ID   CD302_RAT               Reviewed;         228 AA.
AC   Q5FVR3;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=CD302 antigen;
DE   AltName: Full=C-type lectin domain family 13 member A;
DE   AltName: CD_antigen=CD302;
DE   Flags: Precursor;
GN   Name=Cd302; Synonyms=Clec13a;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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).
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}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}. Cell projection, filopodium
CC       {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cell projection,
CC       microvillus {ECO:0000250}. Note=Colocalizes with F-actin in filopodia,
CC       cellular cortex and microvilli of the apical cell surface.
CC       {ECO:0000250}.
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; BC089829; AAH89829.1; -; mRNA.
DR   RefSeq; NP_001013938.1; NM_001013916.1.
DR   AlphaFoldDB; Q5FVR3; -.
DR   SMR; Q5FVR3; -.
DR   STRING; 10116.ENSRNOP00000008987; -.
DR   GlyGen; Q5FVR3; 1 site.
DR   PaxDb; Q5FVR3; -.
DR   Ensembl; ENSRNOT00000008987; ENSRNOP00000008987; ENSRNOG00000006623.
DR   GeneID; 295629; -.
DR   KEGG; rno:295629; -.
DR   UCSC; RGD:1307606; rat.
DR   CTD; 9936; -.
DR   RGD; 1307606; Cd302.
DR   eggNOG; KOG4297; Eukaryota.
DR   GeneTree; ENSGT01050000244928; -.
DR   InParanoid; Q5FVR3; -.
DR   OrthoDB; 1071894at2759; -.
DR   PhylomeDB; Q5FVR3; -.
DR   PRO; PR:Q5FVR3; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   GO; GO:0005938; C:cell cortex; ISO:RGD.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0030175; C:filopodium; ISO:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005902; C:microvillus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0006909; P:phagocytosis; ISO:RGD.
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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..228
FT                   /note="CD302 antigen"
FT                   /id="PRO_0000252334"
FT   TOPO_DOM        21..165
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        187..228
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          30..149
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        125..140
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   228 AA;  25452 MW;  73BADC55E48A6EE1 CRC64;
     MPHAALSSLV LLSLATAIFA DCPSSIWVQF QGSCYTFLQV TINVENIEDV RKQCTDHGAD
     LVSIHNEEEN AFILDTLQKR WKGPDDLLLG MFYDTDDASF KWFDQSNMTF DKWADEDGED
     LVDTCGFLYA KTGEWRKGNC EMSSVTGTLC KTAIPYDKKY LSDNHILIST LVIASTVTLA
     VLGAVIWFLY RRSARSGFTS FSPAPQSPYS DGCALVVSEE DEYSVQLD