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Serotransferrin (Transferrin) (Beta-1 metal-binding globulin) (Siderophilin)

 TRFE_HORSE              Reviewed;         706 AA.
P27425;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
10-MAY-2017, entry version 108.
RecName: Full=Serotransferrin;
Short=Transferrin;
AltName: Full=Beta-1 metal-binding globulin;
AltName: Full=Siderophilin;
Flags: Precursor;
Name=TF;
Equus caballus (Horse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
NCBI_TaxID=9796;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8504171; DOI=10.1016/0167-4781(93)90186-H;
Carpenter M.A., Broad T.E.;
"The cDNA sequence of horse transferrin.";
Biochim. Biophys. Acta 1173:230-232(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Extraembryonic tissue;
McDowell K.J., Adams M.H., Baker C.B.;
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Transferrins are iron binding transport proteins which
can bind two Fe(3+) 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: Monomer.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
-!- SIMILARITY: Belongs to the transferrin family.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
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EMBL; M69020; AAA30958.1; -; mRNA.
EMBL; U21127; AAA63684.1; -; mRNA.
PIR; S33761; S33761.
RefSeq; NP_001075415.2; NM_001081946.2.
UniGene; Eca.1643; -.
ProteinModelPortal; P27425; -.
SMR; P27425; -.
MEROPS; S60.970; -.
PeptideAtlas; P27425; -.
PRIDE; P27425; -.
GeneID; 100034176; -.
KEGG; ecb:100034176; -.
CTD; 7018; -.
HOGENOM; HOG000043759; -.
HOVERGEN; HBG000055; -.
InParanoid; P27425; -.
KO; K14736; -.
Proteomes; UP000002281; Unplaced.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0005615; C:extracellular space; IEA:InterPro.
GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
GO; GO:0015091; F:ferric iron transmembrane transporter activity; IEA:InterPro.
GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
InterPro; IPR030685; Serotransferrin_mammal.
InterPro; IPR016357; Transferrin.
InterPro; IPR001156; Transferrin-like_dom.
InterPro; IPR018195; Transferrin_Fe_BS.
Pfam; PF00405; Transferrin; 2.
PIRSF; PIRSF500682; Serotransferrin; 1.
PIRSF; PIRSF002549; Transferrin; 1.
PRINTS; PR00422; TRANSFERRIN.
SMART; SM00094; TR_FER; 2.
PROSITE; PS00205; TRANSFERRIN_LIKE_1; 2.
PROSITE; PS00206; TRANSFERRIN_LIKE_2; 2.
PROSITE; PS00207; TRANSFERRIN_LIKE_3; 2.
PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
2: Evidence at transcript level;
Complete proteome; Disulfide bond; Glycoprotein; Ion transport; Iron;
Iron transport; Metal-binding; Methylation; Phosphoprotein;
Reference proteome; Repeat; Secreted; Signal; Transport.
SIGNAL 1 19 {ECO:0000250}.
CHAIN 20 706 Serotransferrin.
/FTId=PRO_0000035714.
DOMAIN 23 349 Transferrin-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
DOMAIN 363 691 Transferrin-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 79 79 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 111 111 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 209 209 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 270 270 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 413 413 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 449 449 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 544 544 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 612 612 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 136 136 Carbonate 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 140 140 Carbonate 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 142 142 Carbonate 1; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
BINDING 143 143 Carbonate 1; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
BINDING 476 476 Carbonate 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 480 480 Carbonate 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 482 482 Carbonate 2; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
BINDING 483 483 Carbonate 2; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
MOD_RES 40 40 Dimethylated arginine.
{ECO:0000250|UniProtKB:P12346}.
MOD_RES 391 391 Phosphoserine.
{ECO:0000250|UniProtKB:P02787}.
MOD_RES 693 693 Phosphoserine.
{ECO:0000250|UniProtKB:P02787}.
CARBOHYD 515 515 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 26 64 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 36 55 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 134 215 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 174 190 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 177 198 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 187 200 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 248 262 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 360 623 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 366 398 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 376 389 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 423 701 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 441 664 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 474 550 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 498 692 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 508 522 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 519 533 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 590 604 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 642 647 {ECO:0000255|PROSITE-ProRule:PRU00741}.
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


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