PDXL2_MOUSE
ID PDXL2_MOUSE Reviewed; 603 AA.
AC Q8CAE9; Q8CFW3;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Podocalyxin-like protein 2;
DE AltName: Full=Endoglycan;
DE Flags: Precursor;
GN Name=Podxl2;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Eye;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: Acts as a ligand for vascular selectins. Mediates rapid
CC rolling of leukocytes over vascular surfaces through high affinity
CC divalent cation-dependent interactions with E-, P- and L-selectins (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with SELL, SELE and
CC SELP (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8CAE9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CAE9-2; Sequence=VSP_020878, VSP_020879;
CC Name=3;
CC IsoId=Q8CAE9-3; Sequence=VSP_020877;
CC -!- PTM: Glycosylated; contains chondroitin sulfate. Displays sialylated O-
CC linked oligosaccharides (By similarity). {ECO:0000250}.
CC -!- PTM: Sulfation is necessary for interaction with SELL. Sialylated O-
CC linked oligosaccharides are necessary for interaction with SELL, SELE
CC and SELP (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the podocalyxin family. {ECO:0000305}.
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DR EMBL; AK038943; BAC30176.1; -; mRNA.
DR EMBL; AC153923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033384; AAH33384.1; -; mRNA.
DR CCDS; CCDS20340.1; -. [Q8CAE9-3]
DR CCDS; CCDS85093.1; -. [Q8CAE9-1]
DR RefSeq; NP_795947.3; NM_176973.4.
DR AlphaFoldDB; Q8CAE9; -.
DR IntAct; Q8CAE9; 1.
DR MINT; Q8CAE9; -.
DR STRING; 10090.ENSMUSP00000040417; -.
DR GlyGen; Q8CAE9; 3 sites.
DR iPTMnet; Q8CAE9; -.
DR PhosphoSitePlus; Q8CAE9; -.
DR MaxQB; Q8CAE9; -.
DR PaxDb; Q8CAE9; -.
DR PRIDE; Q8CAE9; -.
DR ProteomicsDB; 288116; -. [Q8CAE9-1]
DR ProteomicsDB; 288118; -. [Q8CAE9-3]
DR DNASU; 319655; -.
DR GeneID; 319655; -.
DR KEGG; mmu:319655; -.
DR UCSC; uc009cvw.1; mouse. [Q8CAE9-2]
DR CTD; 50512; -.
DR MGI; MGI:2442488; Podxl2.
DR eggNOG; ENOG502QTNA; Eukaryota.
DR InParanoid; Q8CAE9; -.
DR OrthoDB; 1103853at2759; -.
DR PhylomeDB; Q8CAE9; -.
DR Reactome; R-MMU-156584; Cytosolic sulfonation of small molecules.
DR BioGRID-ORCS; 319655; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Podxl2; mouse.
DR PRO; PR:Q8CAE9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8CAE9; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050901; P:leukocyte tethering or rolling; ISS:UniProtKB.
DR InterPro; IPR013836; CD34/Podocalyxin.
DR InterPro; IPR042397; PODXL2.
DR PANTHER; PTHR15594; PTHR15594; 1.
DR Pfam; PF06365; CD34_antigen; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Disulfide bond; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Sialic acid; Signal;
KW Sulfation; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..603
FT /note="Podocalyxin-like protein 2"
FT /id="PRO_0000252130"
FT TOPO_DOM 29..499
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 521..603
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 53..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..188
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 93
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 113
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ53"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..64
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020877"
FT VAR_SEQ 112..131
FT /note="DYVFPDLTEKVASMEDPGQA -> GSSAHLPLHRISGVIHGEGP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020878"
FT VAR_SEQ 132..603
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020879"
SQ SEQUENCE 603 AA; 64973 MW; 1FF3CF9472E1BCE3 CRC64;
MARPLRAARL PPPLLLLLAA GASLGAYAVG VDEPGPEGLT STSLLDLLLP TDFEPLDSEE
PSEAMGLDAG LAPGSGFPSE DSEESRLLQP PQYFWEEEEL NGSSLDLGPT ADYVFPDLTE
KVASMEDPGQ APDLPNLPSI LPKMDLAEPP WHMPLQEEEE EEEEEEEERE EEEREKEAEE
EEEEEELLPV SGSPGATAQA HAPSPSTSSS TSSQSPGATR HRQEDSGDQA TSGMEVESSV
KPTLSVPSVT PSTVAPGVQN YSQESGGTEW PTGGLGVQSE VPQGAGEGAT VGAADFDGQQ
GALPSSSLPQ TVPPSGTEVP SEGPLYPRIP DSLPPGPQDT ESTPSSATWG QEGLSEQPLE
GQAAEAHSLT PWDSTQVICK DWSNLAGKSY IILNMTQNID CEVFRRHRGL RLLALVEEVL
PRHRSGHRGD WHISLSKPSE KEQHLLMTLV GEQGVVPTQD VLSMLSGIRR SLEEIGIQNY
STTSSCQARA TQVRSDYGTL FVVLVIIGVI CFIIIVLGLL YNCWQRRMPK LKHVSHGEEL
RFVENGCHDN PTLDVASDSQ SEMQEKQPSL NGGAINGPSS WSALMGSKRD PEDSDVFEED
THL
