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Entry version 71 (18 Sep 2019)
Sequence version 1 (26 Apr 2005)
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Protein

Venom prothrombin activator omicarin-C non-catalytic subunit

Gene
N/A
Organism
Oxyuranus microlepidotus (Inland taipan) (Diemenia microlepidota)
Status
Reviewed-Annotation score:

Annotation score:4 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 transcript 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. It serves as a critical cofactor for the prothrombinase activity of the catalytic subunit, which is similar to the blood coagulation factor X. The complex converts prothrombin to thrombin by sequential cleavage at two positions, Arg-320 followed by Arg-271. Cleavage at Arg-320 produces an active intermediate known as meizothrombin. Meizothrombin is the 'second' substrate for prothrombinase, and it docks in an altered manner to present the second cleavage site (271). Cleavage at Arg-271 releases active thrombin from its pro-fragment. 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.By similarity

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_section">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 oxygenBy similarity1
Metal bindingi139Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi142Calcium 1By similarity1
Metal bindingi143Calcium 1By similarity1
Metal bindingi919Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi934Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi937Calcium 2By similarity1
Metal bindingi938Calcium 2By similarity1

<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_and_taxonomy_section">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 omicarin-C non-catalytic subunit
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_and_taxonomy_section">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>OrganismiOxyuranus microlepidotus (Inland taipan) (Diemenia microlepidota)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri111177 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeAcanthophiinaeOxyuranus

<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 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 – 30By similarityAdd BLAST30
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000040990431 – 771Omicarin-C non-catalytic subunit heavy chainAdd BLAST741
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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_0000409905772 – 817Activation peptide (connecting region)By similarityAdd BLAST46
ChainiPRO_0000409906818 – 1460Omicarin-C non-catalytic subunit light chainAdd BLAST643

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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...) asparaginePROSITE-ProRule annotation1
<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 ↔ 196By similarity
Glycosylationi242N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi251 ↔ 332By similarity
Glycosylationi300N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi385N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi406N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi471N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi503 ↔ 529By similarity
Glycosylationi557N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi672 ↔ 1031By similarity
Glycosylationi943N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi965 ↔ 991By similarity
Glycosylationi1000N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi1147 ↔ 1298By similarity
Glycosylationi1180N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi1303 ↔ 1457By similarity
Glycosylationi1397N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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, omicarin-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 (By similarity).By similarity

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>Sitei771 – 772Cleavage; by thrombinBy similarity2
Sitei817 – 818Cleavage; by thrombinBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q58L90

<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.

<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_section">'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_section">'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.

Found in its active form associated with omicarin-C catalytic subunit (AC Q58L95) (By similarity).

By similarity

<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

3D structure databases

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

More...
SMRi
Q58L90

Database of comparative protein structure models

More...
ModBasei
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_and_domains_section">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
Domaini350 – 685F5/8 type A 2Add BLAST336
Domaini351 – 529Plastocyanin-like 3Add BLAST179
Domaini539 – 685Plastocyanin-like 4Add BLAST147
Domaini823 – 1143F5/8 type A 3Add BLAST321
Domaini823 – 991Plastocyanin-like 5Add BLAST169
Domaini1000 – 1143Plastocyanin-like 6Add BLAST144
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 – 817BAdd BLAST125

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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

Q58L90-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGRYSVSPVP KCLLLMFLGW SGLKYYQVNA AQLREYRIAA QLEDWDYNPQ
60 70 80 90 100
PEELSRLSES ELTFKKIVYR EYELDFKQEK PRDELSGLLG PTLRGEVGDI
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
LNANGAQKFF NREYVLMFSV FDESKNWYRK PSLQYTINGF ANGTLPDVQA
260 270 280 290 300
CAYDHISWHL IGMSSSPEIF SVHFNGQTLE QNHYKVSTIN LVGGASVTAN
310 320 330 340 350
MSVSRTGKWL ISSLVAKHLQ AGMYGYLNIK DCGHPNTLTR KLSFRELRRI
360 370 380 390 400
MNWEYFIAAE 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 LKALSVKGVQ NKADVEQHAV
560 570 580 590 600
FAVFDENKSW YLEDNIKKYC SNPSSVKKDD PKFYKSNVMY TLNGYASDRT
610 620 630 640 650
EVLGFHQSEV VQWHLTSVGT VDEIVPVHLS GHTFLSKGKH QDILNLFPMS
660 670 680 690 700
GESATVTMDN LGTWLLSSWG SCEMSNGMRL RFLDANYDDE DEGNEEEEED
710 720 730 740 750
DGDIFADIFS PPEVVKKKEE VPVNFVPDPE SDALAKELGL LDDEDNPEQS
760 770 780 790 800
RSEQTEDDEE QLMIASVLGL RSFKGSVAEE ELKHTALALE EDAHASDPRI
810 820 830 840 850
DSNSARNSDD IAGRYLRTIN RRNKRRYYIA AEEVLWDYSP IGKSQVRSLP
860 870 880 890 900
AKTTFKKAIF RSYLDDTFQT PSTGGEYEKH LGILGPIIRA EVDDVIEVQF
910 920 930 940 950
RNLASRPYSL HAHGLLYEKS SEGRSYDDNS PELFKKDDAI MPNGTYTYVW
960 970 980 990 1000
QVPPRSGPTD NTEKCKSWAY YSGVNPEKDI HSGLIGPILI CQKGMIDKYN
1010 1020 1030 1040 1050
RTIDIREFVL FFMVFDEEKS WYFPKSDKST CEEKLIGVQS SHHTFPAING
1060 1070 1080 1090 1100
IPYQLQGLMM YKDENVHWHL LNMGGPKDIH VVNFHGQTFT EEGREDNQLG
1110 1120 1130 1140 1150
VLPLLPGTFA SIKMKPSKIG TWLLETEVGE NQERGMQALF TVIDKDCKLP
1160 1170 1180 1190 1200
MGLASGIIQD SQISASGHVE YWEPKLARLN NTGMFNAWSI IKKEHEHPWI
1210 1220 1230 1240 1250
QIDLQRQVVI TGIQTQGTVQ LLKHSYTVEY FVTYSKDGQN WITFKGRHSE
1260 1270 1280 1290 1300
TQMHFEGNSD GTTVKENHID PPIIARYIRL HPTKFYNTPT FRIELLGCEV
1310 1320 1330 1340 1350
EGCSVPLGME SGAIKNSEIT ASSYKKTWWS SWEPFLARLN LEGGTNAWQP
1360 1370 1380 1390 1400
EVNNKDQWLQ IDLQHLTKIT SIITQGATSM TTAMYVKTFS IHYTDDNSTW
1410 1420 1430 1440 1450
KPYLDVRTSM EKVFTGNINS DGHVKHFFKP PILSRFIRII PKTWNQYIAL
1460
RIELFGCEVF
Length:1,460
Mass (Da):166,082
Last modified:April 26, 2005 - 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:iF7BCEC4838695087
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AY940210 mRNA Translation: AAX37266.1

<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
AY940210 mRNA Translation: AAX37266.1

3D structure databases

SMRiQ58L90
ModBaseiSearch...

Proteomic databases

PRIDEiQ58L90

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

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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_OXYMI
<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: Q58L90
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: April 26, 2005
Last modified: September 18, 2019
This is version 71 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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