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Transferrin receptor protein 1 (Transferrin receptor, isoform CRA_a)

 G3V679_RAT              Unreviewed;       761 AA.
G3V679;
16-NOV-2011, integrated into UniProtKB/TrEMBL.
16-NOV-2011, sequence version 1.
23-MAY-2018, entry version 54.
SubName: Full=Transferrin receptor protein 1 {ECO:0000313|Ensembl:ENSRNOP00000002407};
SubName: Full=Transferrin receptor, isoform CRA_a {ECO:0000313|EMBL:EDM11405.1};
Name=Tfrc {ECO:0000313|EMBL:EDM11405.1,
ECO:0000313|Ensembl:ENSRNOP00000002407, ECO:0000313|RGD:70488};
ORFNames=rCG_52708 {ECO:0000313|EMBL:EDM11405.1};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000002407, ECO:0000313|Proteomes:UP000002494};
[1] {ECO:0000313|Ensembl:ENSRNOP00000002407, ECO:0000313|Proteomes:UP000002494}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000002407,
ECO:0000313|Proteomes:UP000002494};
PubMed=15057822; DOI=10.1038/nature02426;
Rat Genome Sequencing Project Consortium;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2] {ECO:0000313|EMBL:EDM11405.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDM11405.1};
PubMed=15632090; DOI=10.1101/gr.2889405;
Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
Istrail S., Li P., Sutton G.;
"Gene and alternative splicing annotation with AIR.";
Genome Res. 15:54-66(2005).
[3] {ECO:0000313|EMBL:EDM11405.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDM11405.1};
Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L.,
Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C.,
Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|Ensembl:ENSRNOP00000002407}
IDENTIFICATION.
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000002407};
Ensembl;
Submitted (SEP-2011) to UniProtKB.
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EMBL; AC136847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH473967; EDM11405.1; -; Genomic_DNA.
RefSeq; NP_073203.1; NM_022712.1.
RefSeq; XP_006248524.1; XM_006248462.3.
RefSeq; XP_006248525.1; XM_006248463.3.
UniGene; Rn.98672; -.
PRIDE; G3V679; -.
Ensembl; ENSRNOT00000002407; ENSRNOP00000002407; ENSRNOG00000001766.
GeneID; 64678; -.
KEGG; rno:64678; -.
CTD; 7037; -.
RGD; 70488; Tfrc.
eggNOG; KOG2195; Eukaryota.
eggNOG; COG2234; LUCA.
GeneTree; ENSGT00550000074421; -.
KO; K06503; -.
OMA; DNSHVEM; -.
OrthoDB; EOG091G02ZM; -.
TreeFam; TF312981; -.
Reactome; R-RNO-432722; Golgi Associated Vesicle Biogenesis.
Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
Reactome; R-RNO-917977; Transferrin endocytosis and recycling.
Proteomes; UP000002494; Chromosome 11.
Bgee; ENSRNOG00000001766; -.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0005905; C:clathrin-coated pit; IEA:Ensembl.
GO; GO:0005769; C:early endosome; IEA:Ensembl.
GO; GO:0010008; C:endosome membrane; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:1990712; C:HFE-transferrin receptor complex; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0055037; C:recycling endosome; IEA:Ensembl.
GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0004998; F:transferrin receptor activity; IEA:Ensembl.
GO; GO:0033570; F:transferrin transmembrane transporter activity; IEA:InterPro.
GO; GO:0006879; P:cellular iron ion homeostasis; IEA:Ensembl.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
GO; GO:0097286; P:iron ion import; IEA:Ensembl.
GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
GO; GO:0030890; P:positive regulation of B cell proliferation; IEA:Ensembl.
GO; GO:0045780; P:positive regulation of bone resorption; IEA:Ensembl.
GO; GO:0045830; P:positive regulation of isotype switching; IEA:Ensembl.
GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0031623; P:receptor internalization; IEA:Ensembl.
CDD; cd02128; PA_TfR; 1.
Gene3D; 1.20.930.40; -; 1.
InterPro; IPR003137; PA_domain.
InterPro; IPR007484; Peptidase_M28.
InterPro; IPR029513; TfR.
InterPro; IPR007365; TFR-like_dimer_dom.
InterPro; IPR036757; TFR-like_dimer_dom_sf.
InterPro; IPR037324; TfR1/2_PA.
PANTHER; PTHR10404:SF26; PTHR10404:SF26; 1.
Pfam; PF02225; PA; 1.
Pfam; PF04389; Peptidase_M28; 1.
Pfam; PF04253; TFR_dimer; 1.
SUPFAM; SSF47672; SSF47672; 1.
1: Evidence at protein level;
Complete proteome {ECO:0000313|Proteomes:UP000002494};
Membrane {ECO:0000256|SAM:Phobius};
Proteomics identification {ECO:0000213|PeptideAtlas:G3V679};
Receptor {ECO:0000313|EMBL:EDM11405.1};
Reference proteome {ECO:0000313|Proteomes:UP000002494};
Transmembrane {ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAM:Phobius}.
TRANSMEM 66 88 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 229 346 PA. {ECO:0000259|Pfam:PF02225}.
DOMAIN 389 577 Peptidase_M28.
{ECO:0000259|Pfam:PF04389}.
DOMAIN 639 750 TFR_dimer. {ECO:0000259|Pfam:PF04253}.
SEQUENCE 761 AA; 85876 MW; 19488AD6D833249D CRC64;
MMDQARSAFS NLFGGEPLSY TRFSLARQVD GDNSHVEMKL AADEEENADS NMKASVRKPK
RFNGRLCFAT IAVVIFFLIG FMIGYLGYCK RVEQKEECVR LAEAEEADKS ENDETEYVPK
SSRLFWADLK TLLSEKLNSI EFTDIIKQLS QNTYTPREAG SQKDENLAYY IENLFHDFKF
SKVWRDEHYV KIQVKNSVSQ NLVTINSGSN IDPVEAPEGY VAFSKAGEVT GKLVHANFGT
KKDFEELNYS VNGSLVIVRA GKITFAEKVA NAQSFNAIGV LIYMDRNTFP VVEADLQFFG
HAHLGTGDPY TPGFPSFNHT QFPPSQSSGL PSIPVQTISR AAAEKLFKNM EGNCPPSWNI
DSSCKLELSQ NQNVKLTVNN VLKETRILNI FGVIKGYEEP DRYIVVGAQR DAWGPGVAKS
SVGTGLLLKL AQVFSDMISK DGFRPSRSII FASWTAGDYG AVGATEWLEG YLSSLHLKAF
TYINLDKVVL GTSNFKVSAS PLLYTLMGKI MQDVKHPIDG KYLYRDSNWI SKIEELSLDN
AAFPFLAYSG IPAVSFCFCE DEDYPYLGTK LDTYEILIQK VPQLNQMVRT AAEVAGQFII
KLTHDIELTL DYEMYNSKLL SFMKDLNQFK ADIKDMGLSL QWLYSARGDY FRATSRLTTD
FHNAEKTNRF VMREINDRIM KVEYHFLSPY VSPRESPFRH IFWGSGSHTL SALVENLRLR
QKNITAFNET LFRNQLALAT WTIQGVANAL SGDIWNIDNE F


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