSP00000319782.9; ENSG00000128567.17. [O00592-2]
DR Ensembl; ENST00000378555.8; ENSP00000367817.3; ENSG00000128567.17. [O00592-1]
DR GeneID; 5420; -.
DR KEGG; hsa:5420; -.
DR MANE-Select; ENST00000378555.8; ENSP00000367817.3; NM_001018111.3; NP_001018121.1.
DR UCSC; uc003vqw.5; human. [O00592-1]
DR CTD; 5420; -.
DR DisGeNET; 5420; -.
DR GeneCards; PODXL; -.
DR HGNC; HGNC:9171; PODXL.
DR HPA; ENSG00000128567; Tissue enhanced (kidney).
DR MalaCards; PODXL; -.
DR MIM; 602632; gene.
DR neXtProt; NX_O00592; -.
DR OpenTargets; ENSG00000128567; -.
DR Orphanet; 391411; Atypical juvenile parkinsonism.
DR Orphanet; 2828; Young-onset Parkinson disease.
DR PharmGKB; PA33493; -.
DR VEuPathDB; HostDB:ENSG00000128567; -.
DR eggNOG; ENOG502S2JU; Eukaryota.
DR GeneTree; ENSGT00730000111314; -.
DR HOGENOM; CLU_032485_0_0_1; -.
DR InParanoid; O00592; -.
DR OMA; NWTKCEA; -.
DR PhylomeDB; O00592; -.
DR TreeFam; TF333564; -.
DR PathwayCommons; O00592; -.
DR SignaLink; O00592; -.
DR SIGNOR; O00592; -.
DR BioGRID-ORCS; 5420; 12 hits in 1067 CRISPR screens.
DR ChiTaRS; PODXL; human.
DR GeneWiki; PODXL; -.
DR GenomeRNAi; 5420; -.
DR Pharos; O00592; Tbio.
DR PRO; PR:O00592; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O00592; protein.
DR Bgee; ENSG00000128567; Expressed in renal glomerulus and 196 other tissues.
DR ExpressionAtlas; O00592; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0031528; C:microvillus membrane; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0036057; C:slit diaphragm; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0072175; P:epithelial tube formation; ISS:UniProtKB.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0072015; P:podocyte development; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0033634; P:positive regulation of cell-cell adhesion mediated by integrin; IDA:UniProtKB.
DR GO; GO:0032534; P:regulation of microvillus assembly; ISS:UniProtKB.
DR InterPro; IPR013836; CD34/Podocalyxin.
DR InterPro; IPR017403; PODXL.
DR PANTHER; PTHR12067; PTHR12067; 1.
DR Pfam; PF06365; CD34_antigen; 1.
DR PIRSF; PIRSF038143; Podocalyxin-like_p1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Cell projection;
KW Direct protein sequencing; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..558
FT /note="Podocalyxin"
FT /id="PRO_0000024754"
FT TOPO_DOM 23..461
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 483..558
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 20..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 518
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0M4"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 556
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 236..268
FT /note="LETVFHHVSQAGLELLTSGDLPTLASQSAGITA -> P (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9188463, ECO:0000303|Ref.2"
FT /id="VSP_037220"
FT VARIANT 60
FT /note="T -> R"
FT /id="VAR_012236"
FT VARIANT 112
FT /note="G -> S (in dbSNP:rs3735035)"
FT /id="VAR_055237"
FT VARIANT 126
FT /note="T -> P (in dbSNP:rs55698400)"
FT /id="VAR_062136"
FT VARIANT 194
FT /note="S -> L (in dbSNP:rs12670788)"
FT /evidence="ECO:0000269|PubMed:9188463"
FT /id="VAR_012237"
FT VARIANT 298
FT /note="P -> A (in dbSNP:rs35893129)"
FT /id="VAR_060090"
FT VARIANT 358
FT /note="V -> I (in dbSNP:rs3212298)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_055238"
FT CONFLICT 31
FT /note="S -> SPS (in Ref. 1; AAB61574)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="G -> Q (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 558 AA; 58635 MW; 8B1CF30D14D51691 CRC64;
MRCALALSAL LLLLSTPPLL PSSPSPSPSP SQNATQTTTD SSNKTAPTPA SSVTIMATDT
AQQSTVPTSK ANEILASVKA TTLGVSSDSP GTTTLAQQVS GPVNTTVARG GGSGNPTTTI
ESPKSTKSAD TTTVATSTAT AKPNTTSSQN GAEDTTNSGG KSSHSVTTDL TSTKAEHLTT
PHPTSPLSPR QPTSTHPVAT PTSSGHDHLM KISSSSSTVA IPGYTFTSPG MTTTLLETVF
HHVSQAGLEL LTSGDLPTLA SQSAGITASS VISQRTQQTS SQMPASSTAP SSQETVQPTS
PATALRTPTL PETMSSSPTA ASTTHRYPKT PSPTVAHESN WAKCEDLETQ TQSEKQLVLN
LTGNTLCAGG ASDEKLISLI CRAVKATFNP AQDKCGIRLA SVPGSQTVVV KEITIHTKLP
AKDVYERLKD KWDELKEAGV SDMKLGDQGP PEEAEDRFSM PLIITIVCMA SFLLLVAALY
GCCHQRLSQR KDQQRLTEEL QTVENGYHDN PTLEVMETSS EMQEKKVVSL NGELGDSWIV
PLDNLTKDDL DEEEDTHL
