LEUK_HUMAN
ID LEUK_HUMAN Reviewed; 400 AA.
AC P16150; A8K9B1;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Leukosialin;
DE AltName: Full=GPL115 {ECO:0000303|PubMed:3711098};
DE AltName: Full=Galactoglycoprotein;
DE Short=GALGP;
DE AltName: Full=Leukocyte sialoglycoprotein;
DE AltName: Full=Sialophorin;
DE AltName: CD_antigen=CD43;
DE Contains:
DE RecName: Full=CD43 cytoplasmic tail {ECO:0000303|PubMed:15540986};
DE Short=CD43-ct {ECO:0000303|PubMed:15540986};
DE Short=CD43ct {ECO:0000303|PubMed:15540986};
DE Flags: Precursor;
GN Name=SPN; Synonyms=CD43;
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].
RX PubMed=2521952; DOI=10.1073/pnas.86.4.1328;
RA Pallant A., Eskenazi A., Mattei M.-G., Fournier R.E.K., Carlsson S.R.,
RA Fukuda M., Frelinger J.G.;
RT "Characterization of cDNAs encoding human leukosialin and localization of
RT the leukosialin gene to chromosome 16.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:1328-1332(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2784859; DOI=10.1073/pnas.86.8.2819;
RA Shelley C.S., Remold-O'Donnell E., Davis A.E. III, Bruns G.A.P.,
RA Rosen F.S., Carroll M.C., Whitehead D.A.S.;
RT "Molecular characterization of sialophorin (CD43), the lymphocyte surface
RT sialoglycoprotein defective in Wiskott-Aldrich syndrome.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:2819-2823(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2241892; DOI=10.1042/bj2700569;
RA Shelley C.S., Remold-O'Donnell E., Rosen F.S., Whitehead D.A.S.;
RT "Structure of the human sialophorin (CD43) gene. Identification of features
RT atypical of genes encoding integral membrane proteins.";
RL Biochem. J. 270:569-576(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1827122; DOI=10.1016/s0021-9258(18)93000-0;
RA Kudo S., Fukuda M.;
RT "A short, novel promoter sequence confers the expression of human
RT leukosialin, a major sialoglycoprotein on leukocytes.";
RL J. Biol. Chem. 266:8483-8489(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 20-245, AND GLYCOSYLATION AT THR-21; THR-22; THR-26;
RP THR-28; SER-29; SER-35; THR-36; SER-37; SER-41; SER-42; THR-46; THR-47;
RP SER-48; THR-50; THR-58; THR-69; SER-99; SER-103; THR-109; THR-113; SER-114;
RP THR-136; THR-137; THR-173; THR-178 AND ASN-239.
RX PubMed=1731338; DOI=10.1073/pnas.89.2.663;
RA Schmid K., Hediger M.A., Brossmer R., Collins J.H., Haupt H., Marti T.,
RA Offner G.D., Schaller J., Takagaki K., Walsh M.T., Schwick H.G., Rose F.S.,
RA Remold-O'Donnell E.;
RT "Amino acid sequence of human plasma galactoglycoprotein: identity with the
RT extracellular region of CD43 (sialophorin).";
RL Proc. Natl. Acad. Sci. U.S.A. 89:663-667(1992).
RN [9]
RP CHARACTERIZATION.
RX PubMed=3711098; DOI=10.1016/s0021-9258(17)38423-5;
RA Remold-O'Donnell E., Davis A.E. III, Kenney D., Bhaskar K.R., Rosen F.S.;
RT "Purification and chemical composition of gpL115, the human lymphocyte
RT surface sialoglycoprotein that is defective in Wiskott-Aldrich syndrome.";
RL J. Biol. Chem. 261:7526-7530(1986).
RN [10]
RP PHOSPHORYLATION AT SER-291 AND SER-351.
RX PubMed=2530225; DOI=10.1016/s0021-9258(18)51541-6;
RA Piller V., Piller F., Fukuda M.;
RT "Phosphorylation of the major leukocyte surface sialoglycoprotein,
RT leukosialin, is increased by phorbol 12-myristate 13-acetate.";
RL J. Biol. Chem. 264:18824-18831(1989).
RN [11]
RP SUBCELLULAR LOCATION, INTERACTION WITH CTNNB1, NUCLEAR LOCALIZATION SIGNAL,
RP AND MUTAGENESIS OF 282-LYS-ARG-283 AND 295-LYS-ARG-296.
RX PubMed=15003504; DOI=10.1016/j.bbrc.2004.02.011;
RA Andersson C.X., Fernandez-Rodriguez J., Laos S., Sikut R., Sikut A.,
RA Baeckstroem D., Hansson G.C.;
RT "CD43 has a functional NLS, interacts with beta-catenin, and affects gene
RT expression.";
RL Biochem. Biophys. Res. Commun. 316:12-17(2004).
RN [12]
RP PROTEOLYTIC PROCESSING.
RX PubMed=15540986; DOI=10.1042/bj20041387;
RA Andersson C.X., Fernandez-Rodriguez J., Laos S., Baeckstroem D., Haass C.,
RA Hansson G.C.;
RT "Shedding and gamma-secretase-mediated intramembrane proteolysis of the
RT mucin-type molecule CD43.";
RL Biochem. J. 387:377-384(2005).
RN [13]
RP FUNCTION.
RX PubMed=18036228; DOI=10.1186/1471-2172-8-30;
RA Ramirez-Pliego O., Escobar-Zarate D.L., Rivera-Martinez G.M.,
RA Cervantes-Badillo M.G., Esquivel-Guadarrama F.R., Rosas-Salgado G.,
RA Rosenstein Y., Santana M.A.;
RT "CD43 signals induce type one lineage commitment of human CD4+ T cells.";
RL BMC Immunol. 8:30-30(2007).
RN [14]
RP PROTEOLYTIC PROCESSING.
RX PubMed=18586676; DOI=10.1074/jbc.m710286200;
RA Mambole A., Baruch D., Nusbaum P., Bigot S., Suzuki M., Lesavre P.,
RA Fukuda M., Halbwachs-Mecarelli L.;
RT "The cleavage of neutrophil leukosialin (CD43) by cathepsin G releases its
RT extracellular domain and triggers its intramembrane proteolysis by
RT presenilin/gamma-secretase.";
RL J. Biol. Chem. 283:23627-23635(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291; SER-336; THR-341;
RP SER-351 AND SER-355, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP FUNCTION.
RX PubMed=24328034; DOI=10.1002/jcp.24430;
RA Galindo-Albarran A.O., Ramirez-Pliego O., Labastida-Conde R.G.,
RA Melchy-Perez E.I., Liquitaya-Montiel A., Esquivel-Guadarrama F.R.,
RA Rosas-Salgado G., Rosenstein Y., Santana M.A.;
RT "CD43 signals prepare human T cells to receive cytokine differentiation
RT signals.";
RL J. Cell. Physiol. 229:172-180(2014).
RN [21]
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: Predominant cell surface sialoprotein of leukocytes which
CC regulates multiple T-cell functions, including T-cell activation,
CC proliferation, differentiation, trafficking and migration. Positively
CC regulates T-cell trafficking to lymph-nodes via its association with
CC ERM proteins (EZR, RDX and MSN) (By similarity). Negatively regulates
CC Th2 cell differentiation and predisposes the differentiation of T-cells
CC towards a Th1 lineage commitment. Promotes the expression of IFN-gamma
CC by T-cells during T-cell receptor (TCR) activation of naive cells and
CC induces the expression of IFN-gamma by CD4(+) T-cells and to a lesser
CC extent by CD8(+) T-cells (PubMed:18036228). Plays a role in preparing
CC T-cells for cytokine sensing and differentiation into effector cells by
CC inducing the expression of cytokine receptors IFNGR and IL4R, promoting
CC IFNGR and IL4R signaling and by mediating the clustering of IFNGR with
CC TCR (PubMed:24328034). Acts as a major E-selectin ligand responsible
CC for Th17 cell rolling on activated vasculature and recruitment during
CC inflammation. Mediates Th17 cells, but not Th1 cells, adhesion to E-
CC selectin. Acts as a T-cell counter-receptor for SIGLEC1 (By
CC similarity). {ECO:0000250|UniProtKB:P15702,
CC ECO:0000269|PubMed:18036228, ECO:0000269|PubMed:24328034}.
CC -!- FUNCTION: [CD43 cytoplasmic tail]: Protects cells from apoptotic
CC signals, promoting cell survival. {ECO:0000250|UniProtKB:P15702}.
CC -!- SUBUNIT: Interacts with SIGLEC1. {ECO:0000250|UniProtKB:P15702}.
CC -!- SUBUNIT: [CD43 cytoplasmic tail]: Monomer (By similarity). Interacts
CC with CTNNB1 (PubMed:15003504). Interacts with RDX (via FERM domain),
CC EZR and MSN (By similarity). {ECO:0000250|UniProtKB:P13838,
CC ECO:0000250|UniProtKB:P15702, ECO:0000269|PubMed:15003504}.
CC -!- INTERACTION:
CC P16150; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-10049055, EBI-11343438;
CC P16150; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-10049055, EBI-2680384;
CC P16150; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-10049055, EBI-781551;
CC P16150; Q04941: PLP2; NbExp=3; IntAct=EBI-10049055, EBI-608347;
CC P16150; Q59EV6: PPGB; NbExp=3; IntAct=EBI-10049055, EBI-14210385;
CC P16150; O43765: SGTA; NbExp=5; IntAct=EBI-10049055, EBI-347996;
CC P16150; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-10049055, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}. Cell projection, microvillus
CC {ECO:0000250|UniProtKB:P13838}. Cell projection, uropodium
CC {ECO:0000250|UniProtKB:P15702}. Note=Localizes to the uropodium and
CC microvilli via its interaction with ERM proteins (EZR, RDX and MSN).
CC {ECO:0000250|UniProtKB:P13838, ECO:0000250|UniProtKB:P15702}.
CC -!- SUBCELLULAR LOCATION: [CD43 cytoplasmic tail]: Nucleus
CC {ECO:0000269|PubMed:15003504}. Nucleus, PML body
CC {ECO:0000250|UniProtKB:P15702}. Note=The sumoylated form localizes to
CC the PML body. {ECO:0000250|UniProtKB:P15702}.
CC -!- TISSUE SPECIFICITY: Cell surface of thymocytes, T-lymphocytes,
CC neutrophils, plasma cells and myelomas.
CC -!- PTM: Glycosylated; has a high content of sialic acid and O-linked
CC carbohydrate structures. {ECO:0000269|PubMed:1731338}.
CC -!- PTM: Phosphorylation at Ser-355 is regulated by chemokines, requires
CC its association with ERM proteins (EZR, RDX and MSN) and is essential
CC for its function in the regulation of T-cell trafficking to lymph
CC nodes. {ECO:0000250|UniProtKB:P15702}.
CC -!- PTM: Has a high content of sialic acid and O-linked carbohydrate
CC structures.
CC -!- PTM: Cleavage by CTSG releases its extracellular domain and triggers
CC its intramembrane proteolysis by gamma-secretase releasing the CD43
CC cytoplasmic tail chain (CD43-ct) which translocates to the nucleus.
CC {ECO:0000269|PubMed:15540986, ECO:0000269|PubMed:18586676}.
CC -!- PTM: [CD43 cytoplasmic tail]: Sumoylated.
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DR EMBL; J04168; AAA59510.1; -; mRNA.
DR EMBL; J04536; AAB59540.1; -; mRNA.
DR EMBL; X52075; CAA36294.1; -; Genomic_DNA.
DR EMBL; M61827; AAA51949.1; -; Genomic_DNA.
DR EMBL; AK292626; BAF85315.1; -; mRNA.
DR EMBL; AK313750; BAG36490.1; -; mRNA.
DR EMBL; CH471238; EAW80015.1; -; Genomic_DNA.
DR EMBL; BC012350; AAH12350.1; -; mRNA.
DR CCDS; CCDS10650.1; -.
DR PIR; A39822; A39822.
DR RefSeq; NP_001025459.1; NM_001030288.2.
DR RefSeq; NP_003114.1; NM_003123.4.
DR AlphaFoldDB; P16150; -.
DR BioGRID; 112571; 53.
DR CORUM; P16150; -.
DR IntAct; P16150; 11.
DR STRING; 9606.ENSP00000353238; -.
DR GlyConnect; 340; 11 O-Linked glycans.
DR GlyGen; P16150; 30 sites, 17 O-linked glycans (29 sites).
DR iPTMnet; P16150; -.
DR PhosphoSitePlus; P16150; -.
DR BioMuta; SPN; -.
DR DMDM; 126213; -.
DR EPD; P16150; -.
DR jPOST; P16150; -.
DR MassIVE; P16150; -.
DR MaxQB; P16150; -.
DR PaxDb; P16150; -.
DR PeptideAtlas; P16150; -.
DR PRIDE; P16150; -.
DR ProteomicsDB; 53297; -.
DR Antibodypedia; 3627; 2231 antibodies from 46 providers.
DR DNASU; 6693; -.
DR Ensembl; ENST00000360121.4; ENSP00000353238.3; ENSG00000197471.12.
DR Ensembl; ENST00000395389.2; ENSP00000378787.2; ENSG00000197471.12.
DR Ensembl; ENST00000563039.2; ENSP00000455266.1; ENSG00000197471.12.
DR Ensembl; ENST00000652691.1; ENSP00000498852.1; ENSG00000197471.12.
DR GeneID; 6693; -.
DR KEGG; hsa:6693; -.
DR MANE-Select; ENST00000652691.1; ENSP00000498852.1; NM_003123.6; NP_003114.1.
DR UCSC; uc002dtm.5; human.
DR CTD; 6693; -.
DR DisGeNET; 6693; -.
DR GeneCards; SPN; -.
DR HGNC; HGNC:11249; SPN.
DR HPA; ENSG00000197471; Group enriched (bone marrow, lung, lymphoid tissue).
DR MIM; 182160; gene.
DR neXtProt; NX_P16150; -.
DR OpenTargets; ENSG00000197471; -.
DR PharmGKB; PA36079; -.
DR VEuPathDB; HostDB:ENSG00000197471; -.
DR eggNOG; ENOG502SBHY; Eukaryota.
DR GeneTree; ENSGT00390000017626; -.
DR HOGENOM; CLU_038831_0_1_1; -.
DR InParanoid; P16150; -.
DR OMA; GVSVMKP; -.
DR OrthoDB; 1178463at2759; -.
DR PhylomeDB; P16150; -.
DR TreeFam; TF337688; -.
DR PathwayCommons; P16150; -.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-210991; Basigin interactions.
DR SignaLink; P16150; -.
DR BioGRID-ORCS; 6693; 17 hits in 1074 CRISPR screens.
DR ChiTaRS; SPN; human.
DR GeneWiki; CD43; -.
DR GenomeRNAi; 6693; -.
DR Pharos; P16150; Tbio.
DR PRO; PR:P16150; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P16150; protein.
DR Bgee; ENSG00000197471; Expressed in buccal mucosa cell and 183 other tissues.
DR ExpressionAtlas; P16150; baseline and differential.
DR Genevisible; P16150; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0001931; C:uropod; ISS:UniProtKB.
DR GO; GO:0031072; F:heat shock protein binding; IPI:CAFA.
DR GO; GO:0030544; F:Hsp70 protein binding; IPI:CAFA.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
DR GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
DR GO; GO:0042742; P:defense response to bacterium; IDA:MGI.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; TAS:ProtInc.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0050901; P:leukocyte tethering or rolling; ISS:UniProtKB.
DR GO; GO:0007162; P:negative regulation of cell adhesion; TAS:ProtInc.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISS:UniProtKB.
DR GO; GO:2000406; P:positive regulation of T cell migration; ISS:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:MGI.
DR GO; GO:0050776; P:regulation of immune response; IBA:GO_Central.
DR GO; GO:2000404; P:regulation of T cell migration; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0002296; P:T-helper 1 cell lineage commitment; IDA:UniProtKB.
DR InterPro; IPR038829; Leukosialin.
DR PANTHER; PTHR35265; PTHR35265; 1.
PE 1: Evidence at protein level;
KW Cell projection; Direct protein sequencing; Glycoprotein; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:1731338"
FT CHAIN 20..400
FT /note="Leukosialin"
FT /id="PRO_0000021588"
FT CHAIN 277..400
FT /note="CD43 cytoplasmic tail"
FT /evidence="ECO:0000250|UniProtKB:P15702"
FT /id="PRO_0000443406"
FT TOPO_DOM 20..253
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..400
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 21..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..308
FT /note="Required for interaction with EZR, MSN and RDX and
FT for co-localization to microvilli"
FT /evidence="ECO:0000250|UniProtKB:P13838"
FT REGION 320..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 282..296
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:15003504"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2530225,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 341
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2530225,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 355
FT /note="Phosphoserine; by PKC/PRKCQ"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15702"
FT CARBOHYD 21
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 22
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 26
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 28
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 29
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 35
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 36
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 37
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 41
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 42
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 46
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 47
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 48
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 50
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 58
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 69
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 99
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 103
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 109
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 113
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 114
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 136
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 137
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 173
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 178
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1731338"
FT VARIANT 22
FT /note="T -> I (in dbSNP:rs2229653)"
FT /id="VAR_051091"
FT VARIANT 93
FT /note="T -> A (in dbSNP:rs2229654)"
FT /id="VAR_051092"
FT MUTAGEN 282..283
FT /note="KR->PG: Reduced nuclear localization. Loss of
FT nuclear localization; when associated with 295-P-G-296."
FT /evidence="ECO:0000269|PubMed:15003504"
FT MUTAGEN 295..296
FT /note="KR->PG: Reduced nuclear localization. Loss of
FT nuclear localization; when associated with 282-P-G-283."
FT /evidence="ECO:0000269|PubMed:15003504"
SQ SEQUENCE 400 AA; 40322 MW; C9C9AB8435D5E1FE CRC64;
MATLLLLLGV LVVSPDALGS TTAVQTPTSG EPLVSTSEPL SSKMYTTSIT SDPKADSTGD
QTSALPPSTS INEGSPLWTS IGASTGSPLP EPTTYQEVSI KMSSVPQETP HATSHPAVPI
TANSLGSHTV TGGTITTNSP ETSSRTSGAP VTTAASSLET SRGTSGPPLT MATVSLETSK
GTSGPPVTMA TDSLETSTGT TGPPVTMTTG SLEPSSGASG PQVSSVKLST MMSPTTSTNA
STVPFRNPDE NSRGMLPVAV LVALLAVIVL VALLLLWRRR QKRRTGALVL SRGGKRNGVV
DAWAGPAQVP EEGAVTVTVG GSGGDKGSGF PDGEGSSRRP TLTTFFGRRK SRQGSLAMEE
LKSGSGPSLK GEEEPLVASE DGAVDAPAPD EPEGGDGAAP
