ID   CD302_PIG               Reviewed;         240 AA.
AC   A8WH75;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=CD302 antigen {ECO:0000250|UniProtKB:Q8IX05};
DE   AltName: Full=Type I transmembrane C-type lectin receptor DCL-1 {ECO:0000303|PubMed:17947679};
DE   Flags: Precursor;
GN   Name=CD302 {ECO:0000303|PubMed:17947679};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver {ECO:0000305};
RX   PubMed=17145712; DOI=10.1093/nar/gkl954;
RA   Uenishi H., Eguchi-Ogawa T., Shinkai H., Okumura N., Suzuki K., Toki D.,
RA   Hamasima N., Awata T.;
RT   "PEDE (Pig EST Data Explorer) has been expanded into Pig Expression Data
RT   Explorer, including 10 147 porcine full-length cDNA sequences.";
RL   Nucleic Acids Res. 35:D650-D653(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305, ECO:0000312|EMBL:DAA06089.1}
RP   IDENTIFICATION.
RX   PubMed=17947679; DOI=10.4049/jimmunol.179.9.6052;
RA   Kato M., Khan S., d'Aniello E., McDonald K.J., Hart D.N.;
RT   "The novel endocytic and phagocytic C-Type lectin receptor DCL-1/CD302 on
RT   macrophages is colocalized with F-actin, suggesting a role in cell adhesion
RT   and migration.";
RL   J. Immunol. 179:6052-6063(2007).
CC   -!- FUNCTION: Potential multifunctional C-type lectin receptor that may
CC       play roles in endocytosis and phagocytosis as well as in cell adhesion
CC       and migration. {ECO:0000250|UniProtKB:Q8IX05}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC       membrane protein {ECO:0000255}. Cell projection, filopodium
CC       {ECO:0000250|UniProtKB:Q8IX05, ECO:0000255}. Cytoplasm, cell cortex
CC       {ECO:0000250|UniProtKB:Q8IX05, ECO:0000255}. Note=Colocalizes with F-
CC       actin in filopodia, cellular cortex and microvilli of the apical cell
CC       surface. {ECO:0000250|UniProtKB:Q8IX05, ECO:0000255}.
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; AK233610; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; CU928024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BK006293; DAA06089.1; -; mRNA.
DR   RefSeq; NP_001103895.1; NM_001110425.1.
DR   AlphaFoldDB; A8WH75; -.
DR   SMR; A8WH75; -.
DR   STRING; 9823.ENSSSCP00000029693; -.
DR   PaxDb; A8WH75; -.
DR   PeptideAtlas; A8WH75; -.
DR   Ensembl; ENSSSCT00070051588; ENSSSCP00070043630; ENSSSCG00070025809.
DR   GeneID; 100126280; -.
DR   KEGG; ssc:100126280; -.
DR   CTD; 9936; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   HOGENOM; CLU_088281_0_0_1; -.
DR   InParanoid; A8WH75; -.
DR   OMA; RWENVSC; -.
DR   OrthoDB; 1071894at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Chromosome 15.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   2: Evidence at transcript level;
KW   Cell projection; Cytoplasm; Disulfide bond; Glycoprotein; Lectin; Membrane;
KW   Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..240
FT                   /note="CD302 antigen"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000413657"
FT   TOPO_DOM        ?..176
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        198..240
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          40..160
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        136..151
FT                   /evidence="ECO:0000250|UniProtKB:Q5KU26,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   240 AA;  26428 MW;  EE544905C36C2B5A CRC64;
     MARAAPPALL LPLLGLAAAT AAAAAAAAAV GCPSSTWVQF QDSCYIFLQE AIKVESIEDV
     RNQCTDHGAD MVSIHNEEEN TFILETLKKQ WKGPDDILLG MFFDTDDASF KWFDKSNMTF
     DKWSDQEDGE DLVDTCAFLH TKTGEWKKGN CEVSSVEGTL CKAAIPYEKK YLSDNHILIS
     ALVIASTVIL TVLGAVIWFL YKRNLDSGFT TVFSTAPQSP FNDDCVLVVA EENEYAVQFD