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 27-MAR-2024, entry version 201. 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. 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; 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; 54. DR CORUM; P16150; -. DR IntAct; P16150; 11. DR STRING; 9606.ENSP00000498852; -. DR GlyConnect; 340; 11 O-Linked glycans. DR GlyCosmos; P16150; 29 sites, 17 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; 9606-ENSP00000353238; -. DR PeptideAtlas; P16150; -. DR ProteomicsDB; 53297; -. DR Pumba; P16150; -. DR Antibodypedia; 3627; 2443 antibodies from 47 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 AGR; HGNC:11249; -. 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; FKMSSMP; -. DR OrthoDB; 4616417at2759; -. 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; 25 hits in 1156 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 184 other cell types or tissues. DR ExpressionAtlas; P16150; baseline and differential. DR GO; GO:0005604; C:basement membrane; IEA:Ensembl. 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: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:0097190; P:apoptotic signaling pathway; IEA:Ensembl. 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:0001808; P:negative regulation of type IV hypersensitivity; IEA:Ensembl. DR GO; GO:0045060; P:negative thymic T cell selection; IEA:Ensembl. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl. DR GO; GO:2000406; P:positive regulation of T cell migration; ISS:UniProtKB. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl. DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:MGI. DR GO; GO:0050688; P:regulation of defense response to virus; IEA:Ensembl. 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:0001562; P:response to protozoan; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0031295; P:T cell costimulation; IEA:Ensembl. DR GO; GO:0042098; P:T cell proliferation; IEA:Ensembl. DR GO; GO:0002296; P:T-helper 1 cell lineage commitment; IDA:UniProtKB. DR InterPro; IPR038829; Leukosialin. DR PANTHER; PTHR35265; LEUKOSIALIN; 1. DR PANTHER; PTHR35265:SF1; LEUKOSIALIN; 1. DR Genevisible; P16150; HS. 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 //