LOCUS       NP_003114                400 aa            linear   PRI 28-APR-2025
DEFINITION  leukosialin precursor [Homo sapiens].
ACCESSION   NP_003114
VERSION     NP_003114.1
DBSOURCE    REFSEQ: accession NM_003123.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Vega-Mendoza,D., Canas-Linares,A., Flores-Alcantar,A.,
            Espinosa-Neira,R., Melchy-Perez,E., Vera-Estrella,R., Auvynet,C.
            and Rosenstein,Y.
  TITLE     CD43 (sialophorin) is involved in the induction of extracellular
            matrix remodeling and angiogenesis by lung cancer cells
  JOURNAL   J Cell Physiol 236 (9), 6643-6656 (2021)
   PUBMED   33533043
  REMARK    GeneRIF: CD43 (sialophorin) is involved in the induction of
            extracellular matrix remodeling and angiogenesis by lung cancer
            cells.
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Yoshimura,A., Asahina,Y., Chang,L.Y., Angata,T., Tanaka,H.,
            Kitajima,K. and Sato,C.
  TITLE     Identification and functional characterization of a Siglec-7
            counter-receptor on K562 cells
  JOURNAL   J Biol Chem 296, 100477 (2021)
   PUBMED   33640457
  REMARK    GeneRIF: Identification and functional characterization of a
            Siglec-7 counter-receptor on K562 cells.
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Sorigue,M.
  TITLE     CD43 in the malignant flow cytometry laboratory in 2020
  JOURNAL   Expert Rev Hematol 14 (1), 123-136 (2021)
   PUBMED   33249940
  REMARK    GeneRIF: CD43 in the malignant flow cytometry laboratory in 2020.
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Rogaev,E.I. and Keryanov,S.A.
  TITLE     Unusual variability of the complex dinucleotide repeat block at the
            SPN locus
  JOURNAL   Hum Mol Genet 1 (8), 657 (1992)
   PUBMED   1301183
REFERENCE   5  (residues 1 to 400)
  AUTHORS   Schmid,K., Hediger,M.A., Brossmer,R., Collins,J.H., Haupt,H.,
            Marti,T., Offner,G.D., Schaller,J., Takagaki,K., Walsh,M.T. et al.
  TITLE     Amino acid sequence of human plasma galactoglycoprotein: identity
            with the extracellular region of CD43 (sialophorin)
  JOURNAL   Proc Natl Acad Sci U S A 89 (2), 663-667 (1992)
   PUBMED   1731338
REFERENCE   6  (residues 1 to 400)
  AUTHORS   Rosenstein,Y., Park,J.K., Hahn,W.C., Rosen,F.S., Bierer,B.E. and
            Burakoff,S.J.
  TITLE     CD43, a molecule defective in Wiskott-Aldrich syndrome, binds
            ICAM-1
  JOURNAL   Nature 354 (6350), 233-235 (1991)
   PUBMED   1683685
REFERENCE   7  (residues 1 to 400)
  AUTHORS   Kudo,S. and Fukuda,M.
  TITLE     A short, novel promoter sequence confers the expression of human
            leukosialin, a major sialoglycoprotein on leukocytes
  JOURNAL   J Biol Chem 266 (13), 8483-8489 (1991)
   PUBMED   1827122
REFERENCE   8  (residues 1 to 400)
  AUTHORS   Park,J.K., Rosenstein,Y.J., Remold-O'Donnell,E., Bierer,B.E.,
            Rosen,F.S. and Burakoff,S.J.
  TITLE     Enhancement of T-cell activation by the CD43 molecule whose
            expression is defective in Wiskott-Aldrich syndrome
  JOURNAL   Nature 350 (6320), 706-709 (1991)
   PUBMED   2023632
REFERENCE   9  (residues 1 to 400)
  AUTHORS   Shelley,C.S., Remold-O'Donnell,E., Rosen,F.S. and Whitehead,A.S.
  TITLE     Structure of the human sialophorin (CD43) gene. Identification of
            features atypical of genes encoding integral membrane proteins
  JOURNAL   Biochem J 270 (3), 569-576 (1990)
   PUBMED   2241892
REFERENCE   10 (residues 1 to 400)
  AUTHORS   Shelley,C.S., Remold-O'Donnell,E., Davis,A.E. 3rd, Bruns,G.A.,
            Rosen,F.S., Carroll,M.C. and Whitehead,A.S.
  TITLE     Molecular characterization of sialophorin (CD43), the lymphocyte
            surface sialoglycoprotein defective in Wiskott-Aldrich syndrome
  JOURNAL   Proc Natl Acad Sci U S A 86 (8), 2819-2823 (1989)
   PUBMED   2784859
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1989 Jun;86(12):4689]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK292626.1, AC009086.6 and
            BQ774811.1.
            
            Summary: This gene encodes a highly sialylated glycoprotein that
            functions in antigen-specific activation of T cells, and is found
            on the surface of thymocytes, T lymphocytes, monocytes,
            granulocytes, and some B lymphocytes. It contains a mucin-like
            extracellular domain, a transmembrane region and a carboxy-terminal
            intracellular region. The extracellular domain has a high
            proportion of serine and threonine residues, allowing extensive
            O-glycosylation, and has one potential N-glycosylation site, while
            the carboxy-terminal region has potential phosphorylation sites
            that may mediate transduction of activation signals. Different
            glycoforms of this protein have been described. In stimulated
            immune cells, proteolytic cleavage of the extracellular domain
            occurs in some cell types, releasing a soluble extracellular
            fragment. Defects in expression of this gene are associated with
            Wiskott-Aldrich syndrome. [provided by RefSeq, Sep 2017].
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 1. Variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK292626.1, SRR1163657.370958.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000652691.1/ ENSP00000498852.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..400
                     /product="leukosialin precursor"
                     /note="sialophorin (gpL115, leukosialin, CD43);
                     galactoglycoprotein; leukocyte sialoglycoprotein"
                     /calculated_mol_wt=38445
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1895
     mat_peptide     20..400
                     /product="Leukosialin. /id=PRO_0000021588"
                     /note="propagated from UniProtKB/Swiss-Prot (P16150.1)"
                     /calculated_mol_wt=38445
     Region          21..224
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P16150.1)"
     Site            21
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            22
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            26
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            28
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            29
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            35
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            36
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            37
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            41
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            42
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Region          45..>244
                     /region_name="Chi1"
                     /note="Chitinase [Carbohydrate transport and metabolism];
                     COG3469"
                     /db_xref="CDD:442692"
     Site            46
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            47
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            48
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            50
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            58
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            69
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            99
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            103
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            109
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            113
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            114
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            136
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            137
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            173
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            178
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            239
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:1731338; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            254..276
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P16150.1)"
     mat_peptide     277..400
                     /product="CD43 cytoplasmic tail.
                     /evidence=ECO:0000250|UniProtKB:P15702.
                     /id=PRO_0000443406"
                     /note="propagated from UniProtKB/Swiss-Prot (P16150.1)"
                     /calculated_mol_wt=12716
     Region          278..308
                     /region_name="Required for interaction with EZR, MSN and
                     RDX and for co-localization to microvilli.
                     /evidence=ECO:0000250|UniProtKB:P13838"
                     /note="propagated from UniProtKB/Swiss-Prot (P16150.1)"
     Region          282..296
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000269|PubMed:15003504"
                     /note="propagated from UniProtKB/Swiss-Prot (P16150.1)"
     Site            291
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:2530225,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Region          320..400
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P16150.1)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            351
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:2530225,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC/PRKCQ.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P15702; propagated from
                     UniProtKB/Swiss-Prot (P16150.1)"
     CDS             1..400
                     /gene="SPN"
                     /gene_synonym="CD43; GALGP; GPL115; LEU-22; LSN"
                     /coded_by="NM_003123.6:105..1307"
                     /db_xref="CCDS:CCDS10650.1"
                     /db_xref="GeneID:6693"
                     /db_xref="HGNC:HGNC:11249"
                     /db_xref="MIM:182160"
ORIGIN      
        1 matlllllgv lvvspdalgs ttavqtptsg eplvstsepl sskmyttsit sdpkadstgd
       61 qtsalppsts inegsplwts igastgsplp epttyqevsi kmssvpqetp hatshpavpi
      121 tanslgshtv tggtittnsp etssrtsgap vttaasslet srgtsgpplt matvsletsk
      181 gtsgppvtma tdsletstgt tgppvtmttg slepssgasg pqvssvklst mmspttstna
      241 stvpfrnpde nsrgmlpvav lvallavivl vallllwrrr qkrrtgalvl srggkrngvv
      301 dawagpaqvp eegavtvtvg gsggdkgsgf pdgegssrrp tlttffgrrk srqgslamee
      361 lksgsgpslk geeeplvase dgavdapapd epeggdgaap
//
