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Entry version 92 (22 Apr 2020)
Sequence version 1 (01 Oct 2003)
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Protein

Venom prothrombin activator pseutarin-C non-catalytic subunit

Gene
N/A
Organism
Pseudonaja textilis (Eastern brown snake)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Snake prothrombin activator that attacks the hemostatic system of prey. This non-catalytic subunit is functionally similar to blood coagulation factor V (PubMed:12362232, PubMed:23869089). It serves as a critical cofactor for the prothrombinase activity of the catalytic subunit, which is similar to the blood coagulation factor X (PubMed:12362232, PubMed:23869089). The complex converts prothrombin to thrombin by sequential cleavage at two positions, Arg-320 followed by Arg-271 (PubMed:23869089). Cleavage at Arg-320 produces an active intermediate known as meizothrombin (PubMed:23869089). Meizothrombin is the 'second' substrate for prothrombinase, and it docks in an altered manner to present the second cleavage site (271) (PubMed:23869089). Cleavage at Arg-271 releases active thrombin from its pro-fragment (PubMed:23869089). This order of events is reversed if the protease component of prothrombinase is used on its own, suggesting that the 271 site is inherently more accessible to proteolysis (PubMed:23869089). The complex converts prothrombin to thrombin in presence but also in the absence of membrane (PubMed:23869089).2 Publications

Miscellaneous

In contrast to blood coagulation factors that circulate as inactive zymogen in plasma, venom prothrombin activators are always found in the active form in the venom. Hence, catalytic and non-catalytic subunits are found naturally in venom as stable complexes.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi124Calcium 1; via carbonyl oxygenImported1
Metal bindingi139Calcium 1; via carbonyl oxygenImported1
Metal bindingi142Calcium 1Imported1
Metal bindingi143Calcium 1Imported1
Metal bindingi920Calcium 2; via carbonyl oxygenImported1
Metal bindingi935Calcium 2; via carbonyl oxygenImported1
Metal bindingi938Calcium 2Imported1
Metal bindingi939Calcium 2Imported1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionBlood coagulation cascade activating toxin, Hemostasis impairing toxin, Prothrombin activator, Toxin
LigandCalcium, Metal-binding

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Venom prothrombin activator pseutarin-C non-catalytic subunit
Short name:
PCNS
Short name:
vPA
Alternative name(s):
Venom coagulation factor Va-like protein
Cleaved into the following 2 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiPseudonaja textilis (Eastern brown snake)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri8673 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeAcanthophiinaePseudonaja

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the use of a protein as a pharmaceutical drug. It indicates the name of the drug, the name of the firm that commercializes it and explains in a few words in which context the drug is used. In some cases, drugs that are under development are also described.<p><a href='/help/pharmaceutical_use' target='_top'>More...</a></p>Pharmaceutical usei

Is under preclinical trial by the Australian biopharmaceutical company QRxPharma Ltd, its subsidiary Venomics Pty Ltd (VPL) and the University of Queensland (UQ) under the name CoVase (V0801). Tested as a procoagulant cofactor that may have application as a systemic anti-bleeding agent in the treatment of internal bleeding and non-compressible hemorrhage.1 Publication

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 301 PublicationAdd BLAST30
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_500008928631 – 772Pseutarin-C non-catalytic subunit heavy chainCuratedAdd BLAST742
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000408521773 – 818Activation peptide (connecting region)Add BLAST46
ChainiPRO_0000408522819 – 1460Pseutarin-C non-catalytic subunit light chainAdd BLAST642

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi156N-linked (GlcNAc...) asparagine1 PublicationImported1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi170 ↔ 1961 PublicationImported
Glycosylationi204N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi242N-linked (GlcNAc...) asparagine1 PublicationImported1
Disulfide bondi251 ↔ 3321 PublicationImported
Glycosylationi406N-linked (GlcNAc...) asparagine1 PublicationImported1
Glycosylationi471N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi503 ↔ 5291 PublicationImported
Glycosylationi557N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi672 ↔ 10321 PublicationImported
Glycosylationi944N-linked (GlcNAc...) asparagine1 PublicationImported1
Disulfide bondi966 ↔ 9921 PublicationImported
Glycosylationi1001N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1147 ↔ 12981 PublicationImported
Glycosylationi1180N-linked (GlcNAc...) asparagine1 PublicationImported1
Disulfide bondi1303 ↔ 14571 PublicationImported

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

In physiological conditions, blood coagulation factor V and factor Va are inactivated by activated protein C (APC) through proteolytic degradation of the heavy chain. However, pseutarin-C non-catalytic subunit (factor V-like protein) retains its full activity even at high concentration of APC. This has two explanations: this protein has only one of the three cleavage sites present in factor V that are targeted by the APC for inactivation, and the binding with the catalytic subunit protect the cleavage site from inactivation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei385Not glycosylated1 Publication1
Sitei772 – 773Cleavage; by thrombinBy similarity2
Sitei818 – 819Cleavage; by thrombinBy similarity2
Sitei1397Not glycosylated1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q7SZN0

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q7SZN0

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed by the venom gland.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterodimer of a light and a heavy chains; non-disulfide-linked. The interaction between the two chains is calcium-dependent (By similarity).

Found in its active form associated with pseutarin-C catalytic subunit (AC Q56VR3).

By similarity1 Publication

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11460
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q7SZN0

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini32 – 330F5/8 type A 1Add BLAST299
Domaini32 – 196Plastocyanin-like 1Add BLAST165
Domaini206 – 330Plastocyanin-like 2Add BLAST125
Domaini351 – 685F5/8 type A 2Add BLAST335
Domaini351 – 529Plastocyanin-like 3Add BLAST179
Domaini539 – 685Plastocyanin-like 4Add BLAST147
Domaini824 – 1143F5/8 type A 3Add BLAST320
Domaini824 – 992Plastocyanin-like 5Add BLAST169
Domaini1001 – 1143Plastocyanin-like 6Add BLAST143
Domaini1147 – 1298F5/8 type C 1PROSITE-ProRule annotationAdd BLAST152
Domaini1303 – 1457F5/8 type C 2PROSITE-ProRule annotationAdd BLAST155

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni693 – 818BAdd BLAST126

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi695 – 699Poly-Glu5

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the multicopper oxidase family.Curated

Keywords - Domaini

Repeat, Signal

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00057, FA58C, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.120.260, 2 hits
2.60.40.420, 5 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011707, Cu-oxidase_3
IPR033138, Cu_oxidase_CS
IPR008972, Cupredoxin
IPR000421, FA58C
IPR024715, Factor_5/8-like
IPR008979, Galactose-bd-like_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07732, Cu-oxidase_3, 3 hits
PF00754, F5_F8_type_C, 2 hits

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000354, Factors_V_VIII, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00231, FA58C, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49503, SSF49503, 6 hits
SSF49785, SSF49785, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01285, FA58C_1, 2 hits
PS01286, FA58C_2, 1 hit
PS50022, FA58C_3, 2 hits
PS00079, MULTICOPPER_OXIDASE1, 3 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q7SZN0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGRYSVSPVP KCLLLMFLGW SGLKYYQVNA AQLREYHIAA QLEDWDYNPQ
60 70 80 90 100
PEELSRLSES DLTFKKIVYR EYELDFKQEE PRDALSGLLG PTLRGEVGDS
110 120 130 140 150
LIIYFKNFAT QPVSIHPQSA VYNKWSEGSS YSDGTSDVER LDDAVPPGQS
160 170 180 190 200
FKYVWNITAE IGPKKADPPC LTYAYYSHVN MVRDFNSGLI GALLICKEGS
210 220 230 240 250
LNANGSQKFF NREYVLMFSV FDESKNWYRK PSLQYTINGF ANGTLPDVQA
260 270 280 290 300
CAYDHISWHL IGMSSSPEIF SVHFNGQTLE QNHYKVSTIN LVGGASVTAD
310 320 330 340 350
MSVSRTGKWL ISSLVAKHLQ AGMYGYLNIK DCGNPDTLTR KLSFRELMKI
360 370 380 390 400
KNWEYFIAAE EITWDYAPEI PSSVDRRYKA QYLDNFSNFI GKKYKKAVFR
410 420 430 440 450
QYEDGNFTKP TYAIWPKERG ILGPVIKAKV RDTVTIVFKN LASRPYSIYV
460 470 480 490 500
HGVSVSKDAE GAIYPSDPKE NITHGKAVEP GQVYTYKWTV LDTDEPTVKD
510 520 530 540 550
SECITKLYHS AVDMTRDIAS GLIGPLLVCK HKALSVKGVQ NKADVEQHAV
560 570 580 590 600
FAVFDENKSW YLEDNIKKYC SNPSAVKKDD PKFYKSNVMY TLNGYASDRT
610 620 630 640 650
EVLRFHQSEV VQWHLTSVGT VDEIVPVHLS GHTFLSKGKH QDILNLFPMS
660 670 680 690 700
GESATVTMDN LGTWLLSSWG SCEMSNGMRL RFLDANYDDE DEGNEEEEED
710 720 730 740 750
DGDIFADIFI PSEVVKKKEE VPVNFVPDPE SDALAKELGL IDDEGNPIIQ
760 770 780 790 800
PRREQTEDDE EQLMKASMLG LRSFKGSVAE EELKHTALAL EEDAHASDPR
810 820 830 840 850
IDSNSARNPD DIAGRYLRTI NRGNKRRYYI AAEEVLWDYS PIGKSQVRSR
860 870 880 890 900
AAKTTFKKAI FRSYLDDTFQ TPSTGGEYEK HLGILGPIIR AEVDDVIEIQ
910 920 930 940 950
FKNLASRPYS LHAHGLLYEK SSEGRSYDDK SPELFKKDDA IMPNGTYTYV
960 970 980 990 1000
WQVPPRSGPT DNTEKCKSWA YYSGVNPEKD IHSGLIGPIL ICQKGMIDKY
1010 1020 1030 1040 1050
NRTIDIREFV LFFMVFDEEK SWYFPKSDKS TCEEKLIGVQ SLHTFPAING
1060 1070 1080 1090 1100
IPYQLQGLTM YKDENVHWHL LNMGGPKDIH VVNFHGQTFT EEGREDNQLG
1110 1120 1130 1140 1150
VLPLLPGTFA SIKMKPSKIG TWLLETEVGE NQERGMQALF TVIDKDCKLP
1160 1170 1180 1190 1200
MGLASGIIQD SQISASGHVG YWEPKLARLN NTGKYNAWSI IKKEHEHPWI
1210 1220 1230 1240 1250
QIDLQRQVVI TGIQTQGTVQ LLQHSYTVEY FVTYSEDGQN WITFKGRHSE
1260 1270 1280 1290 1300
TQMHFEGNSD GTTVKENHID PPIIARYIRL HPTKFYNRPT FRIELLGCEV
1310 1320 1330 1340 1350
EGCSVPLGME SGAIKNSEIT ASSYKKTWWS SWEPSLARLN LEGGTNAWQP
1360 1370 1380 1390 1400
EVNNKDQWLQ IDLQHLTKIT SIITQGATSM TTSMYVKTFS IHYTDDNSTW
1410 1420 1430 1440 1450
KPYLDVRTSM EKVFTGNINS DGHVKHFFKP PILSRFIRII PKTWNQYIAL
1460
RIELFGCEVF
Length:1,460
Mass (Da):165,932
Last modified:October 1, 2003 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6AFB63E2D5D275A6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti80 – 82EPR → KPQ AA sequence (PubMed:12730119).Curated3
Sequence conflicti103I → Q AA sequence (PubMed:12730119).Curated1
Sequence conflicti119 – 124SAVYNK → DAVKIG AA sequence (PubMed:12730119).Curated6
Sequence conflicti146P → A AA sequence (PubMed:12730119).Curated1
Sequence conflicti156N → E AA sequence (PubMed:12730119).Curated1
Sequence conflicti350 – 363IKNWE…AEEIT → AQLWEYHIAAQKED AA sequence (PubMed:12730119).CuratedAdd BLAST14
Sequence conflicti440 – 444NLASR → DLAVQ AA sequence (PubMed:12730119).Curated5
Sequence conflicti522 – 523LI → IL AA sequence (PubMed:12730119).Curated2
Sequence conflicti820 – 827INRGNKRR → QNTGNKLY AA sequence (PubMed:12730119).Curated8
Sequence conflicti840S → I AA sequence (PubMed:12730119).Curated1
Sequence conflicti876G → GK AA sequence (PubMed:12730119).Curated1
Sequence conflicti902K → R AA sequence (PubMed:12730119).Curated1
Sequence conflicti944N → F AA sequence (PubMed:12730119).Curated1
Sequence conflicti981 – 995IHSGL…ICQKG → VEPGLIGPLYSIAEEAV AA sequence (PubMed:12730119).CuratedAdd BLAST15
Sequence conflicti1041 – 1043SLH → NLG AA sequence (PubMed:12730119).Curated3
Sequence conflicti1055 – 1058LQGL → GK AA sequence (PubMed:12730119).Curated4
Sequence conflicti1166 – 1170SGHVG → AGHVQ AA sequence (PubMed:12730119).Curated5
Sequence conflicti1274I → V AA sequence (PubMed:12730119).Curated1
Sequence conflicti1369I → K AA sequence (PubMed:12730119).Curated1
Sequence conflicti1400 – 1404WKPYL → YKPYG AA sequence (PubMed:12730119).Curated5
Sequence conflicti1433 – 1434LS → SL AA sequence (PubMed:12730119).Curated2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AY168281 mRNA Translation: AAO38805.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY168281 mRNA Translation: AAO38805.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4BXSX-ray3.32V31-1460[»]
SMRiQ7SZN0
ModBaseiSearch...
PDBe-KBiSearch...

PTM databases

iPTMnetiQ7SZN0

Proteomic databases

PRIDEiQ7SZN0

Family and domain databases

CDDicd00057, FA58C, 2 hits
Gene3Di2.60.120.260, 2 hits
2.60.40.420, 5 hits
InterProiView protein in InterPro
IPR011707, Cu-oxidase_3
IPR033138, Cu_oxidase_CS
IPR008972, Cupredoxin
IPR000421, FA58C
IPR024715, Factor_5/8-like
IPR008979, Galactose-bd-like_sf
PfamiView protein in Pfam
PF07732, Cu-oxidase_3, 3 hits
PF00754, F5_F8_type_C, 2 hits
PIRSFiPIRSF000354, Factors_V_VIII, 1 hit
SMARTiView protein in SMART
SM00231, FA58C, 2 hits
SUPFAMiSSF49503, SSF49503, 6 hits
SSF49785, SSF49785, 2 hits
PROSITEiView protein in PROSITE
PS01285, FA58C_1, 2 hits
PS01286, FA58C_2, 1 hit
PS50022, FA58C_3, 2 hits
PS00079, MULTICOPPER_OXIDASE1, 3 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFA5V_PSETE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q7SZN0
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: October 1, 2003
Last modified: April 22, 2020
This is version 92 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Pharmaceutical

Documents

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