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P12346 (TRFE_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serotransferrin

Short name=Transferrin
Alternative name(s):
Beta-1 metal-binding globulin
Liver regeneration-related protein LRRG03
Siderophilin
Gene names
Name:Tf
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length698 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Monomer.

Subcellular location

Secreted.

Tissue specificity

Expressed by the liver and secreted in plasma.

Sequence similarities

Belongs to the transferrin family.

Contains 2 transferrin-like domains.

Ontologies

Keywords
   Biological processIon transport
Iron transport
Transport
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
   LigandIron
Metal-binding
   PTMDisulfide bond
Glycoprotein
Methylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processacute-phase response

Inferred from expression pattern PubMed 17417667. Source: RGD

apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

cellular iron ion homeostasis

Traceable author statement PubMed 12608731. Source: RGD

cellular response to cAMP

Inferred from expression pattern PubMed 15831523. Source: UniProtKB

cellular response to follicle-stimulating hormone stimulus

Inferred from expression pattern PubMed 15831523. Source: UniProtKB

ferric iron transport

Inferred from direct assay PubMed 17373738. Source: RGD

iron ion transport

Traceable author statement PubMed 12608731. Source: RGD

positive regulation of myelination

Inferred from direct assay PubMed 16480980. Source: RGD

positive regulation of oligodendrocyte progenitor proliferation

Inferred from direct assay PubMed 23368675. Source: RGD

response to hypoxia

Inferred from expression pattern PubMed 16479386. Source: RGD

response to lead ion

Inferred from expression pattern PubMed 23007736. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 16519141. Source: RGD

   Cellular_componentbasement membrane

Inferred from direct assay PubMed 1723977. Source: RGD

extracellular space

Inferred from direct assay PubMed 17350134. Source: RGD

   Molecular_functionferric iron binding

Inferred from direct assay PubMed 17373738. Source: RGD

ferric iron transmembrane transporter activity

Inferred from direct assay PubMed 17373738. Source: RGD

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P12346-1)

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.
Isoform 2 (identifier: P12346-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.7 Ref.8
Chain20 – 698679Serotransferrin
PRO_0000035718

Regions

Domain25 – 347323Transferrin-like 1
Domain360 – 683324Transferrin-like 2

Sites

Metal binding821Iron 1 By similarity
Metal binding1141Iron 1 By similarity
Metal binding2071Iron 1 By similarity
Metal binding2681Iron 1 By similarity
Metal binding4101Iron 2 By similarity
Metal binding4471Iron 2 By similarity
Metal binding5361Iron 2 By similarity
Metal binding6041Iron 2 By similarity
Binding site1391Carbonate 1 By similarity
Binding site1431Carbonate 1 By similarity
Binding site1451Carbonate 1; via amide nitrogen By similarity
Binding site1461Carbonate 1; via amide nitrogen By similarity
Binding site4731Carbonate 2 By similarity
Binding site4771Carbonate 2 By similarity
Binding site4791Carbonate 2; via amide nitrogen By similarity
Binding site4801Carbonate 2; via amide nitrogen By similarity

Amino acid modifications

Modified residue421Omega-N-methylated arginine Ref.11
Glycosylation5121N-linked (GlcNAc...) Potential
Disulfide bond28 ↔ 67 By similarity
Disulfide bond38 ↔ 58 By similarity
Disulfide bond137 ↔ 213 By similarity
Disulfide bond156 ↔ 350 By similarity
Disulfide bond177 ↔ 193 By similarity
Disulfide bond180 ↔ 196 By similarity
Disulfide bond190 ↔ 198 By similarity
Disulfide bond246 ↔ 260 By similarity
Disulfide bond363 ↔ 395 By similarity
Disulfide bond373 ↔ 386 By similarity
Disulfide bond420 ↔ 693 By similarity
Disulfide bond435 ↔ 656 By similarity
Disulfide bond471 ↔ 542 By similarity
Disulfide bond495 ↔ 684 By similarity
Disulfide bond505 ↔ 519 By similarity
Disulfide bond516 ↔ 525 By similarity
Disulfide bond582 ↔ 596 By similarity
Disulfide bond634 ↔ 639 By similarity

Natural variations

Alternative sequence65 – 266202Missing in isoform 2.
VSP_011840

Experimental info

Sequence conflict571A → P in CAA54403. Ref.1
Sequence conflict1101P → R in CAA54403. Ref.1
Sequence conflict3181A → R in CAA54403. Ref.1
Sequence conflict321 – 3233LLR → CYG in BAA07458. Ref.2
Sequence conflict324 – 35431VPPRM…CPEGS → APKDGLQAVPRPQLCHCHSK SAGSCPDA in CAA54403. Ref.1
Sequence conflict3531G → A in BAA07458. Ref.2
Sequence conflict3791S → T in CAA54403. Ref.1
Sequence conflict3791S → T in BAA07458. Ref.2
Sequence conflict3801S → G in CAA54403. Ref.1
Sequence conflict6911E → D in AAA42267. Ref.6
Sequence conflict696 – 6972HK → TA in AAA42267. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 9, 2007. Version 3.
Checksum: B91ABB41CA447194

FASTA69876,395
        10         20         30         40         50         60 
MRFAVGALLA CAALGLCLAV PDKTVKWCAV SEHENTKCIS FRDHMKTVLP ADGPRLACVK 

        70         80         90        100        110        120 
KTSYQDCIKA ISGGEADAIT LDGGWVYDAG LTPNNLKPVA AEFYGSLEHP QTHYLAVAVV 

       130        140        150        160        170        180 
KKGTDFQLNQ LQGKKSCHTG LGRSAGWIIP IGLLFCNLPE PRKPLEKAVA SFFSGSCVPC 

       190        200        210        220        230        240 
ADPVAFPQLC QLCPGCGCSP TQPFFGYVGA FKCLRDGGGD VAFVKHTTIF EVLPQKADRD 

       250        260        270        280        290        300 
QYELLCLDNT RKPVDQYEDC YLARIPSHAV VARNGDGKED LIWEILKVAQ EHFGKGKSKD 

       310        320        330        340        350        360 
FQLFGSPLGK DLLFKDSAFG LLRVPPRMDY RLYLGHSYVT AIRNQREGVC PEGSIDSAPV 

       370        380        390        400        410        420 
KWCALSHQER AKCDEWSVSS NGQIECESAE STEDCIDKIV NGEADAMSLD GGHAYIAGQC 

       430        440        450        460        470        480 
GLVPVMAENY DISSCTNPQS DVFPKGYYAV AVVKASDSSI NWNNLKGKKS CHTGVDRTAG 

       490        500        510        520        530        540 
WNIPMGLLFS RINHCKFDEF FSQGCAPGYK KNSTLCDLCI GPAKCAPNNR EGYNGYTGAF 

       550        560        570        580        590        600 
QCLVEKGDVA FVKHQTVLEN TNGKNTAAWA KDLKQEDFQL LCPDGTKKPV TEFATCHLAQ 

       610        620        630        640        650        660 
APNHVVVSRK EKAARVSTVL TAQKDLFWKG DKDCTGNFCL FRSSTKDLLF RDDTKCLTKL 

       670        680        690 
PEGTTYEEYL GAEYLQAVGN IRKCSTSRLL EACTFHKS 

« Hide

Isoform 2 [UniParc].

Checksum: 7FADB62945314E20
Show »

FASTA49654,524

References

« Hide 'large scale' references
[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]"Organellar proteomics reveals Golgi arginine dimethylation."
Wu C.C., MacCoss M.J., Mardones G., Finnigan C., Mogelsvang S., Yates J.R. III, Howell K.E.
Mol. Biol. Cell 15:2907-2919(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT ARG-42, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS49163.
RefSeqNP_001013128.1. NM_001013110.1. [P12346-1]
UniGeneRn.91296.

3D structure databases

ProteinModelPortalP12346.
SMRP12346. Positions 22-697.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246945. 1 interaction.
IntActP12346. 1 interaction.
MINTMINT-246684.

Protein family/group databases

Allergome1417. Rat n Transferrin.
MEROPSS60.972.

PTM databases

PhosphoSiteP12346.
UniCarbKBP12346.

2D gel databases

World-2DPAGE0004:P12346.

Proteomic databases

PRIDEP12346.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000012946; ENSRNOP00000012946; ENSRNOG00000030625. [P12346-2]
ENSRNOT00000045628; ENSRNOP00000045637; ENSRNOG00000030625. [P12346-1]
GeneID24825.
KEGGrno:24825.
UCSCRGD:3845. rat. [P12346-1]

Organism-specific databases

CTD7018.
RGD3845. Tf.

Phylogenomic databases

GeneTreeENSGT00390000001619.
HOGENOMHOG000043759.
HOVERGENHBG000055.
KOK14736.
PhylomeDBP12346.

Gene expression databases

ArrayExpressP12346.
GenevestigatorP12346.

Family and domain databases

InterProIPR016357. Transferrin.
IPR001156. Transferrin_fam.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PfamPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFPIRSF002549. Transferrin. 1 hit.
PRINTSPR00422. TRANSFERRIN.
SMARTSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEPS00205. 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]
ProtoNetSearch...

Other

NextBio604536.
PROP12346.

Entry information

Entry nameTRFE_RAT
AccessionPrimary (citable) accession number: P12346
Secondary accession number(s): Q63602 expand/collapse secondary AC list , Q64628, Q64630, Q7TNX0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 9, 2007
Last modified: July 9, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families