TRFE_PANTR
ID TRFE_PANTR Reviewed; 698 AA.
AC A5A6I6;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cerebellum;
RX PubMed=17574350; DOI=10.1016/j.gene.2007.04.013;
RA Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I.,
RA Kusuda J., Gojobori T., Hashimoto K., Hirai M.;
RT "Mapping of chimpanzee full-length cDNAs onto the human genome unveils
RT large potential divergence of the transcriptome.";
RL Gene 399:1-10(2007).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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; AB222114; BAF62359.1; -; mRNA.
DR RefSeq; NP_001138307.1; NM_001144835.1.
DR AlphaFoldDB; A5A6I6; -.
DR SMR; A5A6I6; -.
DR STRING; 9598.ENSPTRP00000026561; -.
DR MEROPS; S60.975; -.
DR PaxDb; A5A6I6; -.
DR PRIDE; A5A6I6; -.
DR Ensembl; ENSPTRT00000028781; ENSPTRP00000026561; ENSPTRG00000015412.
DR GeneID; 460710; -.
DR KEGG; ptr:460710; -.
DR CTD; 7018; -.
DR VGNC; VGNC:12236; TF.
DR eggNOG; ENOG502QT0C; Eukaryota.
DR GeneTree; ENSGT00940000154388; -.
DR HOGENOM; CLU_011309_1_0_1; -.
DR InParanoid; A5A6I6; -.
DR OMA; SGNFCLF; -.
DR OrthoDB; 232859at2759; -.
DR TreeFam; TF324013; -.
DR Proteomes; UP000002277; Chromosome 3.
DR Bgee; ENSPTRG00000015412; Expressed in liver and 18 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0009925; C:basal plasma membrane; IEA:Ensembl.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0031232; C:extrinsic component of external side of plasma membrane; IEA:Ensembl.
DR GO; GO:1990712; C:HFE-transferrin receptor complex; IEA:Ensembl.
DR GO; GO:0005770; C:late endosome; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0008198; F:ferrous iron binding; IEA:Ensembl.
DR GO; GO:0034986; F:iron chaperone activity; IEA:Ensembl.
DR GO; GO:1990459; F:transferrin receptor binding; IEA:Ensembl.
DR GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
DR GO; GO:0019731; P:antibacterial humoral response; IBA:GO_Central.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
DR GO; GO:0071281; P:cellular response to iron ion; IEA:Ensembl.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
DR GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0045780; P:positive regulation of bone resorption; IEA:Ensembl.
DR GO; GO:2000147; P:positive regulation of cell motility; IEA:Ensembl.
DR GO; GO:0042327; P:positive regulation of phosphorylation; IEA:Ensembl.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0034756; P:regulation of iron ion transport; IEA:Ensembl.
DR GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
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..698
FT /note="Serotransferrin"
FT /id="PRO_0000309747"
FT DOMAIN 25..347
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 361..683
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 82
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 114
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 139
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 145
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 146
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 207
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 268
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 411
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 445
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 471
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 475
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 477
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 478
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 536
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 604
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT MOD_RES 42
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:P12346"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02787"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02787"
FT CARBOHYD 51
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 38..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 137..213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 156..350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 177..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 180..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 190..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 246..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 358..615
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 364..396
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 374..387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 421..693
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 437..656
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 469..542
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 493..684
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 503..517
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 514..525
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 582..596
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 634..639
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
SQ SEQUENCE 698 AA; 77064 MW; 0A526FDBEDD0B237 CRC64;
MRLAVGALLV CAVLGLCLAV PDKTVRWCAV SEHEATKCQS FRDHMKSVIP SDGPSVACVK
KASYLDCIRA IAANEADAVT LDAGLVYDAY LAPNNLKPVV AEFYGSKEDP QTFYYAVAVV
KKDSGFQMNQ LRGKKSCHTG LGRSAGWNIP IGLLYCDLPE PRKPLEKAVA NFFSGSCAPC
ADGTDFPQLC QLCPGCGCST LNQYFGYSGA FKCLKDGAGD VAFVKHSTIF ENLANKADRD
QYELLCLDNT RKPVDEYKDC HLAQVPSHTV VARSMGGKED LIWELLNQAQ EHFGKDKSKE
FQLFSSPHGK DLLFKDSAHG FLKVPPRMDA KMYLGYEYVT AIRNLREGTC PEATTDECKP
VKWCALSHHE RLKCDEWSVN SVGKIECVSA ETTEDCIAKI MNGEADAMSL DGGFVYIAGK
CGLVPVLAEN YNKNDNCEDT PEAGYFAVAV VKKSASDLTW DNLKGKKSCH TAVGRTAGWN
IPMGLLYNKI NHCRFDEFFS EGCAPGSKKD SSLCKLCMGS GPNLCEPNNK EGYYGYTGAF
RCLVEKGDVA FVKHQTVPQN TGGKNPDPWA KNLNEKDYEL LCLDGTRKPV KEYANCHLAR
APNHAVVTRK DKEACVHKIL RQQQHLFGSN VTDCSGNFCL FRSETKDLLF RDDTVCLAKL
HDRNTYEKYL GEEYVKAVGN LRKCSTSSLL EACTFRRP
