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P27425 (TRFE_HORSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Serotransferrin
Short name=Transferrin
Alternative name(s):
Beta-1 metal-binding globulin
Siderophilin
Gene names
Name:TF
OrganismEquus caballus (Horse) [Reference proteome]
Taxonomic identifier9796 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus ›

Protein attributes

Sequence length706 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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
   DomainRepeat
Signal
   LigandIron
Metal-binding
   PTMDisulfide bond
Glycoprotein
Methylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular iron ion homeostasis

Inferred from electronic annotation. Source: InterPro

iron ion transport

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionferric iron binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Chain20 – 706687Serotransferrin
PRO_0000035714

Regions

Domain23 – 349327Transferrin-like 1
Domain363 – 691329Transferrin-like 2

Sites

Metal binding791Iron 1 By similarity
Metal binding1111Iron 1 By similarity
Metal binding2091Iron 1 By similarity
Metal binding2701Iron 1 By similarity
Metal binding4131Iron 2 By similarity
Metal binding4491Iron 2 By similarity
Metal binding5441Iron 2 By similarity
Metal binding6121Iron 2 By similarity
Binding site1361Carbonate 1 By similarity
Binding site1401Carbonate 1 By similarity
Binding site1421Carbonate 1; via amide nitrogen By similarity
Binding site1431Carbonate 1; via amide nitrogen By similarity
Binding site4761Carbonate 2 By similarity
Binding site4801Carbonate 2 By similarity
Binding site4821Carbonate 2; via amide nitrogen By similarity
Binding site4831Carbonate 2; via amide nitrogen By similarity

Amino acid modifications

Modified residue401Omega-N-methylated arginine By similarity
Glycosylation5151N-linked (GlcNAc...) Potential
Disulfide bond26 ↔ 64 By similarity
Disulfide bond36 ↔ 55 By similarity
Disulfide bond134 ↔ 215 By similarity
Disulfide bond174 ↔ 190 By similarity
Disulfide bond177 ↔ 198 By similarity
Disulfide bond187 ↔ 200 By similarity
Disulfide bond248 ↔ 262 By similarity
Disulfide bond360 ↔ 623 By similarity
Disulfide bond366 ↔ 398 By similarity
Disulfide bond376 ↔ 389 By similarity
Disulfide bond423 ↔ 701 By similarity
Disulfide bond441 ↔ 664 By similarity
Disulfide bond474 ↔ 550 By similarity
Disulfide bond498 ↔ 692 By similarity
Disulfide bond508 ↔ 522 By similarity
Disulfide bond519 ↔ 533 By similarity
Disulfide bond590 ↔ 604 By similarity
Disulfide bond642 ↔ 647 By similarity

Sequences

Sequence LengthMass (Da)Tools
P27425 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 1A0FA566C0409D8A

FASTA70678,095
        10         20         30         40         50         60 
MRLAIRALLA CAVLGLCLAE QTVRWCTVSN HEVSKCASFR DSMKSIVPAP PLVACVKRTS 

        70         80         90        100        110        120 
YLECIKAIAD NEADAVTLDA GLVFEAGLSP YNLKPVVAEF YGSKTEPQTH YYAVAVVKKN 

       130        140        150        160        170        180 
SNFQLNQLQG KKSCHTGLGR SAGWNIPIGL LYWQLPEPRE SLQKAVSNFF AGSCVPCADR 

       190        200        210        220        230        240 
TAVPNLCQLC VGKGTDKCAC SNHEPYFGYS GAFKCLADGA GDVAFVKHST VLENLPQEAD 

       250        260        270        280        290        300 
RDEYQLLCRD NTRKSVDEYK DCYLASIPSH AVVARSVDGK EDLIWGLLNQ AQEHFGTEKS 

       310        320        330        340        350        360 
KDFHLFSSPH GKDLLFKDSA LGFLRIPPAM DTWLYLGYEY VTAIRNLRED IRPEVPKDEC 

       370        380        390        400        410        420 
KKVKWCAIGH HEKVKCDEWS VNSGGNIECE SAQSTEDCIA KIVKGEADAM SLDGGFIYIA 

       430        440        450        460        470        480 
GKCGLVPVLA ENYETRSGSA CVDTPEEGYH AVAVVKSSSD PDLTWNSLKG KKSCHTGVDR 

       490        500        510        520        530        540 
TAGWNIPMGL LYSEIKHCEF DKFFREGCAP GYRRNSTLCN LCIGSASGPG RECEPNNHER 

       550        560        570        580        590        600 
YYGYTGAFRC LVEKGDVAFV KHQTVEQNTD GRNPDDWAKD LKSENFKLLC PDGTRKSVTE 

       610        620        630        640        650        660 
FKSCYLARAP NHAVVSRKEK AACVCQELHN QQASYGKNGS HCPDKFCLFQ SATKDLLFRD 

       670        680        690        700 
DTQCLANLQP TTTYKTYLGE KYLTAVANLR QCSTSRLLEA CTFHRV

« Hide

References

[1]"The cDNA sequence of horse transferrin."
Carpenter M.A., Broad T.E.
Biochim. Biophys. Acta 1173:230-232(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]McDowell K.J., Adams M.H., Baker C.B.
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Extraembryonic tissue.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M69020 mRNA. Translation: AAA30958.1.
U21127 mRNA. Translation: AAA63684.1.
PIRS33761.
RefSeqNP_001075415.1. NM_001081946.1.
UniGeneEca.1643.

3D structure databases

ProteinModelPortalP27425.
SMRP27425. Positions 20-704.
ModBaseSearch...

Protein family/group databases

MEROPSS60.971.

Proteomic databases

PRIDEP27425.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100034176.
KEGGecb:100034176.

Organism-specific databases

CTD7018.

Phylogenomic databases

eggNOGCOG2229.
HOGENOMHOG000043759.
HOVERGENHBG000055.
InParanoidP27425.
KOK14736.
OrthoDBEOG4CRKZG.

Family and domain databases

InterProIPR016357. Transferrin.
IPR001156. Transferrin_fam.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PANTHERPTHR11485. PTHR11485. 1 hit.
PfamPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFPIRSF002549. Transferrin. 1 hit.
PRINTSPR00422. TRANSFERRIN.
SMARTSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEPS00205. TRANSFERRIN_LIKE_1. 2 hits.
PS00206. TRANSFERRIN_LIKE_2. 2 hits.
PS00207. TRANSFERRIN_LIKE_3. 2 hits.
PS51408. TRANSFERRIN_LIKE_4. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRFE_HORSE
AccessionPrimary (citable) accession number: P27425
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: April 3, 2013
This is version 87 of the entry and version 1 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

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