CD320_BOVIN
ID CD320_BOVIN Reviewed; 255 AA.
AC A6QNY1;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=CD320 antigen;
DE AltName: Full=Transcobalamin receptor;
DE Short=TCblR;
DE AltName: CD_antigen=CD320;
DE Flags: Precursor;
GN Name=CD320;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for transcobalamin saturated with cobalamin (TCbl).
CC Plays an important role in cobalamin uptake. Plasma membrane protein
CC that is expressed on follicular dendritic cells (FDC) and mediates
CC interaction with germinal center B cells. Functions as costimulator to
CC promote B cell responses to antigenic stimuli; promotes B cell
CC differentiation and proliferation. Germinal center-B (GC-B) cells
CC differentiate into memory B-cells and plasma cells (PC) through
CC interaction with T-cells and follicular dendritic cells (FDC). CD320
CC augments the proliferation of PC precursors generated by IL-10.
CC {ECO:0000250|UniProtKB:Q9NPF0}.
CC -!- SUBUNIT: Interacts (via LDL-receptor class A domains) with TCN2.
CC {ECO:0000250|UniProtKB:Q9NPF0}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NPF0};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9NPF0}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI49058.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC149057; AAI49058.1; ALT_INIT; mRNA.
DR RefSeq; NP_001160030.1; NM_001166558.1.
DR AlphaFoldDB; A6QNY1; -.
DR STRING; 9913.ENSBTAP00000005777; -.
DR PaxDb; A6QNY1; -.
DR PRIDE; A6QNY1; -.
DR Ensembl; ENSBTAT00000005777; ENSBTAP00000005777; ENSBTAG00000004403.
DR GeneID; 505043; -.
DR KEGG; bta:505043; -.
DR CTD; 51293; -.
DR VEuPathDB; HostDB:ENSBTAG00000004403; -.
DR VGNC; VGNC:52223; CD320.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00730000111436; -.
DR HOGENOM; CLU_094249_0_0_1; -.
DR InParanoid; A6QNY1; -.
DR OMA; RIEPCTQ; -.
DR OrthoDB; 1306682at2759; -.
DR TreeFam; TF337215; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000004403; Expressed in digestive system secreted substance and 107 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0031296; P:B cell costimulation; ISS:UniProtKB.
DR GO; GO:0015889; P:cobalamin transport; ISS:UniProtKB.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; ISS:UniProtKB.
DR CDD; cd00112; LDLa; 2.
DR Gene3D; 4.10.400.10; -; 2.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR Pfam; PF00057; Ldl_recept_a; 2.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00192; LDLa; 2.
DR SUPFAM; SSF57424; SSF57424; 2.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 2.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Growth factor; Membrane;
KW Metal-binding; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..255
FT /note="CD320 antigen"
FT /id="PRO_0000354051"
FT TOPO_DOM 30..203
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 52..89
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 120..157
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF0"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF0"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF0"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF0"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF0"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF0"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF0"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF0"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF0"
FT BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF0"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF0"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF0"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 60..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 73..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 121..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 128..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 141..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 255 AA; 26935 MW; 45CDA7CCBA4DAD8E CRC64;
MNGWVARGLA RRAAALGLGL RVLLCFGLCL EIAPTPIQTW SPTQAPGPSA GSCPPTNFQC
RSDGRCLPLI WRCDVDQDCP DGSDEEECGT EVPNGSPSPC DIMDDCPDHN KNLLNCGPQS
CPEGELCCPL DGVCIPSTWL CDGHRDCSDY SDELGCGTKT HEEGRTMSTG TPVTLENVTY
LSNATVTAIE DWDSVQSGNR NVYGIIAAVA VLSISLAAGI LFALSRLCAQ GCLAPLGLLV
SMKGSLQPEK KTSVL
