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P12346

- TRFE_RAT

UniProt

P12346 - TRFE_RAT

Protein

Serotransferrin

Gene

Tf

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 3 (09 Jan 2007)
      Previous versions | rss
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    Functioni

    Transferrins are iron binding transport proteins which can bind two Fe3+ ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi82 – 821Iron 1PROSITE-ProRule annotation
    Metal bindingi114 – 1141Iron 1PROSITE-ProRule annotation
    Binding sitei139 – 1391Carbonate 1PROSITE-ProRule annotation
    Binding sitei143 – 1431Carbonate 1PROSITE-ProRule annotation
    Binding sitei145 – 1451Carbonate 1; via amide nitrogenPROSITE-ProRule annotation
    Binding sitei146 – 1461Carbonate 1; via amide nitrogenPROSITE-ProRule annotation
    Metal bindingi207 – 2071Iron 1PROSITE-ProRule annotation
    Metal bindingi268 – 2681Iron 1PROSITE-ProRule annotation
    Metal bindingi410 – 4101Iron 2PROSITE-ProRule annotation
    Metal bindingi447 – 4471Iron 2PROSITE-ProRule annotation
    Binding sitei473 – 4731Carbonate 2PROSITE-ProRule annotation
    Binding sitei477 – 4771Carbonate 2PROSITE-ProRule annotation
    Binding sitei479 – 4791Carbonate 2; via amide nitrogenPROSITE-ProRule annotation
    Binding sitei480 – 4801Carbonate 2; via amide nitrogenPROSITE-ProRule annotation
    Metal bindingi536 – 5361Iron 2PROSITE-ProRule annotation
    Metal bindingi604 – 6041Iron 2PROSITE-ProRule annotation

    GO - Molecular functioni

    1. ferric iron binding Source: RGD
    2. ferric iron transmembrane transporter activity Source: RGD

    GO - Biological processi

    1. acute-phase response Source: RGD
    2. apoptotic process Source: UniProtKB
    3. cellular iron ion homeostasis Source: RGD
    4. cellular response to cAMP Source: UniProtKB
    5. cellular response to follicle-stimulating hormone stimulus Source: UniProtKB
    6. ferric iron transport Source: RGD
    7. iron ion transport Source: RGD
    8. positive regulation of myelination Source: RGD
    9. positive regulation of oligodendrocyte progenitor proliferation Source: RGD
    10. response to hypoxia Source: RGD
    11. response to lead ion Source: RGD
    12. response to organic cyclic compound Source: RGD

    Keywords - Biological processi

    Ion transport, Iron transport, Transport

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_196255. Transferrin endocytosis and recycling.

    Protein family/group databases

    MEROPSiS60.972.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serotransferrin
    Short name:
    Transferrin
    Alternative name(s):
    Beta-1 metal-binding globulin
    Liver regeneration-related protein LRRG03
    Siderophilin
    Gene namesi
    Name:Tf
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 8

    Organism-specific databases

    RGDi3845. Tf.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: RGD
    2. extracellular space Source: RGD

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Protein family/group databases

    Allergomei1417. Rat n Transferrin.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19192 PublicationsAdd
    BLAST
    Chaini20 – 698679SerotransferrinPRO_0000035718Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi28 ↔ 67PROSITE-ProRule annotation
    Disulfide bondi38 ↔ 58PROSITE-ProRule annotation
    Modified residuei42 – 421Omega-N-methylated arginine1 Publication
    Disulfide bondi137 ↔ 213PROSITE-ProRule annotation
    Disulfide bondi156 ↔ 350PROSITE-ProRule annotation
    Disulfide bondi177 ↔ 193PROSITE-ProRule annotation
    Disulfide bondi180 ↔ 196PROSITE-ProRule annotation
    Disulfide bondi190 ↔ 198PROSITE-ProRule annotation
    Disulfide bondi246 ↔ 260PROSITE-ProRule annotation
    Disulfide bondi363 ↔ 395PROSITE-ProRule annotation
    Disulfide bondi373 ↔ 386PROSITE-ProRule annotation
    Disulfide bondi420 ↔ 693PROSITE-ProRule annotation
    Disulfide bondi435 ↔ 656PROSITE-ProRule annotation
    Disulfide bondi471 ↔ 542PROSITE-ProRule annotation
    Disulfide bondi495 ↔ 684PROSITE-ProRule annotation
    Disulfide bondi505 ↔ 519PROSITE-ProRule annotation
    Glycosylationi512 – 5121N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi516 ↔ 525PROSITE-ProRule annotation
    Disulfide bondi582 ↔ 596PROSITE-ProRule annotation
    Disulfide bondi634 ↔ 639PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Methylation

    Proteomic databases

    PRIDEiP12346.

    2D gel databases

    World-2DPAGE0004:P12346.

    PTM databases

    PhosphoSiteiP12346.
    UniCarbKBiP12346.

    Expressioni

    Tissue specificityi

    Expressed by the liver and secreted in plasma.

    Gene expression databases

    ArrayExpressiP12346.
    GenevestigatoriP12346.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    BioGridi246945. 1 interaction.
    IntActiP12346. 1 interaction.
    MINTiMINT-246684.

    Structurei

    3D structure databases

    ProteinModelPortaliP12346.
    SMRiP12346. Positions 22-697.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 347323Transferrin-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini360 – 683324Transferrin-like 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the transferrin family.PROSITE-ProRule annotation
    Contains 2 transferrin-like domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    GeneTreeiENSGT00390000001619.
    HOGENOMiHOG000043759.
    HOVERGENiHBG000055.
    KOiK14736.
    PhylomeDBiP12346.

    Family and domain databases

    InterProiIPR016357. Transferrin.
    IPR001156. Transferrin-like_dom.
    IPR018195. Transferrin_Fe_BS.
    [Graphical view]
    PfamiPF00405. Transferrin. 2 hits.
    [Graphical view]
    PIRSFiPIRSF002549. Transferrin. 1 hit.
    PRINTSiPR00422. TRANSFERRIN.
    SMARTiSM00094. TR_FER. 2 hits.
    [Graphical view]
    PROSITEiPS00205. TRANSFERRIN_LIKE_1. 1 hit.
    PS00206. TRANSFERRIN_LIKE_2. 2 hits.
    PS00207. TRANSFERRIN_LIKE_3. 2 hits.
    PS51408. TRANSFERRIN_LIKE_4. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P12346-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MRFAVGALLA CAALGLCLAV PDKTVKWCAV SEHENTKCIS FRDHMKTVLP    50
    ADGPRLACVK KTSYQDCIKA ISGGEADAIT LDGGWVYDAG LTPNNLKPVA 100
    AEFYGSLEHP QTHYLAVAVV KKGTDFQLNQ LQGKKSCHTG LGRSAGWIIP 150
    IGLLFCNLPE PRKPLEKAVA SFFSGSCVPC ADPVAFPQLC QLCPGCGCSP 200
    TQPFFGYVGA FKCLRDGGGD VAFVKHTTIF EVLPQKADRD QYELLCLDNT 250
    RKPVDQYEDC YLARIPSHAV VARNGDGKED LIWEILKVAQ EHFGKGKSKD 300
    FQLFGSPLGK DLLFKDSAFG LLRVPPRMDY RLYLGHSYVT AIRNQREGVC 350
    PEGSIDSAPV KWCALSHQER AKCDEWSVSS NGQIECESAE STEDCIDKIV 400
    NGEADAMSLD GGHAYIAGQC GLVPVMAENY DISSCTNPQS DVFPKGYYAV 450
    AVVKASDSSI NWNNLKGKKS CHTGVDRTAG WNIPMGLLFS RINHCKFDEF 500
    FSQGCAPGYK KNSTLCDLCI GPAKCAPNNR EGYNGYTGAF QCLVEKGDVA 550
    FVKHQTVLEN TNGKNTAAWA KDLKQEDFQL LCPDGTKKPV TEFATCHLAQ 600
    APNHVVVSRK EKAARVSTVL TAQKDLFWKG DKDCTGNFCL FRSSTKDLLF 650
    RDDTKCLTKL PEGTTYEEYL GAEYLQAVGN IRKCSTSRLL EACTFHKS 698
    Length:698
    Mass (Da):76,395
    Last modified:January 9, 2007 - v3
    Checksum:iB91ABB41CA447194
    GO
    Isoform 2 (identifier: P12346-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         65-266: Missing.

    Show »
    Length:496
    Mass (Da):54,524
    Checksum:i7FADB62945314E20
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti57 – 571A → P in CAA54403. (PubMed:7717992)Curated
    Sequence conflicti110 – 1101P → R in CAA54403. (PubMed:7717992)Curated
    Sequence conflicti318 – 3181A → R in CAA54403. (PubMed:7717992)Curated
    Sequence conflicti321 – 3233LLR → CYG in BAA07458. (PubMed:8829802)Curated
    Sequence conflicti324 – 35431VPPRM…CPEGS → APKDGLQAVPRPQLCHCHSK SAGSCPDA in CAA54403. (PubMed:7717992)CuratedAdd
    BLAST
    Sequence conflicti353 – 3531G → A in BAA07458. (PubMed:8829802)Curated
    Sequence conflicti379 – 3791S → T in CAA54403. (PubMed:7717992)Curated
    Sequence conflicti379 – 3791S → T in BAA07458. (PubMed:8829802)Curated
    Sequence conflicti380 – 3801S → G in CAA54403. (PubMed:7717992)Curated
    Sequence conflicti691 – 6911E → D in AAA42267. (PubMed:3023031)Curated
    Sequence conflicti696 – 6972HK → TA in AAA42267. (PubMed:3023031)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei65 – 266202Missing in isoform 2. 1 PublicationVSP_011840Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X77158 mRNA. Translation: CAA54403.1.
    D38380 mRNA. Translation: BAA07458.1.
    AY327504 mRNA. Translation: AAP97736.1.
    BC087021 mRNA. Translation: AAH87021.1.
    M26113 mRNA. Translation: AAA42266.1.
    M27966 mRNA. Translation: AAA42267.1.
    PIRiS49163.
    RefSeqiNP_001013128.1. NM_001013110.1. [P12346-1]
    UniGeneiRn.91296.

    Genome annotation databases

    EnsembliENSRNOT00000012946; ENSRNOP00000012946; ENSRNOG00000030625. [P12346-2]
    ENSRNOT00000045628; ENSRNOP00000045637; ENSRNOG00000030625. [P12346-1]
    GeneIDi24825.
    KEGGirno:24825.
    UCSCiRGD:3845. rat. [P12346-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X77158 mRNA. Translation: CAA54403.1 .
    D38380 mRNA. Translation: BAA07458.1 .
    AY327504 mRNA. Translation: AAP97736.1 .
    BC087021 mRNA. Translation: AAH87021.1 .
    M26113 mRNA. Translation: AAA42266.1 .
    M27966 mRNA. Translation: AAA42267.1 .
    PIRi S49163.
    RefSeqi NP_001013128.1. NM_001013110.1. [P12346-1 ]
    UniGenei Rn.91296.

    3D structure databases

    ProteinModelPortali P12346.
    SMRi P12346. Positions 22-697.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246945. 1 interaction.
    IntActi P12346. 1 interaction.
    MINTi MINT-246684.

    Protein family/group databases

    Allergomei 1417. Rat n Transferrin.
    MEROPSi S60.972.

    PTM databases

    PhosphoSitei P12346.
    UniCarbKBi P12346.

    2D gel databases

    World-2DPAGE 0004:P12346.

    Proteomic databases

    PRIDEi P12346.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000012946 ; ENSRNOP00000012946 ; ENSRNOG00000030625 . [P12346-2 ]
    ENSRNOT00000045628 ; ENSRNOP00000045637 ; ENSRNOG00000030625 . [P12346-1 ]
    GeneIDi 24825.
    KEGGi rno:24825.
    UCSCi RGD:3845. rat. [P12346-1 ]

    Organism-specific databases

    CTDi 7018.
    RGDi 3845. Tf.

    Phylogenomic databases

    GeneTreei ENSGT00390000001619.
    HOGENOMi HOG000043759.
    HOVERGENi HBG000055.
    KOi K14736.
    PhylomeDBi P12346.

    Enzyme and pathway databases

    Reactomei REACT_196255. Transferrin endocytosis and recycling.

    Miscellaneous databases

    NextBioi 604536.
    PROi P12346.

    Gene expression databases

    ArrayExpressi P12346.
    Genevestigatori P12346.

    Family and domain databases

    InterProi IPR016357. Transferrin.
    IPR001156. Transferrin-like_dom.
    IPR018195. Transferrin_Fe_BS.
    [Graphical view ]
    Pfami PF00405. Transferrin. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF002549. Transferrin. 1 hit.
    PRINTSi PR00422. TRANSFERRIN.
    SMARTi SM00094. TR_FER. 2 hits.
    [Graphical view ]
    PROSITEi PS00205. TRANSFERRIN_LIKE_1. 1 hit.
    PS00206. TRANSFERRIN_LIKE_2. 2 hits.
    PS00207. TRANSFERRIN_LIKE_3. 2 hits.
    PS51408. TRANSFERRIN_LIKE_4. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Rat mammary-gland transferrin: nucleotide sequence, phylogenetic analysis and glycan structure."
      Escriva H., Pierce A., Coddeville B., Gonzalez F., Benaissa M., Leger D., Wieruszeski J.-M., Spik G., Pamblanco M.
      Biochem. J. 307:47-55(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: Wistar.
      Tissue: Mammary gland.
    2. "Complete sequence analysis of rat transferrin and expression of transferrin but not lactoferrin in the digestive glands."
      Hosino A., Hisayasu S., Shimada T.
      Comp. Biochem. Physiol. 113B:491-497(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: Wistar.
      Tissue: Liver.
    3. "Liver regeneration after PH."
      Xu C.S., Li W.Q., Li Y.C., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y., Yang K.J., Yan H.M., Chang C.F., Zhao L.F., Ma H., Wang L., Wang S.F., Shi J.B., Rahman S., Wang Q.N., Zhang J.B.
      Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Testis.
    5. "Synthesis of rat transferrin in Escherichia coli containing a recombinant bacteriophage."
      Aldred A.R., Howlett G.J., Schreiber G.
      Biochem. Biophys. Res. Commun. 122:960-965(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-295 (ISOFORM 2).
    6. "Transferrin messenger ribonucleic acid: molecular cloning and hormonal regulation in rat Sertoli cells."
      Huggenvik J.I., Idzerda R.L., Haywood L., Lee D.C., McKnight G.S., Griswold M.D.
      Endocrinology 120:332-340(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 521-698.
    7. "The synthesis and secretion of rat transferrin."
      Schreiber G., Dryburgh H., Millership A., Matsuda Y., Inglis A., Phillips J., Edwards K., Maggs J.
      J. Biol. Chem. 254:12013-12019(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-47.
    8. "Properties of the transferrin associated with rat intestinal mucosa."
      Purves L.R., Purves M., Linton N., Brandt W., Johnson G., Jacobs P.
      Biochim. Biophys. Acta 966:318-327(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-30 AND 642-653.
    9. "Lung-derived growth factor that stimulates the growth of lung-metastasizing tumor cells: identification as transferrin."
      Cavanaugh P.G., Nicolson G.L.
      J. Cell. Biochem. 47:261-271(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 89-102; 232-243 AND 404-411.
    10. Lubec G., Afjehi-Sadat L., Kang S.U.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 144-162; 240-251; 332-343; 588-609; 616-624; 630-642 AND 660-682, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Brain and Spinal cord.
    11. Cited for: METHYLATION AT ARG-42, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiTRFE_RAT
    AccessioniPrimary (citable) accession number: P12346
    Secondary accession number(s): Q63602
    , Q64628, Q64630, Q7TNX0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 9, 2007
    Last modified: October 1, 2014
    This is version 129 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3