TRFE2_SALSA
ID TRFE2_SALSA Reviewed; 691 AA.
AC P80429;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Serotransferrin-2;
DE AltName: Full=Serotransferrin II;
DE Short=STF II;
DE Short=sTF2;
DE AltName: Full=Siderophilin II;
DE Flags: Precursor;
GN Name=tf2;
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 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 AlphaFoldDB; P80429; -.
DR SMR; P80429; -.
DR MEROPS; S60.970; -.
DR Proteomes; UP000087266; Genome assembly.
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.2"
FT CHAIN 19..691
FT /note="Serotransferrin-2"
FT /id="PRO_0000035725"
FT DOMAIN 25..329
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 340..670
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 524
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 592
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..682
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 419..643
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 451..530
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 475..671
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 485..499
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 496..513
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 570..584
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
SQ SEQUENCE 691 AA; 74664 MW; 8D2431663677CF2D 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 GSGKARGGDE DRCKARSEEQ YYGYTGAFRC LVEDAGDVAF
IKHTIVPEST DGNGPDWAKD LKSSDFELLC QDGTTQPVTK FSECHLAKVP AHAVITRPET
RGDVVSILLE LQAKFGSSGS DSSFRMFQSS VEKNLLFKDS TKCLQEIPKG TKYQDFLGKE
YMIAMQSLRK CSDSTSDLEK ACTFHSCQQK E
