CD320_HUMAN
ID CD320_HUMAN Reviewed; 282 AA.
AC Q9NPF0; B2RDS5; D6W668; F5H6D3; Q53HF7;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=CD320 antigen;
DE AltName: Full=8D6 antigen {ECO:0000303|PubMed:10727470};
DE AltName: Full=FDC-signaling molecule 8D6 {ECO:0000303|PubMed:10727470, ECO:0000303|PubMed:11418631};
DE Short=FDC-SM-8D6 {ECO:0000303|PubMed:11418631};
DE AltName: Full=Transcobalamin receptor {ECO:0000303|PubMed:18779389};
DE Short=TCblR {ECO:0000303|PubMed:18779389, ECO:0000303|PubMed:20524213};
DE AltName: CD_antigen=CD320;
DE Flags: Precursor;
GN Name=CD320; Synonyms=8D6A; ORFNames=UNQ198/PRO224;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, FUNCTION, AND
RP TISSUE SPECIFICITY.
RX PubMed=10727470; DOI=10.1084/jem.191.6.1077;
RA Li L., Zhang X., Kovacic S., Long A.J., Bourque K., Wood C.R., Choi Y.S.;
RT "Identification of a human follicular dendritic cell molecule that
RT stimulates germinal center B cell growth.";
RL J. Exp. Med. 191:1077-1084(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RG The European IMAGE consortium;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Gastric mucosa, and Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-8.
RC TISSUE=Coronary artery;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Kidney;
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 [11]
RP PROTEIN SEQUENCE OF 36-50.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11418631; DOI=10.4049/jimmunol.167.1.49;
RA Zhang X., Li L., Jung J., Xiang S., Hollmann C., Choi Y.S.;
RT "The distinct roles of T cell-derived cytokines and a novel follicular
RT dendritic cell-signaling molecule 8D6 in germinal center-B cell
RT differentiation.";
RL J. Immunol. 167:49-56(2001).
RN [13]
RP FUNCTION AS A RECEPTOR FOR TRANSCOBALAMIN, AND SUBCELLULAR LOCATION.
RX PubMed=18779389; DOI=10.1182/blood-2008-05-158949;
RA Quadros E.V., Nakayama Y., Sequeira J.M.;
RT "The protein and the gene encoding the receptor for the cellular uptake of
RT transcobalamin-bound cobalamin.";
RL Blood 113:186-192(2009).
RN [14]
RP FUNCTION, INVOLVEMENT IN MMATC, VARIANT MMATC GLU-88 DEL, CHARACTERIZATION
RP OF VARIANT MMATC GLU-88 DEL, AND VARIANTS GLY-142 AND ARG-220.
RX PubMed=20524213; DOI=10.1002/humu.21297;
RA Quadros E.V., Lai S.-C., Nakayama Y., Sequeira J.M., Hannibal L., Wang S.,
RA Jacobsen D.W., Fedosov S., Wright E., Gallagher R.C., Anastasio N.,
RA Watkins D., Rosenblatt D.S.;
RT "Positive newborn screen for methylmalonic aciduria identifies the first
RT mutation in TCblR/CD320, the gene for cellular uptake of transcobalamin-
RT bound vitamin B(12).";
RL Hum. Mutat. 31:924-929(2010).
RN [15] {ECO:0007744|PDB:4ZRP, ECO:0007744|PDB:4ZRQ}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 53-171 OF WILD-TYPE AND VARIANT
RP MMATC GLU-88 DEL IN COMPLEX WITH TCN2 AND CALCIUM, INTERACTION WITH TCN2,
RP DISULFIDE BONDS, AND CHARACTERIZATION OF VARIANT MMATC GLU-88 DEL.
RX PubMed=27411955; DOI=10.1038/ncomms12100;
RA Alam A., Woo J.S., Schmitz J., Prinz B., Root K., Chen F., Bloch J.S.,
RA Zenobi R., Locher K.P.;
RT "Structural basis of transcobalamin recognition by human CD320 receptor.";
RL Nat. Commun. 7:12100-12100(2016).
RN [16]
RP VARIANT MMATC GLU-88 DEL.
RX PubMed=22819238; DOI=10.1016/j.jaapos.2012.04.003;
RA Karth P., Singh R., Kim J., Costakos D.;
RT "Bilateral central retinal artery occlusions in an infant with
RT hyperhomocysteinemia.";
RL J. AAPOS 16:398-400(2012).
RN [17]
RP VARIANT MMATC GLU-88 DEL.
RX PubMed=27535533; DOI=10.1038/nature19057;
RG Exome Aggregation Consortium;
RA Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E., Fennell T.,
RA O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B., Tukiainen T.,
RA Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K., Zhao F., Zou J.,
RA Pierce-Hoffman E., Berghout J., Cooper D.N., Deflaux N., DePristo M.,
RA Do R., Flannick J., Fromer M., Gauthier L., Goldstein J., Gupta N.,
RA Howrigan D., Kiezun A., Kurki M.I., Moonshine A.L., Natarajan P.,
RA Orozco L., Peloso G.M., Poplin R., Rivas M.A., Ruano-Rubio V., Rose S.A.,
RA Ruderfer D.M., Shakir K., Stenson P.D., Stevens C., Thomas B.P., Tiao G.,
RA Tusie-Luna M.T., Weisburd B., Won H.H., Yu D., Altshuler D.M.,
RA Ardissino D., Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
RA Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S., Laakso M.,
RA McCarroll S., McCarthy M.I., McGovern D., McPherson R., Neale B.M.,
RA Palotie A., Purcell S.M., Saleheen D., Scharf J.M., Sklar P.,
RA Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C., Wilson J.G.,
RA Daly M.J., MacArthur D.G.;
RT "Analysis of protein-coding genetic variation in 60,706 humans.";
RL Nature 536:285-291(2016).
CC -!- FUNCTION: Receptor for transcobalamin saturated with cobalamin (TCbl)
CC (PubMed:18779389). Plays an important role in cobalamin uptake
CC (PubMed:18779389, PubMed:20524213). Plasma membrane protein that is
CC expressed on follicular dendritic cells (FDC) and mediates interaction
CC with germinal center B cells (PubMed:10727470). Functions as
CC costimulator to promote B cell responses to antigenic stimuli; promotes
CC B cell differentiation and proliferation (PubMed:10727470,
CC PubMed:11418631). Germinal center-B (GC-B) cells differentiate into
CC memory B-cells and plasma cells (PC) through interaction with T-cells
CC and follicular dendritic cells (FDC) (PubMed:11418631). CD320 augments
CC the proliferation of PC precursors generated by IL-10
CC (PubMed:11418631). {ECO:0000269|PubMed:10727470,
CC ECO:0000269|PubMed:11418631, ECO:0000269|PubMed:18779389,
CC ECO:0000269|PubMed:20524213}.
CC -!- SUBUNIT: Interacts (via LDL-receptor class A domains) with TCN2
CC (PubMed:27411955). {ECO:0000269|PubMed:27411955}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10727470,
CC ECO:0000269|PubMed:11418631, ECO:0000305|PubMed:18779389}; Single-pass
CC type I membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NPF0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NPF0-2; Sequence=VSP_045368;
CC -!- TISSUE SPECIFICITY: Detected in the germinal center (GC) of lymphoid
CC follicles (at protein level) (PubMed:11418631). Expressed abundantly on
CC follicular dendritic cells (FDCs) (PubMed:10727470).
CC {ECO:0000269|PubMed:10727470, ECO:0000269|PubMed:11418631}.
CC -!- DISEASE: Methylmalonic aciduria, transient, due to transcobalamin
CC receptor defect (MMATC) [MIM:613646]: A metabolic disorder
CC characterized by increased blood C3-acylcarnitine levels, elevated
CC methylmalonate and homocysteine, and low uptake of transcobalamin-bound
CC cobalamin, but normal conversion to adenosylcobalamin and
CC methylcobalamin. {ECO:0000269|PubMed:20524213,
CC ECO:0000269|PubMed:22819238, ECO:0000269|PubMed:27411955,
CC ECO:0000269|PubMed:27535533}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
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DR EMBL; AF161254; AAF61850.1; -; mRNA.
DR EMBL; AL365455; CAB97010.1; -; mRNA.
DR EMBL; AL136652; CAB66587.1; -; mRNA.
DR EMBL; AY358420; AAQ88786.1; -; mRNA.
DR EMBL; AK058014; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK315656; BAG38022.1; -; mRNA.
DR EMBL; AK222623; BAD96343.1; -; mRNA.
DR EMBL; CR457174; CAG33455.1; -; mRNA.
DR EMBL; AC010323; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471139; EAW68936.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW68939.1; -; Genomic_DNA.
DR EMBL; BC000668; AAH00668.1; -; mRNA.
DR EMBL; BC007083; AAH07083.1; -; mRNA.
DR CCDS; CCDS12198.1; -. [Q9NPF0-1]
DR CCDS; CCDS54210.1; -. [Q9NPF0-2]
DR RefSeq; NP_001159367.1; NM_001165895.1. [Q9NPF0-2]
DR RefSeq; NP_057663.1; NM_016579.3. [Q9NPF0-1]
DR PDB; 4ZRP; X-ray; 2.10 A; C/D=53-171.
DR PDB; 4ZRQ; X-ray; 2.60 A; C/D=53-171.
DR PDB; 7QBD; X-ray; 4.18 A; C/D=52-198.
DR PDB; 7QBE; X-ray; 3.00 A; B/D=52-198.
DR PDB; 7QBF; X-ray; 1.85 A; C=52-198.
DR PDB; 7QBG; X-ray; 2.69 A; B/D=52-198.
DR PDBsum; 4ZRP; -.
DR PDBsum; 4ZRQ; -.
DR PDBsum; 7QBD; -.
DR PDBsum; 7QBE; -.
DR PDBsum; 7QBF; -.
DR PDBsum; 7QBG; -.
DR AlphaFoldDB; Q9NPF0; -.
DR SMR; Q9NPF0; -.
DR BioGRID; 119444; 58.
DR IntAct; Q9NPF0; 23.
DR STRING; 9606.ENSP00000301458; -.
DR GlyGen; Q9NPF0; 3 sites.
DR iPTMnet; Q9NPF0; -.
DR PhosphoSitePlus; Q9NPF0; -.
DR BioMuta; CD320; -.
DR DMDM; 74734303; -.
DR EPD; Q9NPF0; -.
DR jPOST; Q9NPF0; -.
DR MassIVE; Q9NPF0; -.
DR MaxQB; Q9NPF0; -.
DR PaxDb; Q9NPF0; -.
DR PeptideAtlas; Q9NPF0; -.
DR PRIDE; Q9NPF0; -.
DR ProteomicsDB; 27153; -.
DR ProteomicsDB; 81981; -. [Q9NPF0-1]
DR Antibodypedia; 3048; 145 antibodies from 26 providers.
DR DNASU; 51293; -.
DR Ensembl; ENST00000301458.10; ENSP00000301458.4; ENSG00000167775.11. [Q9NPF0-1]
DR Ensembl; ENST00000537716.6; ENSP00000437697.1; ENSG00000167775.11. [Q9NPF0-2]
DR GeneID; 51293; -.
DR KEGG; hsa:51293; -.
DR MANE-Select; ENST00000301458.10; ENSP00000301458.4; NM_016579.4; NP_057663.1.
DR UCSC; uc002mjj.3; human. [Q9NPF0-1]
DR CTD; 51293; -.
DR DisGeNET; 51293; -.
DR GeneCards; CD320; -.
DR HGNC; HGNC:16692; CD320.
DR HPA; ENSG00000167775; Low tissue specificity.
DR MalaCards; CD320; -.
DR MIM; 606475; gene.
DR MIM; 613646; phenotype.
DR neXtProt; NX_Q9NPF0; -.
DR OpenTargets; ENSG00000167775; -.
DR Orphanet; 280183; Methylmalonic aciduria due to transcobalamin receptor defect.
DR PharmGKB; PA142672142; -.
DR VEuPathDB; HostDB:ENSG00000167775; -.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00730000111436; -.
DR HOGENOM; CLU_094249_0_0_1; -.
DR InParanoid; Q9NPF0; -.
DR OMA; RIEPCTQ; -.
DR OrthoDB; 1306682at2759; -.
DR PhylomeDB; Q9NPF0; -.
DR TreeFam; TF337215; -.
DR PathwayCommons; Q9NPF0; -.
DR Reactome; R-HSA-3359485; Defective CD320 causes MMATC.
DR Reactome; R-HSA-9758890; Transport of RCbl within the body.
DR SABIO-RK; Q9NPF0; -.
DR SignaLink; Q9NPF0; -.
DR BioGRID-ORCS; 51293; 14 hits in 1077 CRISPR screens.
DR ChiTaRS; CD320; human.
DR GeneWiki; CD320; -.
DR GenomeRNAi; 51293; -.
DR Pharos; Q9NPF0; Tbio.
DR PRO; PR:Q9NPF0; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NPF0; protein.
DR Bgee; ENSG00000167775; Expressed in mucosa of transverse colon and 186 other tissues.
DR ExpressionAtlas; Q9NPF0; baseline and differential.
DR Genevisible; Q9NPF0; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:LIFEdb.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0038024; F:cargo receptor activity; TAS:Reactome.
DR GO; GO:0031419; F:cobalamin binding; IDA:MGI.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0031296; P:B cell costimulation; IMP:UniProtKB.
DR GO; GO:0009235; P:cobalamin metabolic process; TAS:Reactome.
DR GO; GO:0015889; P:cobalamin transport; IMP:UniProtKB.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:UniProtKB.
DR GO; GO:0030656; P:regulation of vitamin metabolic process; IEA:Ensembl.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell membrane;
KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein;
KW Growth factor; Membrane; Metal-binding; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 36..282
FT /note="CD320 antigen"
FT /id="PRO_0000045798"
FT TOPO_DOM 36..229
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 53..90
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 131..168
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT REGION 199..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27411955,
FT ECO:0007744|PDB:4ZRP"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27411955,
FT ECO:0007744|PDB:4ZRP"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27411955,
FT ECO:0007744|PDB:4ZRP"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27411955,
FT ECO:0007744|PDB:4ZRP"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27411955,
FT ECO:0007744|PDB:4ZRP"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27411955,
FT ECO:0007744|PDB:4ZRP"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27411955,
FT ECO:0007744|PDB:4ZRP"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27411955,
FT ECO:0007744|PDB:4ZRP"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27411955,
FT ECO:0007744|PDB:4ZRP"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27411955,
FT ECO:0007744|PDB:4ZRP"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27411955,
FT ECO:0007744|PDB:4ZRP"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27411955,
FT ECO:0007744|PDB:4ZRP"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124,
FT ECO:0000269|PubMed:27411955, ECO:0007744|PDB:4ZRP,
FT ECO:0007744|PDB:4ZRQ"
FT DISULFID 61..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124,
FT ECO:0000269|PubMed:27411955, ECO:0007744|PDB:4ZRP,
FT ECO:0007744|PDB:4ZRQ"
FT DISULFID 74..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124,
FT ECO:0000269|PubMed:27411955, ECO:0007744|PDB:4ZRP"
FT DISULFID 132..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124,
FT ECO:0000269|PubMed:27411955, ECO:0007744|PDB:4ZRP,
FT ECO:0007744|PDB:4ZRQ"
FT DISULFID 139..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124,
FT ECO:0000269|PubMed:27411955, ECO:0007744|PDB:4ZRP,
FT ECO:0007744|PDB:4ZRQ"
FT DISULFID 152..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124,
FT ECO:0000269|PubMed:27411955, ECO:0007744|PDB:4ZRP,
FT ECO:0007744|PDB:4ZRQ"
FT VAR_SEQ 49..90
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045368"
FT VARIANT 8
FT /note="Q -> R (in dbSNP:rs2232775)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_047315"
FT VARIANT 88
FT /note="Missing (in MMATC; unknown pathological
FT significance; decreased function in cobalamin transport;
FT does not affect stability; does not affect interaction with
FT TCN2; dbSNP:rs150384171)"
FT /evidence="ECO:0000269|PubMed:20524213,
FT ECO:0000269|PubMed:22819238, ECO:0000269|PubMed:27411955,
FT ECO:0000269|PubMed:27535533"
FT /id="VAR_064080"
FT VARIANT 142
FT /note="S -> G"
FT /evidence="ECO:0000269|PubMed:20524213"
FT /id="VAR_077921"
FT VARIANT 220
FT /note="G -> R (in dbSNP:rs2336573)"
FT /evidence="ECO:0000269|PubMed:20524213"
FT /id="VAR_047316"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:4ZRP"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:4ZRP"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:4ZRP"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:4ZRP"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:4ZRP"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:4ZRP"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:4ZRP"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:4ZRQ"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:4ZRP"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:4ZRP"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:4ZRP"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:4ZRP"
SQ SEQUENCE 282 AA; 28991 MW; 59E172986B220E4F CRC64;
MSGGWMAQVG AWRTGALGLA LLLLLGLGLG LEAAASPLST PTSAQAAGPS SGSCPPTKFQ
CRTSGLCVPL TWRCDRDLDC SDGSDEEECR IEPCTQKGQC PPPPGLPCPC TGVSDCSGGT
DKKLRNCSRL ACLAGELRCT LSDDCIPLTW RCDGHPDCPD SSDELGCGTN EILPEGDATT
MGPPVTLESV TSLRNATTMG PPVTLESVPS VGNATSSSAG DQSGSPTAYG VIAAAAVLSA
SLVTATLLLL SWLRAQERLR PLGLLVAMKE SLLLSEQKTS LP
