TRFE1_SALSA
ID TRFE1_SALSA Reviewed; 690 AA.
AC P80426;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Serotransferrin-1;
DE AltName: Full=Serotransferrin I;
DE Short=STF I;
DE Short=sTF1;
DE AltName: Full=Siderophilin I;
DE Flags: Precursor;
GN Name=tf1;
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8293074;
RA Kvingedal A.M., Roervik K.A., Alestroem P.;
RT "Cloning and characterization of Atlantic salmon (Salmo salar) serum
RT transferrin cDNA.";
RL Mol. Mar. Biol. Biotechnol. 2:233-238(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
RX PubMed=7821802; DOI=10.1016/0378-1119(94)90448-0;
RA Kvingedal A.M.;
RT "Characterization of the 5' region of the Atlantic salmon (Salmo salar)
RT transferrin-encoding gene.";
RL Gene 150:335-339(1994).
RN [3]
RP PROTEIN SEQUENCE OF 19-37.
RC TISSUE=Serum;
RA Roeed K.H., Dehli A.K., Flengsrud R., Midthjell L., Roervik K.A.;
RT "Immunoassay and partial characterization of serum transferrin from
RT Atlantic salon (Salmo salr L.).";
RL Fish Shellfish Immunol. 5:71-80(1995).
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: Abundant in liver and serum with smaller amounts
CC found in the stomach and kidney.
CC -!- SIMILARITY: Belongs to the transferrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00741}.
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DR EMBL; L20313; AAA18838.1; -; mRNA.
DR EMBL; L26909; AAC42221.1; -; Genomic_DNA.
DR PIR; I51350; I51350.
DR PIR; T11749; T11749.
DR RefSeq; NP_001117127.1; NM_001123655.1.
DR AlphaFoldDB; P80426; -.
DR SMR; P80426; -.
DR STRING; 8030.ENSSSAP00000074134; -.
DR MEROPS; S60.970; -.
DR GeneID; 100136560; -.
DR KEGG; sasa:100136560; -.
DR CTD; 30255; -.
DR Proteomes; UP000087266; Chromosome ssa03.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR InterPro; IPR016357; Transferrin.
DR InterPro; IPR001156; Transferrin-like_dom.
DR InterPro; IPR018195; Transferrin_Fe_BS.
DR Pfam; PF00405; Transferrin; 2.
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; 1.
DR PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Ion transport;
KW Iron; Iron transport; Metal-binding; Reference proteome; Repeat; Secreted;
KW Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 19..690
FT /note="Serotransferrin-1"
FT /id="PRO_0000035724"
FT DOMAIN 25..329
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 340..669
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 74
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 104
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 129
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 134
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
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 137
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 201
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 257
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 394
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 428
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 453
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 457
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 459
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 460
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 523
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 591
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 127..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 172..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 235..249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 343..379
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 353..370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 404..681
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 419..642
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 451..529
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 475..670
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 485..499
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 496..512
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 569..583
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT CONFLICT 34
FT /note="E -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 690 AA; 74598 MW; D1F4FC74A6AFA3FB CRC64;
MKLLLLSALL GCLATAYAAP AEGIVKWCVK SEQELRKCHD LAAKVAEFSC VRKDGSFECI
QAIKGGEADA ITLDGGDIYT AGLTNYGLQP IIAEDYGEDS DTCYYAVAVA KKGTAFGFKT
LRGKKSCHTG LGKSAGWNIP IGTLVTESQI RWAGIEDRPV ESAVSDFFNA SCAPGATMGS
KLCQLCKGDC SRSHKEPYYD YAGAFQCLKD GAGDVAFIKP LAVPAAEKAS YELLCKDGTR
ASIDSYKTCH LARVPAHAVV SRKDPELANR IYNKLVAVKD FNLFSSDGYA AKNLMFKDSA
QKLVQLPTTT DSFLYLGAEY MSTIRSLKKS QATGASSRAI KWCAVGHAEK GKCDTWTINS
FADGESKISC QDAPTVEECI KKIMRKEADA IAVDGGEVYT AGKCGLVPVM VEQYDADLCS
APGEASSYYA VAVAKKGSGL TWKTLKGKRS CHTGLGRTAG WNIPMGLIHQ ETNDCDFTKY
FSKGCAPGSE VGSPFCAQCK GSGKAVGDEY RCKARSEEQY YGYTGAFRCL VEDAGDVAFI
KHTIVPESTD GNGPDWAKDL KSSDFELLCQ DGTTQPVTKF SECHLAKVPA HAVITRPETR
GDVVSILLEL QAKFGSSGSD SSFRMFQSSV EKNLLFKDST KCLQEIPKGT KYQDFLGKEY
MIAMQSLRKC SDSTSDLEKA CTFHSCQQKE
