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 13-FEB-2019, entry version 144. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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., RA Thomas P.E., Wiggins R.C.; RT "Molecular cloning and characterization of human podocalyxin-like RT protein. Orthologous relationship to rabbit PCLP1 and rat RT podocalyxin."; RL J. Biol. Chem. 272:15708-15714(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT RP 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., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA 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., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., 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., RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., RA 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., RA Mural R.J., 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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., RA Nakai K., 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 RT 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., RA Ayuso M.S., 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 RP BY 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation 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., RA Buerckstuemmer T., 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., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome 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., RA Ayoub D., 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. Function as an anti-adhesive CC molecule that maintains an open filtration pathway between CC neighboring foot processes in the podocyte by charge repulsion. CC Acts as a pro-adhesive molecule, enhancing the adherence of cells CC to immobilized ligands, increasing the rate of migration and cell- CC cell contacts in an integrin-dependent manner. Induces the CC formation of apical actin-dependent microvilli. Involved in the CC formation of a preapical plasma membrane subdomain to set up CC initial epithelial polarization and the apical lumen formation CC during renal tubulogenesis. Plays a role in cancer development and CC aggressiveness by inducing cell migration and invasion through its CC interaction with the actin-binding protein EZR. Affects EZR- CC dependent signaling events, leading to increased activities of the CC 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. CC Oligomer; when integrated in the apical membrane. Interacts (via CC the C-terminal PDZ-binding motif DTHL) with SLC9A3R1 (via the PDZ CC domains); the interaction is not detected in glomerular epithelium CC cells, take place early in the secretory pathway and is necessary CC for its apical membrane sorting. Found in a complex with EZR, CC PODXL and SLC9A3R2. Associates with the actin cytoskeleton through CC complex formation with EZR and SLC9A3R2. Interacts (via the C- CC terminal PDZ-binding motif DTHL) with SLC9A3R2 (via the PDZ 1 CC domain); interaction is detected in glomerular epithelium cells CC (By similarity). Interacts with EZR. {ECO:0000250, CC ECO:0000269|PubMed:17616675}. CC -!- INTERACTION: CC P46940:IQGAP1; NbExp=4; IntAct=EBI-6897823, EBI-297509; CC -!- SUBCELLULAR LOCATION: Apical cell membrane. Cell projection, CC lamellipodium. Cell projection, filopodium. Cell projection, CC ruffle. 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- CC Golgi network (transiently) and at the apical plasma membrane. Its CC association with the membrane raft is transient. Colocalizes with CC actin filaments, EZR and SLC9A3R1 in a punctate pattern at the CC apical cell surface where microvilli form. Colocalizes with EZR CC and SLC9A3R2 at the apical cell membrane of glomerular epithelium CC cells (By similarity). Forms granular, punctuated pattern, forming CC patches, preferentially adopting a polar distribution, located on CC the migrating poles of the cell or forming clusters along the CC terminal ends of filipodia establishing contact with the CC endothelial cells. Colocalizes with the submembrane actin of CC lamellipodia, particularly associated with ruffles. Colocalizes CC with vinculin at protrusions of cells. Colocalizes with ITGB1. CC Colocalizes with PARD3, PRKCI, EXOC5, OCLN, RAB11A and RAB8A in CC apical membrane initiation sites (AMIS) during the generation of CC 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 CC and the C-terminus PDZ-binding motif (DTHL) in the cytoplasmic CC tail harbor an apical sorting signal. The cytoplasmic domain is CC necessary for the apical membrane targeting and renal CC tubulogenesis. The cytoplasmic C-terminus PDZ-binding motif (DTHL) CC is essential for interaction with SLC9A3R1 and for targeting CC SLC9A3R1 to the apical cell membrane. The extracellular domain is CC necessary for microvillus formation (By similarity). The large CC highly anionic extracellular domain allows to maintain open CC filtration pathways between neighboring podocyte foot processes. CC {ECO:0000250}. CC -!- PTM: N- and O-linked glycosylated. Sialoglycoprotein (By CC similarity). {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 UniGene; Hs.744213; -. DR ProteinModelPortal; O00592; -. DR SMR; O00592; -. DR BioGrid; 111416; 23. DR CORUM; O00592; -. DR DIP; DIP-58638N; -. DR IntAct; O00592; 7. DR STRING; 9606.ENSP00000367817; -. DR GlyConnect; 1617; -. DR iPTMnet; O00592; -. DR PhosphoSitePlus; O00592; -. DR SwissPalm; O00592; -. DR BioMuta; PODXL; -. DR EPD; O00592; -. DR jPOST; O00592; -. DR MaxQB; O00592; -. DR PaxDb; O00592; -. DR PeptideAtlas; O00592; -. DR PRIDE; O00592; -. DR ProteomicsDB; 47992; -. DR ProteomicsDB; 47993; -. [O00592-2] DR Ensembl; ENST00000322985; ENSP00000319782; ENSG00000128567. [O00592-2] DR Ensembl; ENST00000378555; ENSP00000367817; ENSG00000128567. [O00592-1] DR GeneID; 5420; -. DR KEGG; hsa:5420; -. DR UCSC; uc003vqw.5; human. [O00592-1] DR CTD; 5420; -. DR DisGeNET; 5420; -. DR EuPathDB; HostDB:ENSG00000128567.16; -. DR GeneCards; PODXL; -. DR H-InvDB; HIX0007089; -. DR HGNC; HGNC:9171; PODXL. DR HPA; CAB016169; -. DR HPA; CAB062558; -. DR HPA; CAB068219; -. DR HPA; CAB068220; -. DR HPA; HPA002110; -. DR HPA; HPA045507; -. 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 eggNOG; ENOG410IFKB; Eukaryota. DR eggNOG; ENOG410YCG4; LUCA. DR GeneTree; ENSGT00730000111314; -. DR HOVERGEN; HBG053629; -. DR InParanoid; O00592; -. DR KO; K06817; -. DR OMA; QDECSIR; -. DR OrthoDB; 1404598at2759; -. DR PhylomeDB; O00592; -. DR TreeFam; TF333564; -. DR SIGNOR; O00592; -. DR ChiTaRS; PODXL; human. DR GeneWiki; PODXL; -. DR GenomeRNAi; 5420; -. DR PRO; PR:O00592; -. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; ENSG00000128567; Expressed in 225 organ(s), highest expression level in metanephric glomerulus. DR ExpressionAtlas; O00592; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB. 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:0005815; C:microtubule organizing center; IDA:HPA. 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:0072015; P:glomerular visceral epithelial cell development; 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: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 Complete proteome; Direct protein sequencing; Glycoprotein; Membrane; KW Phosphoprotein; Polymorphism; Reference proteome; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 22 {ECO:0000255}. FT CHAIN 23 558 Podocalyxin. FT /FTId=PRO_0000024754. FT TOPO_DOM 23 461 Extracellular. {ECO:0000255}. FT TRANSMEM 462 482 Helical. {ECO:0000255}. FT TOPO_DOM 483 558 Cytoplasmic. {ECO:0000255}. FT COMPBIAS 35 334 Thr-rich. FT MOD_RES 518 518 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q9R0M4}. FT MOD_RES 529 529 Phosphoserine. FT {ECO:0000244|PubMed:21406692}. FT MOD_RES 537 537 Phosphoserine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 556 556 Phosphothreonine. FT {ECO:0000244|PubMed:21406692}. FT CARBOHYD 33 33 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 43 43 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 104 104 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 144 144 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 360 360 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT VAR_SEQ 236 268 LETVFHHVSQAGLELLTSGDLPTLASQSAGITA -> P FT (in isoform 2). FT {ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9188463, FT ECO:0000303|Ref.2}. FT /FTId=VSP_037220. FT VARIANT 60 60 T -> R. FT /FTId=VAR_012236. FT VARIANT 112 112 G -> S (in dbSNP:rs3735035). FT /FTId=VAR_055237. FT VARIANT 126 126 T -> P (in dbSNP:rs55698400). FT /FTId=VAR_062136. FT VARIANT 194 194 S -> L (in dbSNP:rs12670788). FT {ECO:0000269|PubMed:9188463}. FT /FTId=VAR_012237. FT VARIANT 298 298 P -> A (in dbSNP:rs35893129). FT /FTId=VAR_060090. FT VARIANT 358 358 V -> I (in dbSNP:rs3212298). FT {ECO:0000269|Ref.2}. FT /FTId=VAR_055238. FT CONFLICT 31 31 S -> SPS (in Ref. 1; AAB61574). FT {ECO:0000305}. FT CONFLICT 404 404 G -> Q (in Ref. 8; AA sequence). FT {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 //