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Protein

Ovotransferrin

Gene
N/A
Organism
Anas platyrhynchos (Mallard) (Anas boschas)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Transferrins are iron binding transport proteins which can bind two Fe3+ 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.
Ovotransferrin has a bacteriostatic function. Its concentration in avian egg is the highest concentration of any transferrin in vivo (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ion transport, Iron transport, Transport

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ovotransferrin
OrganismiAnas platyrhynchos (Mallard) (Anas boschas)
Taxonomic identifieri8839 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeAnseriformesAnatidaeAnas
Proteomesi
  • UP000016666 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Protein family/group databases

Allergomei2104. Ana p 3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 686686OvotransferrinPRO_0000082440Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi10 ↔ 45
Disulfide bondi20 ↔ 36
Disulfide bondi115 ↔ 197
Disulfide bondi160 ↔ 174
Disulfide bondi171 ↔ 182
Disulfide bondi228 ↔ 242
Disulfide bondi348 ↔ 380
Disulfide bondi358 ↔ 371
Disulfide bondi405 ↔ 680
Disulfide bondi421 ↔ 643
Disulfide bondi454 ↔ 530
Glycosylationi473 – 4731N-linked (GlcNAc...)Sequence analysis
Disulfide bondi478 ↔ 671
Disulfide bondi488 ↔ 502
Disulfide bondi499 ↔ 513
Glycosylationi548 – 5481N-linked (GlcNAc...)Sequence analysis
Disulfide bondi570 ↔ 584

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP56410.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
686
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 138Combined sources
Helixi16 – 238Combined sources
Turni24 – 296Combined sources
Beta strandi30 – 389Combined sources
Helixi42 – 509Combined sources
Turni51 – 533Combined sources
Beta strandi56 – 594Combined sources
Helixi61 – 677Combined sources
Beta strandi75 – 817Combined sources
Beta strandi84 – 863Combined sources
Beta strandi92 – 998Combined sources
Helixi106 – 1083Combined sources
Beta strandi113 – 1175Combined sources
Turni122 – 1254Combined sources
Helixi126 – 1349Combined sources
Beta strandi136 – 1383Combined sources
Helixi143 – 1453Combined sources
Helixi148 – 1558Combined sources
Beta strandi156 – 1605Combined sources
Helixi168 – 1714Combined sources
Turni178 – 1825Combined sources
Beta strandi183 – 1864Combined sources
Helixi190 – 19910Combined sources
Beta strandi204 – 2096Combined sources
Helixi212 – 2165Combined sources
Helixi218 – 2236Combined sources
Beta strandi224 – 2274Combined sources
Turni229 – 2313Combined sources
Beta strandi233 – 2353Combined sources
Helixi236 – 2416Combined sources
Beta strandi244 – 2474Combined sources
Beta strandi251 – 2544Combined sources
Beta strandi256 – 2583Combined sources
Helixi260 – 27415Combined sources
Beta strandi275 – 2773Combined sources
Beta strandi279 – 2813Combined sources
Helixi293 – 2953Combined sources
Beta strandi296 – 3005Combined sources
Beta strandi306 – 3094Combined sources
Helixi316 – 3205Combined sources
Helixi323 – 33210Combined sources
Beta strandi344 – 3518Combined sources
Helixi352 – 36514Combined sources
Beta strandi367 – 37711Combined sources
Helixi378 – 3858Combined sources
Beta strandi391 – 3944Combined sources
Helixi396 – 4038Combined sources
Turni404 – 4063Combined sources
Beta strandi408 – 4158Combined sources
Beta strandi419 – 4246Combined sources
Beta strandi431 – 4377Combined sources
Helixi445 – 4473Combined sources
Beta strandi454 – 4563Combined sources
Turni461 – 4644Combined sources
Helixi465 – 47511Combined sources
Helixi480 – 4823Combined sources
Beta strandi484 – 4863Combined sources
Helixi497 – 4993Combined sources
Beta strandi505 – 5095Combined sources
Turni510 – 5134Combined sources
Helixi523 – 53311Combined sources
Beta strandi538 – 5414Combined sources
Helixi545 – 5473Combined sources
Beta strandi548 – 5525Combined sources
Turni557 – 5593Combined sources
Helixi563 – 5653Combined sources
Beta strandi567 – 5693Combined sources
Beta strandi575 – 5773Combined sources
Beta strandi586 – 5894Combined sources
Beta strandi593 – 5964Combined sources
Turni598 – 6003Combined sources
Helixi601 – 61515Combined sources
Turni620 – 6245Combined sources
Beta strandi631 – 6344Combined sources
Beta strandi643 – 6464Combined sources
Helixi653 – 6575Combined sources
Helixi659 – 66810Combined sources
Helixi675 – 6839Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOVX-ray4.00A1-686[»]
1DOTX-ray2.35A1-686[»]
1GV8X-ray1.95A91-249[»]
1GVCX-ray1.90A91-247[»]
1OVBX-ray2.30A91-249[»]
ProteinModelPortaliP56410.
SMRiP56410. Positions 1-686.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56410.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 333327Transferrin-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini345 – 670326Transferrin-like 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni333 – 3419Connecting region

Sequence similaritiesi

Belongs to the transferrin family.PROSITE-ProRule annotation
Contains 2 transferrin-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG000055.

Family and domain databases

InterProiIPR016357. Transferrin.
IPR001156. Transferrin-like_dom.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PfamiPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFiPIRSF002549. Transferrin. 1 hit.
PRINTSiPR00422. TRANSFERRIN.
SMARTiSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEiPS00205. TRANSFERRIN_LIKE_1. 2 hits.
PS00206. TRANSFERRIN_LIKE_2. 2 hits.
PS00207. TRANSFERRIN_LIKE_3. 1 hit.
PS51408. TRANSFERRIN_LIKE_4. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P56410-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
APPKTTVRWC TISSAEEKKC NSLKDHMQQE RVTLSCVQKA TYLDCIKAIS
60 70 80 90 100
NNEADAISLD GGQVFEAGLA PYKLKPIAAE VYERSGGSTT SYYAVAVVKK
110 120 130 140 150
GTDFMIKDLR GKTSCHTGLG RSAGWNIPIG TLIHREDIEW EGIESGISEQ
160 170 180 190 200
AVAKFFSASC VPGATIEQKL CRQCKGDAKT KCLRNGPYSG YSGAFQCLKD
210 220 230 240 250
GKGDVAFVKH TTVQENAPEE KDEYELLCLD GSRQPVDSYK TCNWARVAAH
260 270 280 290 300
AVVARDDSKI DDIWSFLGMQ AYSLGVDTTS DFHLFGPPGK KDPVLKDLLF
310 320 330 340 350
KDSAIMLKRV PELMDSQLYL GFEYYSAIQS LRKDQLTVGP RENKIQWCAV
360 370 380 390 400
GKDEKSKCDR WSVVSNGEVE CTILDDNKDC IVKITKGEAD AISLDGGFVY
410 420 430 440 450
TAGVCGLVPV VGESYEDETQ CSKDEEQPAY YFAVAVVKKS SAITWNNLQG
460 470 480 490 500
KKSCHTAVGR TAGWNIPMGL IHNKTGSCDF DDYFSEGCAP GSPPNSRLCK
510 520 530 540 550
LCQGSGENLL EKCVASSHEK YYGYTGALRC LVEQGDVAFI KHSTVGENVS
560 570 580 590 600
GSNKDDWAKG LTRDDFELLC TNGKRAKTMD YKTCHLAKVP THAVVARPEK
610 620 630 640 650
ANKIRELLEG QEKLFGLHGT EKERFMMFQS QTKDLLFKAL TKCLVKLRQG
660 670 680
ITYKEFLGDE YYASVASLNT CNPSDLLQVC TFLEDK
Length:686
Mass (Da):75,633
Last modified:July 15, 1998 - v1
Checksum:i963FCF4727C3EBDD
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOVX-ray4.00A1-686[»]
1DOTX-ray2.35A1-686[»]
1GV8X-ray1.95A91-249[»]
1GVCX-ray1.90A91-247[»]
1OVBX-ray2.30A91-249[»]
ProteinModelPortaliP56410.
SMRiP56410. Positions 1-686.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei2104. Ana p 3.

Proteomic databases

PRIDEiP56410.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG000055.

Miscellaneous databases

EvolutionaryTraceiP56410.

Family and domain databases

InterProiIPR016357. Transferrin.
IPR001156. Transferrin-like_dom.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PfamiPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFiPIRSF002549. Transferrin. 1 hit.
PRINTSiPR00422. TRANSFERRIN.
SMARTiSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEiPS00205. TRANSFERRIN_LIKE_1. 2 hits.
PS00206. TRANSFERRIN_LIKE_2. 2 hits.
PS00207. TRANSFERRIN_LIKE_3. 1 hit.
PS51408. TRANSFERRIN_LIKE_4. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Structure of diferric duck ovotransferrin at 2.35-A resolution."
    Rawas A., Muirhead H., Williams J.
    Acta Crystallogr. D 52:631-640(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
  2. "Structure of apo duck ovotransferrin: the structures of the N and C lobes are in the open form."
    Rawas A., Muirhead H., Williams J.
    Acta Crystallogr. D 53:464-468(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS).

Entry informationi

Entry nameiTRFE_ANAPL
AccessioniPrimary (citable) accession number: P56410
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: December 9, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.