CD320_MOUSE
ID CD320_MOUSE Reviewed; 260 AA.
AC Q9Z1P5; Q3V2Q4; Q7TSW0; Q8C2Q4; Q9CWC2;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 148.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Rowen L., Qin S., Madan A., Loretz C., Hall J., James R., Dors M.,
RA Shaffer T., Abbasi N., Ratcliffe A., Dickhoff R., Lasky S., Hood L.;
RT "Sequence of the mouse major histocompatibility complex class II region.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129/Sv;
RA Nagaraja R., Brathwaite M.E., Abe K.;
RT "Genomic sequence analysis in the mouse T-complex region.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Corpora quadrigemina, Medulla oblongata, Placenta, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-213.
RC STRAIN=A/J;
RA Kierstein S., Lundstroem C., Iraqi F., Gibson J.;
RT "Fifteen gene-associated SNPs within the MHC region on mouse chromosome
RT 17.";
RL Submitted (MAY-2003) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Z1P5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z1P5-2; Sequence=VSP_035723;
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD91188.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR EMBL; AF110520; AAC97969.1; -; Genomic_DNA.
DR EMBL; AF528162; AAO17374.1; -; Genomic_DNA.
DR EMBL; AK021187; BAB32321.1; -; mRNA.
DR EMBL; AK078151; BAC37150.1; -; mRNA.
DR EMBL; AK088189; BAC40198.1; -; mRNA.
DR EMBL; AK131655; BAE20743.1; -; mRNA.
DR EMBL; AK140204; BAE24278.1; -; mRNA.
DR EMBL; CH466660; EDL10217.1; -; Genomic_DNA.
DR EMBL; BC026888; AAH26888.1; -; mRNA.
DR EMBL; AJ560661; CAD91188.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ560659; CAD91188.1; JOINED; Genomic_DNA.
DR EMBL; AJ560660; CAD91188.1; JOINED; Genomic_DNA.
DR CCDS; CCDS28632.1; -. [Q9Z1P5-1]
DR CCDS; CCDS79533.1; -. [Q9Z1P5-2]
DR RefSeq; NP_001292098.1; NM_001305169.1. [Q9Z1P5-2]
DR RefSeq; NP_062294.3; NM_019421.3. [Q9Z1P5-1]
DR AlphaFoldDB; Q9Z1P5; -.
DR BioGRID; 207609; 2.
DR STRING; 10090.ENSMUSP00000002379; -.
DR GlyGen; Q9Z1P5; 2 sites.
DR iPTMnet; Q9Z1P5; -.
DR PhosphoSitePlus; Q9Z1P5; -.
DR PaxDb; Q9Z1P5; -.
DR PeptideAtlas; Q9Z1P5; -.
DR PRIDE; Q9Z1P5; -.
DR ProteomicsDB; 279965; -. [Q9Z1P5-1]
DR ProteomicsDB; 279966; -. [Q9Z1P5-2]
DR Antibodypedia; 3048; 145 antibodies from 26 providers.
DR DNASU; 54219; -.
DR Ensembl; ENSMUST00000002379; ENSMUSP00000002379; ENSMUSG00000002308. [Q9Z1P5-1]
DR Ensembl; ENSMUST00000087559; ENSMUSP00000084839; ENSMUSG00000002308. [Q9Z1P5-2]
DR GeneID; 54219; -.
DR KEGG; mmu:54219; -.
DR UCSC; uc008bzv.1; mouse. [Q9Z1P5-1]
DR UCSC; uc056zej.1; mouse. [Q9Z1P5-2]
DR CTD; 51293; -.
DR MGI; MGI:1860083; Cd320.
DR VEuPathDB; HostDB:ENSMUSG00000002308; -.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00730000111436; -.
DR HOGENOM; CLU_094249_0_0_1; -.
DR InParanoid; Q9Z1P5; -.
DR OMA; RIEPCTQ; -.
DR OrthoDB; 1306682at2759; -.
DR PhylomeDB; Q9Z1P5; -.
DR TreeFam; TF337215; -.
DR BioGRID-ORCS; 54219; 5 hits in 76 CRISPR screens.
DR ChiTaRS; Cd320; mouse.
DR PRO; PR:Q9Z1P5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9Z1P5; protein.
DR Bgee; ENSMUSG00000002308; Expressed in placenta labyrinth and 244 other tissues.
DR Genevisible; Q9Z1P5; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IMP:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0038024; F:cargo receptor activity; IMP:MGI.
DR GO; GO:0031419; F:cobalamin binding; ISO:MGI.
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; IMP:MGI.
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; IMP:MGI.
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 Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Growth factor; Membrane; Metal-binding; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..260
FT /note="CD320 antigen"
FT /id="PRO_0000354052"
FT TOPO_DOM 29..208
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 46..83
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 123..160
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF0"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF0"
FT BINDING 70
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 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF0"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF0"
FT BINDING 147
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 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF0"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF0"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 54..73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 67..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 124..137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 131..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 144..159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT VAR_SEQ 1..40
FT /note="MARGGAGRAVALGLVLRLLFGLRTGLEAAPAPAHTRVQVS -> MWAGRLLF
FT LILTSHHAGLVTRYLLAA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035723"
FT CONFLICT 74
FT /note="S -> F (in Ref. 3; BAB32321)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="Q -> H (in Ref. 3; BAE20743)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="P -> T (in Ref. 3; BAC40198)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 260 AA; 27739 MW; 5AA3B6081C8E080C CRC64;
MARGGAGRAV ALGLVLRLLF GLRTGLEAAP APAHTRVQVS GSRADSCPTD TFQCLTSGYC
VPLSWRCDGD QDCSDGSDEE DCRIESCAQN GQCQPQSALP CSCDNISGCS DVSDKNLNCS
RPPCQESELH CILDDVCIPH TWRCDGHPDC LDSSDELSCD TDTEIDKIFQ EENATTTRIS
TTMENETSFR NVTFTSAGDS SRNPSAYGVI AAAGVLSAIL VSATLLILLR LRGQGYLPPP
GLLVAVKESL LLSERKTSLI
