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Protein

Ectonucleotide pyrophosphatase/phosphodiesterase family member 2

Gene

Enpp2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes lysophospholipids to produce lysophosphatidic acid (LPA) in extracellular fluids. Major substrate is lysophosphatidylcholine. Also can act on sphingosylphosphphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility. Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP. Involved in several motility-related processes such as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by stimulating migration of smooth muscle cells and microtubule formation. Stimulates migration of melanoma cells, probably via a pertussis toxin-sensitive G protein. May have a role in induction of parturition. Possible involvement in cell proliferation and adipose tissue development. Tumor cell motility-stimulating factor.2 Publications

Catalytic activityi

1-alkyl-sn-glycero-3-phosphoethanolamine + H2O = 1-alkyl-sn-glycerol 3-phosphate + ethanolamine.1 Publication

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Inhibited by lysophosphatidic acid (LPA) and sphingosine-1-phosphate (S1P). Inhibited by EDTA and EGTA (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi171Zinc 1; catalytic1
Active sitei209NucleophileBy similarity1
Metal bindingi209Zinc 1; catalytic1
Binding sitei230SubstrateBy similarity1
Binding sitei306SubstrateBy similarity1
Metal bindingi311Zinc 2; catalytic1
Metal bindingi315Zinc 2; catalytic1
Metal bindingi315Zinc 2; via tele nitrogen; catalyticBy similarity1
Metal bindingi358Zinc 1; catalytic1
Metal bindingi359Zinc 1; catalytic1
Metal bindingi359Zinc 1; via tele nitrogen; catalyticBy similarity1
Metal bindingi474Zinc 2; catalytic1
Metal bindingi474Zinc 2; via tele nitrogen; catalyticBy similarity1
Metal bindingi764Calcium1
Metal bindingi766Calcium1
Metal bindingi768Calcium1
Metal bindingi770Calcium; via carbonyl oxygen1
Metal bindingi772Calcium1
Sitei877Essential for catalytic activityBy similarity1

GO - Molecular functioni

  • alkylglycerophosphoethanolamine phosphodiesterase activity Source: RGD
  • calcium ion binding Source: UniProtKB
  • lysophospholipase activity Source: UniProtKB
  • nucleic acid binding Source: InterPro
  • nucleotide diphosphatase activity Source: InterPro
  • phosphodiesterase I activity Source: RGD
  • polysaccharide binding Source: InterPro
  • scavenger receptor activity Source: InterPro
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • cell chemotaxis Source: RGD
  • cellular response to cadmium ion Source: RGD
  • cellular response to estradiol stimulus Source: RGD
  • estrous cycle Source: RGD
  • immune response Source: InterPro
  • negative regulation of cell-matrix adhesion Source: RGD
  • phosphatidylcholine catabolic process Source: UniProtKB
  • positive regulation of cell proliferation Source: RGD
  • positive regulation of focal adhesion assembly Source: RGD
  • positive regulation of oligodendrocyte differentiation Source: RGD
  • positive regulation of substrate adhesion-dependent cell spreading Source: RGD
  • regulation of angiogenesis Source: InterPro
  • regulation of cell migration Source: InterPro
  • response to polycyclic arene Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Chemotaxis, Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.1.4.39. 5301.
SABIO-RKQ64610.

Chemistry databases

SwissLipidsiSLP:000000394.

Names & Taxonomyi

Protein namesi
Recommended name:
Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 (EC:3.1.4.39)
Short name:
E-NPP 2
Alternative name(s):
Autotaxin
Extracellular lysophospholipase D
Short name:
LysoPLD
Gene namesi
Name:Enpp2
Synonyms:Atx, Npps2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi69298. Enpp2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • extracellular space Source: UniProtKB
  • Golgi apparatus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi13I → L: No effect on secretion. 1 Publication1
Mutagenesisi16 – 18FTF → VLS: No effect on secretion. 1 Publication3
Mutagenesisi18 – 21FAIS → SVCV: No effect on secretion. 1 Publication4
Mutagenesisi21 – 24SVNI → VLTT: No effect on secretion. 1 Publication4
Mutagenesisi24 – 25IC → TI: No effect on secretion. 1 Publication2
Mutagenesisi28 – 30FTA → CIF: No effect on secretion. 1 Publication3
Mutagenesisi171D → N: Abolishes lysophospholipase D activity. 1 Publication1
Mutagenesisi209T → A: Abolishes lysophospholipase D activity. 1 Publication1
Mutagenesisi209T → S: 15% of wild-type lysophospholipase D activity. 1 Publication1
Mutagenesisi311D → N: Abolishes lysophospholipase D activity. 1 Publication1
Mutagenesisi315H → Q: 20% of wild-type lysophospholipase D activity. 1 Publication1
Mutagenesisi430K → A: Impaired secretion. No effect on lysophospholipase activity. 1 Publication1
Mutagenesisi764 – 768DYNYD → SYAYS: Abolishes secretion. Strongly reduced lysophospholipase activity. 1 Publication5

Keywords - Diseasei

Obesity

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 272 PublicationsAdd BLAST27
PropeptideiPRO_000028165128 – 35Removed by furin2 Publications8
ChainiPRO_000018856936 – 887Ectonucleotide pyrophosphatase/phosphodiesterase family member 2Add BLAST852

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi53N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi58 ↔ 75PROSITE-ProRule annotation1 Publication
Disulfide bondi62 ↔ 93PROSITE-ProRule annotation1 Publication
Disulfide bondi73 ↔ 86PROSITE-ProRule annotation1 Publication
Disulfide bondi79 ↔ 85PROSITE-ProRule annotation1 Publication
Disulfide bondi102 ↔ 119PROSITE-ProRule annotation1 Publication
Disulfide bondi107 ↔ 137PROSITE-ProRule annotation1 Publication
Disulfide bondi117 ↔ 130PROSITE-ProRule annotation1 Publication
Disulfide bondi123 ↔ 129PROSITE-ProRule annotation1 Publication
Disulfide bondi148 ↔ 194PROSITE-ProRule annotation1 Publication
Disulfide bondi156 ↔ 350PROSITE-ProRule annotation1 Publication
Disulfide bondi366 ↔ 468PROSITE-ProRule annotation1 Publication
Glycosylationi398N-linked (GlcNAc...)Sequence analysis1
Glycosylationi410N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi413 ↔ 830PROSITE-ProRule annotation1 Publication
Glycosylationi524N-linked (GlcNAc...)1 Publication1
Disulfide bondi566 ↔ 691PROSITE-ProRule annotation1 Publication
Disulfide bondi568 ↔ 676PROSITE-ProRule annotation1 Publication
Glycosylationi610N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi799 ↔ 809PROSITE-ProRule annotation1 Publication
Glycosylationi831N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

N-glycosylation, but not furin-cleavage, plays a critical role on secretion and on lysoPLD activity.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ64610.

Expressioni

Tissue specificityi

Abundantly expressed in cerebrum and cerebellum. Localized in secretory epithelial cells in the brain and the eye including choroid plexus epithelial cells, ciliary epithelial cells, iris pigment epithelial cells, and retinal pigment cells.2 Publications

Interactioni

Protein-protein interaction databases

MINTiMINT-4997409.

Structurei

Secondary structure

1887
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni59 – 63Combined sources5
Beta strandi70 – 72Combined sources3
Turni77 – 83Combined sources7
Helixi89 – 92Combined sources4
Turni98 – 100Combined sources3
Helixi104 – 106Combined sources3
Beta strandi107 – 109Combined sources3
Beta strandi115 – 118Combined sources4
Helixi123 – 126Combined sources4
Helixi133 – 137Combined sources5
Helixi143 – 145Combined sources3
Beta strandi165 – 171Combined sources7
Helixi175 – 180Combined sources6
Turni182 – 184Combined sources3
Helixi186 – 194Combined sources9
Beta strandi195 – 197Combined sources3
Helixi209 – 218Combined sources10
Helixi222 – 225Combined sources4
Beta strandi230 – 234Combined sources5
Turni235 – 238Combined sources4
Beta strandi239 – 241Combined sources3
Beta strandi243 – 246Combined sources4
Helixi247 – 249Combined sources3
Helixi251 – 253Combined sources3
Helixi259 – 265Combined sources7
Helixi281 – 292Combined sources12
Turni296 – 298Combined sources3
Beta strandi301 – 310Combined sources10
Helixi311 – 317Combined sources7
Helixi322 – 324Combined sources3
Helixi325 – 344Combined sources20
Turni348 – 350Combined sources3
Beta strandi352 – 358Combined sources7
Beta strandi368 – 371Combined sources4
Helixi372 – 374Combined sources3
Helixi379 – 381Combined sources3
Beta strandi382 – 385Combined sources4
Beta strandi387 – 395Combined sources9
Beta strandi396 – 398Combined sources3
Helixi404 – 410Combined sources7
Beta strandi419 – 424Combined sources6
Helixi425 – 427Combined sources3
Helixi430 – 432Combined sources3
Beta strandi442 – 447Combined sources6
Beta strandi452 – 456Combined sources5
Helixi457 – 459Combined sources3
Beta strandi471 – 473Combined sources3
Helixi481 – 483Combined sources3
Beta strandi487 – 494Combined sources8
Beta strandi496 – 499Combined sources4
Helixi505 – 507Combined sources3
Helixi508 – 515Combined sources8
Turni527 – 530Combined sources4
Helixi531 – 533Combined sources3
Beta strandi534 – 536Combined sources3
Helixi559 – 561Combined sources3
Helixi577 – 581Combined sources5
Turni583 – 586Combined sources4
Helixi587 – 591Combined sources5
Helixi617 – 620Combined sources4
Beta strandi634 – 638Combined sources5
Beta strandi643 – 647Combined sources5
Turni648 – 651Combined sources4
Beta strandi652 – 660Combined sources9
Helixi671 – 673Combined sources3
Helixi685 – 687Combined sources3
Helixi691 – 696Combined sources6
Beta strandi701 – 706Combined sources6
Helixi708 – 710Combined sources3
Helixi714 – 717Combined sources4
Helixi718 – 721Combined sources4
Helixi723 – 725Combined sources3
Beta strandi726 – 729Combined sources4
Helixi731 – 742Combined sources12
Helixi744 – 752Combined sources9
Beta strandi754 – 762Combined sources9
Beta strandi768 – 770Combined sources3
Helixi774 – 776Combined sources3
Beta strandi790 – 801Combined sources12
Helixi806 – 808Combined sources3
Beta strandi813 – 821Combined sources9
Turni830 – 833Combined sources4
Helixi836 – 838Combined sources3
Helixi840 – 846Combined sources7
Helixi851 – 858Combined sources8
Helixi870 – 878Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XR9X-ray2.05A36-887[»]
2XRGX-ray3.20A1-887[»]
5DLTX-ray1.60A36-887[»]
5DLVX-ray2.00A/B36-887[»]
5DLWX-ray1.80A36-887[»]
5IJQX-ray2.05A36-887[»]
5IJSX-ray2.20A36-887[»]
5L0BX-ray2.41A/B1-887[»]
5L0EX-ray3.06A/B1-887[»]
5L0KX-ray2.73A/B51-884[»]
ProteinModelPortaliQ64610.
SMRiQ64610.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ64610.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini54 – 97SMB 1PROSITE-ProRule annotationAdd BLAST44
Domaini98 – 142SMB 2PROSITE-ProRule annotationAdd BLAST45

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni210 – 213Substrate bindingBy similarity4
Regioni243 – 254Substrate bindingBy similarityAdd BLAST12
Regioni854 – 875Required for secretionBy similarityAdd BLAST22

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi126 – 128Cell attachment siteSequence analysis3

Sequence similaritiesi

Contains 2 SMB (somatomedin-B) domains.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

HOGENOMiHOG000037439.
HOVERGENiHBG051484.
InParanoidiQ64610.
KOiK01122.
PhylomeDBiQ64610.

Family and domain databases

Gene3Di3.40.570.10. 1 hit.
3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR001604. DNA/RNA_non-sp_Endonuclease.
IPR024873. E-NPP.
IPR029881. ENPP2.
IPR020821. Extracellular_endonuc_su_A.
IPR002591. Phosphodiest/P_Trfase.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PANTHERiPTHR10151. PTHR10151. 2 hits.
PTHR10151:SF21. PTHR10151:SF21. 2 hits.
PfamiPF01223. Endonuclease_NS. 1 hit.
PF01663. Phosphodiest. 1 hit.
PF01033. Somatomedin_B. 2 hits.
[Graphical view]
PRINTSiPR00022. SOMATOMEDINB.
SMARTiSM00892. Endonuclease_NS. 1 hit.
SM00477. NUC. 1 hit.
SM00201. SO. 2 hits.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
SSF90188. SSF90188. 2 hits.
PROSITEiPS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q64610-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MARQGCLGSF QVISLFTFAI SVNICLGFTA SRIKRAEWDE GPPTVLSDSP
60 70 80 90 100
WTNTSGSCKG RCFELQEVGP PDCRCDNLCK SYSSCCHDFD ELCLKTARGW
110 120 130 140 150
ECTKDRCGEV RNEENACHCS EDCLSRGDCC TNYQVVCKGE SHWVDDDCEE
160 170 180 190 200
IKVPECPAGF VRPPLIIFSV DGFRASYMKK GSKVMPNIEK LRSCGTHAPY
210 220 230 240 250
MRPVYPTKTF PNLYTLATGL YPESHGIVGN SMYDPVFDAS FHLRGREKFN
260 270 280 290 300
HRWWGGQPLW ITATKQGVRA GTFFWSVSIP HERRILTILQ WLSLPDNERP
310 320 330 340 350
SVYAFYSEQP DFSGHKYGPF GPEMTNPLRE IDKTVGQLMD GLKQLRLHRC
360 370 380 390 400
VNVIFVGDHG MEDVTCDRTE FLSNYLTNVD DITLVPGTLG RIRAKSINNS
410 420 430 440 450
KYDPKTIIAN LTCKKPDQHF KPYMKQHLPK RLHYANNRRI EDIHLLVDRR
460 470 480 490 500
WHVARKPLDV YKKPSGKCFF QGDHGFDNKV NSMQTVFVGY GPTFKYRTKV
510 520 530 540 550
PPFENIELYN VMCDLLGLKP APNNGTHGSL NHLLRTNTFR PTMPDEVSRP
560 570 580 590 600
NYPGIMYLQS EFDLGCTCDD KVEPKNKLEE LNKRLHTKGS TEAETGKFRG
610 620 630 640 650
SKHENKKNLN GSVEPRKERH LLYGRPAVLY RTSYDILYHT DFESGYSEIF
660 670 680 690 700
LMPLWTSYTI SKQAEVSSIP EHLTNCVRPD VRVSPGFSQN CLAYKNDKQM
710 720 730 740 750
SYGFLFPPYL SSSPEAKYDA FLVTNMVPMY PAFKRVWAYF QRVLVKKYAS
760 770 780 790 800
ERNGVNVISG PIFDYNYDGL RDTEDEIKQY VEGSSIPVPT HYYSIITSCL
810 820 830 840 850
DFTQPADKCD GPLSVSSFIL PHRPDNDESC NSSEDESKWV EELMKMHTAR
860 870 880
VRDIEHLTGL DFYRKTSRSY SEILTLKTYL HTYESEI
Length:887
Mass (Da):101,576
Last modified:March 20, 2007 - v2
Checksum:i40AD1C957F833869
GO
Isoform 2 (identifier: Q64610-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     591-615: Missing.

Note: No experimental confirmation available.
Show »
Length:862
Mass (Da):98,836
Checksum:i2A530389DBA57952
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti97A → V in BAA05910 (PubMed:7961762).Curated1
Sequence conflicti107C → S in BAA05910 (PubMed:7961762).Curated1
Sequence conflicti120S → P in BAA05910 (PubMed:7961762).Curated1
Sequence conflicti147 – 162DCEEI…AGFVR → AARNQSSECLQVCP in BAA05910 (PubMed:7961762).CuratedAdd BLAST16
Sequence conflicti198A → V in BAA05910 (PubMed:7961762).Curated1
Sequence conflicti201M → T in BAA05910 (PubMed:7961762).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_024018591 – 615Missing in isoform 2. 1 PublicationAdd BLAST25

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28560 mRNA. Translation: BAA05910.1.
DQ131564 mRNA. Translation: AAZ99725.1.
BC081747 mRNA. Translation: AAH81747.1.
PIRiA55453.
RefSeqiNP_476445.2. NM_057104.2.
UniGeneiRn.20403.

Genome annotation databases

GeneIDi84050.
KEGGirno:84050.
UCSCiRGD:69298. rat. [Q64610-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28560 mRNA. Translation: BAA05910.1.
DQ131564 mRNA. Translation: AAZ99725.1.
BC081747 mRNA. Translation: AAH81747.1.
PIRiA55453.
RefSeqiNP_476445.2. NM_057104.2.
UniGeneiRn.20403.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XR9X-ray2.05A36-887[»]
2XRGX-ray3.20A1-887[»]
5DLTX-ray1.60A36-887[»]
5DLVX-ray2.00A/B36-887[»]
5DLWX-ray1.80A36-887[»]
5IJQX-ray2.05A36-887[»]
5IJSX-ray2.20A36-887[»]
5L0BX-ray2.41A/B1-887[»]
5L0EX-ray3.06A/B1-887[»]
5L0KX-ray2.73A/B51-884[»]
ProteinModelPortaliQ64610.
SMRiQ64610.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4997409.

Chemistry databases

SwissLipidsiSLP:000000394.

Proteomic databases

PRIDEiQ64610.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi84050.
KEGGirno:84050.
UCSCiRGD:69298. rat. [Q64610-1]

Organism-specific databases

CTDi5168.
RGDi69298. Enpp2.

Phylogenomic databases

HOGENOMiHOG000037439.
HOVERGENiHBG051484.
InParanoidiQ64610.
KOiK01122.
PhylomeDBiQ64610.

Enzyme and pathway databases

BRENDAi3.1.4.39. 5301.
SABIO-RKQ64610.

Miscellaneous databases

EvolutionaryTraceiQ64610.
PROiQ64610.

Family and domain databases

Gene3Di3.40.570.10. 1 hit.
3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR001604. DNA/RNA_non-sp_Endonuclease.
IPR024873. E-NPP.
IPR029881. ENPP2.
IPR020821. Extracellular_endonuc_su_A.
IPR002591. Phosphodiest/P_Trfase.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PANTHERiPTHR10151. PTHR10151. 2 hits.
PTHR10151:SF21. PTHR10151:SF21. 2 hits.
PfamiPF01223. Endonuclease_NS. 1 hit.
PF01663. Phosphodiest. 1 hit.
PF01033. Somatomedin_B. 2 hits.
[Graphical view]
PRINTSiPR00022. SOMATOMEDINB.
SMARTiSM00892. Endonuclease_NS. 1 hit.
SM00477. NUC. 1 hit.
SM00201. SO. 2 hits.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
SSF90188. SSF90188. 2 hits.
PROSITEiPS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiENPP2_RAT
AccessioniPrimary (citable) accession number: Q64610
Secondary accession number(s): Q66HQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: March 20, 2007
Last modified: November 30, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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.