GenomeNet

Database: UniProt
Entry: Q9NPF0
LinkDB: Q9NPF0
Original site: Q9NPF0 
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   08-MAY-2019, entry version 154.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
RP   FUNCTION, AND 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.,
RA   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.,
RA   Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA   Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA   Wambutt R., Korn B., Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and
RT   analysis of 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.,
RA   Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA   Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA   Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA   Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA   Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA   Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale
RT   effort to identify novel human secreted and transmembrane proteins: a
RT   bioinformatics 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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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
RT   verified 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
RT   uptake of transcobalamin-bound cobalamin.";
RL   Blood 113:186-192(2009).
RN   [14]
RP   FUNCTION, INVOLVEMENT IN MMATC, VARIANT MMATC GLU-88 DEL,
RP   CHARACTERIZATION OF VARIANT MMATC GLU-88 DEL, AND VARIANTS GLY-142 AND
RP   ARG-220.
RX   PubMed=20524213; DOI=10.1002/humu.21297;
RA   Quadros E.V., Lai S.-C., Nakayama Y., Sequeira J.M., Hannibal L.,
RA   Wang S., Jacobsen D.W., Fedosov S., Wright E., Gallagher R.C.,
RA   Anastasio N., Watkins D., Rosenblatt D.S.;
RT   "Positive newborn screen for methylmalonic aciduria identifies the
RT   first mutation in TCblR/CD320, the gene for cellular uptake of
RT   transcobalamin-bound vitamin B(12).";
RL   Hum. Mutat. 31:924-929(2010).
RN   [15] {ECO:0000244|PDB:4ZRP, ECO:0000244|PDB:4ZRQ}
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 53-171 OF WILD-TYPE AND
RP   VARIANT MMATC GLU-88 DEL IN COMPLEX WITH TCN2 AND CALCIUM, INTERACTION
RP   WITH TCN2, DISULFIDE BONDS, AND CHARACTERIZATION OF VARIANT MMATC
RP   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
RT   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.,
RA   Fennell T., O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B.,
RA   Tukiainen T., Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K.,
RA   Zhao F., Zou J., Pierce-Hoffman E., Berghout J., Cooper D.N.,
RA   Deflaux N., DePristo M., Do R., Flannick J., Fromer M., Gauthier L.,
RA   Goldstein J., Gupta N., Howrigan D., Kiezun A., Kurki M.I.,
RA   Moonshine A.L., Natarajan P., Orozco L., Peloso G.M., Poplin R.,
RA   Rivas M.A., Ruano-Rubio V., Rose S.A., Ruderfer D.M., Shakir K.,
RA   Stenson P.D., Stevens C., Thomas B.P., Tiao G., Tusie-Luna M.T.,
RA   Weisburd B., Won H.H., Yu D., Altshuler D.M., Ardissino D.,
RA   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.,
RA   Laakso M., McCarroll S., McCarthy M.I., McGovern D., McPherson R.,
RA   Neale B.M., Palotie A., Purcell S.M., Saleheen D., Scharf J.M.,
RA   Sklar P., Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C.,
RA   Wilson J.G., 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
CC       (TCbl) (PubMed:18779389). Plays an important role in cobalamin
CC       uptake (PubMed:18779389, PubMed:20524213). Plasma membrane protein
CC       that is expressed on follicular dendritic cells (FDC) and mediates
CC       interaction with germinal center B cells (PubMed:10727470).
CC       Functions as costimulator to promote B cell responses to antigenic
CC       stimuli; promotes B cell differentiation and proliferation
CC       (PubMed:10727470, PubMed:11418631). 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)
CC       (PubMed:11418631). CD320 augments the proliferation of PC
CC       precursors generated by IL-10 (PubMed:11418631).
CC       {ECO:0000269|PubMed:10727470, ECO:0000269|PubMed:11418631,
CC       ECO:0000269|PubMed:18779389, 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-
CC       pass 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         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Detected in the germinal center (GC) of
CC       lymphoid follicles (at protein level) (PubMed:11418631). Expressed
CC       abundantly on 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-
CC       bound 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       mutations affecting the gene represented in this entry.
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   PDBsum; 4ZRP; -.
DR   PDBsum; 4ZRQ; -.
DR   SMR; Q9NPF0; -.
DR   BioGrid; 119444; 29.
DR   IntAct; Q9NPF0; 2.
DR   STRING; 9606.ENSP00000301458; -.
DR   iPTMnet; Q9NPF0; -.
DR   PhosphoSitePlus; Q9NPF0; -.
DR   BioMuta; CD320; -.
DR   DMDM; 74734303; -.
DR   EPD; Q9NPF0; -.
DR   jPOST; Q9NPF0; -.
DR   MaxQB; Q9NPF0; -.
DR   PaxDb; Q9NPF0; -.
DR   PeptideAtlas; Q9NPF0; -.
DR   PRIDE; Q9NPF0; -.
DR   ProteomicsDB; 81981; -.
DR   DNASU; 51293; -.
DR   Ensembl; ENST00000301458; ENSP00000301458; ENSG00000167775. [Q9NPF0-1]
DR   Ensembl; ENST00000537716; ENSP00000437697; ENSG00000167775. [Q9NPF0-2]
DR   GeneID; 51293; -.
DR   KEGG; hsa:51293; -.
DR   UCSC; uc002mjj.3; human. [Q9NPF0-1]
DR   CTD; 51293; -.
DR   DisGeNET; 51293; -.
DR   GeneCards; CD320; -.
DR   HGNC; HGNC:16692; CD320.
DR   HPA; HPA014500; -.
DR   HPA; HPA073489; -.
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   eggNOG; KOG1215; Eukaryota.
DR   eggNOG; ENOG410XP34; LUCA.
DR   GeneTree; ENSGT00730000111436; -.
DR   HOGENOM; HOG000111486; -.
DR   InParanoid; Q9NPF0; -.
DR   KO; K06734; -.
DR   OMA; RIEPCTQ; -.
DR   OrthoDB; 1306682at2759; -.
DR   PhylomeDB; Q9NPF0; -.
DR   TreeFam; TF337215; -.
DR   Reactome; R-HSA-196741; Cobalamin (Cbl, vitamin B12) transport and metabolism.
DR   Reactome; R-HSA-3359485; Defective CD320 causes methylmalonic aciduria.
DR   SABIO-RK; Q9NPF0; -.
DR   ChiTaRS; CD320; human.
DR   GeneWiki; CD320; -.
DR   GenomeRNAi; 51293; -.
DR   PRO; PR:Q9NPF0; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   Bgee; ENSG00000167775; Expressed in 209 organ(s), highest expression level in mucosa of transverse colon.
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:0031419; F:cobalamin binding; IDA:MGI.
DR   GO; GO:0015420; F:cobalamin-transporting ATPase activity; TAS:Reactome.
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   Complete proteome; Direct protein sequencing; Disease mutation;
KW   Disulfide bond; Glycoprotein; Growth factor; Membrane; Metal-binding;
KW   Polymorphism; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     35       {ECO:0000269|PubMed:15340161}.
FT   CHAIN        36    282       CD320 antigen.
FT                                /FTId=PRO_0000045798.
FT   TOPO_DOM     36    229       Extracellular. {ECO:0000255}.
FT   TRANSMEM    230    250       Helical. {ECO:0000255}.
FT   TOPO_DOM    251    282       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       53     90       LDL-receptor class A 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      131    168       LDL-receptor class A 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   COMPBIAS    101    104       Poly-Pro.
FT   COMPBIAS    233    236       Poly-Ala.
FT   COMPBIAS    247    250       Poly-Leu.
FT   METAL        72     72       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000244|PDB:4ZRP,
FT                                ECO:0000269|PubMed:27411955}.
FT   METAL        75     75       Calcium 1. {ECO:0000244|PDB:4ZRP,
FT                                ECO:0000269|PubMed:27411955}.
FT   METAL        77     77       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000244|PDB:4ZRP,
FT                                ECO:0000269|PubMed:27411955}.
FT   METAL        79     79       Calcium 1. {ECO:0000244|PDB:4ZRP,
FT                                ECO:0000269|PubMed:27411955}.
FT   METAL        85     85       Calcium 1. {ECO:0000244|PDB:4ZRP,
FT                                ECO:0000269|PubMed:27411955}.
FT   METAL        86     86       Calcium 1. {ECO:0000244|PDB:4ZRP,
FT                                ECO:0000269|PubMed:27411955}.
FT   METAL       150    150       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000244|PDB:4ZRP,
FT                                ECO:0000269|PubMed:27411955}.
FT   METAL       153    153       Calcium 2. {ECO:0000244|PDB:4ZRP,
FT                                ECO:0000269|PubMed:27411955}.
FT   METAL       155    155       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000244|PDB:4ZRP,
FT                                ECO:0000269|PubMed:27411955}.
FT   METAL       157    157       Calcium 2. {ECO:0000244|PDB:4ZRP,
FT                                ECO:0000269|PubMed:27411955}.
FT   METAL       163    163       Calcium 2. {ECO:0000244|PDB:4ZRP,
FT                                ECO:0000269|PubMed:27411955}.
FT   METAL       164    164       Calcium 2. {ECO:0000244|PDB:4ZRP,
FT                                ECO:0000269|PubMed:27411955}.
FT   CARBOHYD    126    126       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    195    195       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    213    213       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     54     67       {ECO:0000244|PDB:4ZRP,
FT                                ECO:0000244|PDB:4ZRQ,
FT                                ECO:0000255|PROSITE-ProRule:PRU00124,
FT                                ECO:0000269|PubMed:27411955}.
FT   DISULFID     61     80       {ECO:0000244|PDB:4ZRP,
FT                                ECO:0000244|PDB:4ZRQ,
FT                                ECO:0000255|PROSITE-ProRule:PRU00124,
FT                                ECO:0000269|PubMed:27411955}.
FT   DISULFID     74     89       {ECO:0000244|PDB:4ZRP,
FT                                ECO:0000255|PROSITE-ProRule:PRU00124,
FT                                ECO:0000269|PubMed:27411955}.
FT   DISULFID    132    145       {ECO:0000244|PDB:4ZRP,
FT                                ECO:0000244|PDB:4ZRQ,
FT                                ECO:0000255|PROSITE-ProRule:PRU00124,
FT                                ECO:0000269|PubMed:27411955}.
FT   DISULFID    139    158       {ECO:0000244|PDB:4ZRP,
FT                                ECO:0000244|PDB:4ZRQ,
FT                                ECO:0000255|PROSITE-ProRule:PRU00124,
FT                                ECO:0000269|PubMed:27411955}.
FT   DISULFID    152    167       {ECO:0000244|PDB:4ZRP,
FT                                ECO:0000244|PDB:4ZRQ,
FT                                ECO:0000255|PROSITE-ProRule:PRU00124,
FT                                ECO:0000269|PubMed:27411955}.
FT   VAR_SEQ      49     90       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_045368.
FT   VARIANT       8      8       Q -> R (in dbSNP:rs2232775).
FT                                {ECO:0000269|Ref.6}.
FT                                /FTId=VAR_047315.
FT   VARIANT      88     88       Missing (in MMATC; unknown pathological
FT                                significance; decreased function in
FT                                cobalamin transport; does not affect
FT                                stability; does not affect interaction
FT                                with TCN2). {ECO:0000269|PubMed:20524213,
FT                                ECO:0000269|PubMed:22819238,
FT                                ECO:0000269|PubMed:27411955,
FT                                ECO:0000269|PubMed:27535533}.
FT                                /FTId=VAR_064080.
FT   VARIANT     142    142       S -> G. {ECO:0000269|PubMed:20524213}.
FT                                /FTId=VAR_077921.
FT   VARIANT     220    220       G -> R (in dbSNP:rs2336573).
FT                                {ECO:0000269|PubMed:20524213}.
FT                                /FTId=VAR_047316.
FT   STRAND       56     60       {ECO:0000244|PDB:4ZRP}.
FT   HELIX        62     64       {ECO:0000244|PDB:4ZRP}.
FT   STRAND       67     69       {ECO:0000244|PDB:4ZRP}.
FT   HELIX        70     72       {ECO:0000244|PDB:4ZRP}.
FT   STRAND       80     82       {ECO:0000244|PDB:4ZRP}.
FT   HELIX        84     86       {ECO:0000244|PDB:4ZRP}.
FT   STRAND      136    138       {ECO:0000244|PDB:4ZRP}.
FT   STRAND      140    143       {ECO:0000244|PDB:4ZRQ}.
FT   STRAND      145    147       {ECO:0000244|PDB:4ZRP}.
FT   HELIX       148    150       {ECO:0000244|PDB:4ZRP}.
FT   STRAND      153    155       {ECO:0000244|PDB:4ZRP}.
FT   HELIX       162    164       {ECO:0000244|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
//
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