TRFE_HORSE
ID TRFE_HORSE Reviewed; 706 AA.
AC P27425;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Serotransferrin;
DE Short=Transferrin;
DE AltName: Full=Beta-1 metal-binding globulin;
DE AltName: Full=Siderophilin;
DE Flags: Precursor;
GN Name=TF;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8504171; DOI=10.1016/0167-4781(93)90186-h;
RA Carpenter M.A., Broad T.E.;
RT "The cDNA sequence of horse transferrin.";
RL Biochim. Biophys. Acta 1173:230-232(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Extraembryonic tissue;
RA McDowell K.J., Adams M.H., Baker C.B.;
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transferrins are iron binding transport proteins which can
CC bind two Fe(3+) ions in association with the binding of an anion,
CC usually bicarbonate. It is responsible for the transport of iron from
CC sites of absorption and heme degradation to those of storage and
CC utilization. Serum transferrin may also have a further role in
CC stimulating cell proliferation.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC -!- SIMILARITY: Belongs to the transferrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00741}.
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DR EMBL; M69020; AAA30958.1; -; mRNA.
DR EMBL; U21127; AAA63684.1; -; mRNA.
DR PIR; S33761; S33761.
DR RefSeq; NP_001075415.2; NM_001081946.2.
DR AlphaFoldDB; P27425; -.
DR SMR; P27425; -.
DR STRING; 9796.ENSECAP00000050263; -.
DR MEROPS; S60.970; -.
DR PeptideAtlas; P27425; -.
DR PRIDE; P27425; -.
DR GeneID; 100034176; -.
DR KEGG; ecb:100034176; -.
DR CTD; 7018; -.
DR InParanoid; P27425; -.
DR OrthoDB; 232859at2759; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
DR GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR InterPro; IPR030685; Serotransferrin_mammal.
DR InterPro; IPR016357; Transferrin.
DR InterPro; IPR001156; Transferrin-like_dom.
DR InterPro; IPR018195; Transferrin_Fe_BS.
DR Pfam; PF00405; Transferrin; 2.
DR PIRSF; PIRSF500682; Serotransferrin; 1.
DR PIRSF; PIRSF002549; Transferrin; 1.
DR PRINTS; PR00422; TRANSFERRIN.
DR SMART; SM00094; TR_FER; 2.
DR PROSITE; PS00205; TRANSFERRIN_LIKE_1; 2.
DR PROSITE; PS00206; TRANSFERRIN_LIKE_2; 2.
DR PROSITE; PS00207; TRANSFERRIN_LIKE_3; 2.
DR PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Ion transport; Iron; Iron transport;
KW Metal-binding; Methylation; Phosphoprotein; Reference proteome; Repeat;
KW Secreted; Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..706
FT /note="Serotransferrin"
FT /id="PRO_0000035714"
FT DOMAIN 23..349
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 363..691
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 79
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 111
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 136
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 140
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 142
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 143
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 209
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 270
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 413
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 449
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 476
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 480
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 482
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 483
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 544
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 612
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT MOD_RES 40
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:P12346"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02787"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02787"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 36..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 134..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 174..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 177..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 187..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 248..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 360..623
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 366..398
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 376..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 423..701
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 441..664
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 474..550
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 498..692
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 508..522
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 519..533
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 590..604
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 642..647
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
SQ SEQUENCE 706 AA; 78095 MW; 1A0FA566C0409D8A CRC64;
MRLAIRALLA CAVLGLCLAE QTVRWCTVSN HEVSKCASFR DSMKSIVPAP PLVACVKRTS
YLECIKAIAD NEADAVTLDA GLVFEAGLSP YNLKPVVAEF YGSKTEPQTH YYAVAVVKKN
SNFQLNQLQG KKSCHTGLGR SAGWNIPIGL LYWQLPEPRE SLQKAVSNFF AGSCVPCADR
TAVPNLCQLC VGKGTDKCAC SNHEPYFGYS GAFKCLADGA GDVAFVKHST VLENLPQEAD
RDEYQLLCRD NTRKSVDEYK DCYLASIPSH AVVARSVDGK EDLIWGLLNQ AQEHFGTEKS
KDFHLFSSPH GKDLLFKDSA LGFLRIPPAM DTWLYLGYEY VTAIRNLRED IRPEVPKDEC
KKVKWCAIGH HEKVKCDEWS VNSGGNIECE SAQSTEDCIA KIVKGEADAM SLDGGFIYIA
GKCGLVPVLA ENYETRSGSA CVDTPEEGYH AVAVVKSSSD PDLTWNSLKG KKSCHTGVDR
TAGWNIPMGL LYSEIKHCEF DKFFREGCAP GYRRNSTLCN LCIGSASGPG RECEPNNHER
YYGYTGAFRC LVEKGDVAFV KHQTVEQNTD GRNPDDWAKD LKSENFKLLC PDGTRKSVTE
FKSCYLARAP NHAVVSRKEK AACVCQELHN QQASYGKNGS HCPDKFCLFQ SATKDLLFRD
DTQCLANLQP TTTYKTYLGE KYLTAVANLR QCSTSRLLEA CTFHRV
