CD320_RAT
ID CD320_RAT Reviewed; 264 AA.
AC Q5HZW5;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
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 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=Ovary;
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: 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}.
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DR EMBL; BC088861; AAH88861.1; -; mRNA.
DR RefSeq; NP_001014223.1; NM_001014201.1.
DR AlphaFoldDB; Q5HZW5; -.
DR STRING; 10116.ENSRNOP00000009067; -.
DR GlyGen; Q5HZW5; 2 sites.
DR PaxDb; Q5HZW5; -.
DR PRIDE; Q5HZW5; -.
DR Ensembl; ENSRNOT00000009067; ENSRNOP00000009067; ENSRNOG00000006901.
DR GeneID; 362851; -.
DR KEGG; rno:362851; -.
DR UCSC; RGD:1305860; rat.
DR CTD; 51293; -.
DR RGD; 1305860; Cd320.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00730000111436; -.
DR HOGENOM; CLU_094249_0_0_1; -.
DR InParanoid; Q5HZW5; -.
DR OMA; RIEPCTQ; -.
DR OrthoDB; 1306682at2759; -.
DR PhylomeDB; Q5HZW5; -.
DR TreeFam; TF337215; -.
DR PRO; PR:Q5HZW5; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000006901; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q5HZW5; RN.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0038024; F:cargo receptor activity; ISO:RGD.
DR GO; GO:0031419; F:cobalamin binding; ISO:RGD.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0031296; P:B cell costimulation; ISS:UniProtKB.
DR GO; GO:0009235; P:cobalamin metabolic process; ISO:RGD.
DR GO; GO:0015889; P:cobalamin transport; ISS:UniProtKB.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; ISS:UniProtKB.
DR GO; GO:0030656; P:regulation of vitamin metabolic process; ISO:RGD.
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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..264
FT /note="CD320 antigen"
FT /id="PRO_0000354053"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 50..87
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 127..164
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF0"
FT BINDING 72
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 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF0"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF0"
FT BINDING 151
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 BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF0"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF0"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 58..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 71..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 128..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 135..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 148..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 264 AA; 27943 MW; FD32FAAB1D1EA4AC CRC64;
MARCGAGRAA ALGLVLRLLL GLRTGPEAAP APTSAPAHTL VQVSGPRAGS CPTDTFKCLT
SGYCVPLSWR CDGDRDCSDG SDEEECRIEP CAQNRQCQPQ PALPCSCDNI SGCSAGSDKN
LNCSRSPCQE GELRCILDDV CIPHTWRCDG HPDCPDSSDE LSCDTDTETD KIFQEENATT
SMSSMIVEKE TSFRNVTVAS AGHPSRNPNA YGVIAAAGVL SAILVSATIL ILLRLRGQGY
LPPTGLLVAV KESLLLSERK TSLI
