TRF_SARPE
ID TRF_SARPE Reviewed; 629 AA.
AC Q26643;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Transferrin;
DE Flags: Precursor;
OS Sarcophaga peregrina (Flesh fly) (Boettcherisca peregrina).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Sarcophagidae; Sarcophaga; Boettcherisca.
OX NCBI_TaxID=7386;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 22-35; 71-85; 203-213;
RP 231-244; 327-340; 391-394; 418-429 AND 480-497.
RC TISSUE=Hemolymph;
RX PubMed=7705333; DOI=10.1111/j.1432-1033.1995.tb20254.x;
RA Kurama T., Kurata S., Natori S.;
RT "Molecular characterization of an insect transferrin and its selective
RT incorporation into eggs during oogenesis.";
RL Eur. J. Biochem. 228:229-235(1995).
CC -!- FUNCTION: Transferrins are iron binding transport proteins which bind
CC Fe(3+) ion in association with the binding of an anion, usually
CC bicarbonate. This transferrin binds only one Fe(3+) ion per protein
CC molecule. Transports iron ions from the hemolymph into the eggs during
CC the vitellogenic stage (oogenesis).
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Not expressed in embryos. Maternal transferrin is
CC used throughout embryogenesis.
CC -!- SIMILARITY: Belongs to the transferrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00741}.
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DR EMBL; D28940; BAA06067.1; -; mRNA.
DR PIR; S68986; S68986.
DR AlphaFoldDB; Q26643; -.
DR SMR; Q26643; -.
DR PRIDE; Q26643; -.
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; 3.
DR PIRSF; PIRSF002549; Transferrin; 1.
DR PRINTS; PR00422; TRANSFERRIN.
DR SMART; SM00094; TR_FER; 1.
DR PROSITE; PS00206; TRANSFERRIN_LIKE_2; 1.
DR PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Ion transport; Iron;
KW Iron transport; Metal-binding; Repeat; Signal; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:7705333"
FT CHAIN 22..629
FT /note="Transferrin"
FT /id="PRO_0000035748"
FT DOMAIN 26..366
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 372..621
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 111
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 137
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 141
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 143
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 144
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 225
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 408
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 561
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 29..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 38..54
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 135..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 184..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 207..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 270..283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 375..409
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 385..403
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
SQ SEQUENCE 629 AA; 71149 MW; 66A95170A7ECC243 CRC64;
MTIKNVLKLA ALLGVLALVQ AEEQTYRMCV PQKYYEDCLN LLKDPSEAGI RMECVAGRDR
IDCLDKINQR KADVLASEPE DMYVAYHTKN SDYKVISEIR TQEDKDAAFR YEGIILVKKN
SNIHSLKELR GAKSCHTGFG RNVGFKIPVT KLKNAHILKV SMDPELTATE RELKALSEFF
SESCLVGTYS PYPETDRLLK KKYPNLCALC EKPEQCNYPD KFSGYDGAIR CLDKGKGEVA
FTKVQFIKKY FGMVPGVTAE GDPSEFEYLC EDGSRRPLNG PACSWAQRPW TGYISNVDAV
SGDEKLHNLQ HRLEKFFENG LHAENKEAAS HLLINPNAVY HSKPQAVDPK EYLEKAGYKD
VIERDGSAIR KMKMCVQTDV EMQKCDTMRR AAYSREIRPE IECVQEKDCI LAVKDNKADM
VAVPAQNYKE ARDGKLKPIV YESYGPNNVY VAVVDSALTK ENLQSMPIHY NGQDHRAEKA
AAYLNKLRGI NTCQTTPSSE KNIMIVNAQQ LEQYKNKQLL CSSLDKKPVT EWQSCNLEAN
LPVGVFIRET MTPVEQETMK HLFVSLSDKF GSKGKLPDVF TLFGQYKDNV HNVLFADDAV
EFVTELKNPN TNEQTYNGLK CDTNTIKKN
