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Protein

Thioredoxin reductase 3

Gene

Txnrd3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Displays thioredoxin reductase, glutaredoxin and glutathione reductase activities. Catalyzes disulfide bond isomerization. Promotes disulfide bond formation between GPX4 and various sperm proteins and may play a role in sperm maturation by promoting formation of sperm structural components.2 Publications

Catalytic activityi

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.1 Publication

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Kineticsi

  1. KM=14.7 µM for 5,5'-dithiobis(2-nitrobenzoic acid)1 Publication
  2. KM=10.7 µM for NADPH1 Publication
  3. KM=3.0 µM for thioredoxin1 Publication
  4. KM=8.84 µM for oxidized glutathione1 Publication
  5. KM=45.2 µM for beta-hydroxyethyl disulfide1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei625 – 6251Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi167 – 19630FADBy similarityAdd
    BLAST

    GO - Molecular functioni

    GO - Biological processi

    • cell differentiation Source: UniProtKB-KW
    • cell redox homeostasis Source: InterPro
    • cellular oxidant detoxification Source: GOC
    • glutathione metabolic process Source: MGI
    • multicellular organism development Source: UniProtKB-KW
    • spermatogenesis Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Developmental protein, Oxidoreductase

    Keywords - Biological processi

    Differentiation, Electron transport, Spermatogenesis, Transport

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    BRENDAi1.8.1.B1. 3474.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thioredoxin reductase 3 (EC:1.8.1.9)
    Alternative name(s):
    Thioredoxin and glutathione reductase
    Thioredoxin reductase TR2
    Gene namesi
    Name:Txnrd3Imported
    Synonyms:TgrImported, Trxr3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    Proteomesi
    • UP000000589 Componenti: Unplaced

    Organism-specific databases

    MGIiMGI:2386711. Txnrd3.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Microsome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi651 – 6522Missing : Abolishes thioredoxin reductase, glutaredoxin and gluthioine reductase activities. 1 Publication
    Mutagenesisi651 – 6511U → C: Thioredoxin reductase activity reduced to 21%. Glutaredoxin activity reduced to 14%. Glutathione reductase activity reduced to 18%. 1 Publication
    Mutagenesisi651 – 6511U → S: Abolishes thioredoxin reductase, glutaredoxin and gluthioine reductase activities. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 652652Thioredoxin reductase 3PRO_0000320696Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei50 – 501PhosphoserineBy similarity
    Disulfide bondi212 ↔ 217Redox-activeBy similarity
    Modified residuei388 – 3881N6-succinyllysineCombined sources
    Cross-linki650 ↔ 651Cysteinyl-selenocysteine (Cys-Sec)By similarity

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    EPDiQ99MD6.
    MaxQBiQ99MD6.
    PaxDbiQ99MD6.
    PRIDEiQ99MD6.

    PTM databases

    iPTMnetiQ99MD6.
    PhosphoSiteiQ99MD6.

    Expressioni

    Tissue specificityi

    Expressed preferentially in testis where it is found in spermatids and spermatocytes but not in sperm. In elongating spermatids, expressed at the site of mitochondrial sheath formation. Low levels in other tissues including heart, lung, liver, kidney, brain, muscle and prostate.3 Publications

    Developmental stagei

    Accumulates in the testis after puberty. Not detected in 20-day-old mice but highly expressed in testes of 7-month-old mice.1 Publication

    Gene expression databases

    CleanExiMM_TXNRD3.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000000828.

    Structurei

    Secondary structure

    1
    652
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi61 – 7414Combined sources
    Beta strandi75 – 817Combined sources
    Turni86 – 894Combined sources
    Helixi90 – 978Combined sources
    Beta strandi103 – 1064Combined sources
    Turni107 – 1093Combined sources
    Helixi113 – 12412Combined sources
    Beta strandi126 – 1283Combined sources
    Beta strandi133 – 1364Combined sources
    Helixi144 – 1518Combined sources
    Helixi155 – 1595Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LV3NMR-A60-161[»]
    ProteinModelPortaliQ99MD6.
    SMRiQ99MD6. Positions 68-645.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini65 – 165101GlutaredoxinPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The N-terminal glutaredoxin domain does not contain the C-X-X-C redox-active motif normally found in glutaredoxins but activity may be mediated through a single cysteine. The C-terminal Cys-Sec motif of one subunit of the homodimer may transfer electrons from the thiol-disulfide center to the glutaredoxin domain of the other subunit.2 Publications

    Sequence similaritiesi

    Contains 1 glutaredoxin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiKOG1752. Eukaryota.
    KOG4716. Eukaryota.
    COG1249. LUCA.
    HOGENOMiHOG000276712.
    HOVERGENiHBG004959.
    InParanoidiQ99MD6.
    KOiK00384.

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    3.40.30.10. 1 hit.
    3.50.50.60. 2 hits.
    InterProiIPR023753. FAD/NAD-binding_dom.
    IPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR002109. Glutaredoxin.
    IPR011899. Glutaredoxin_euk/vir.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR012999. Pyr_OxRdtase_I_AS.
    IPR012336. Thioredoxin-like_fold.
    IPR006338. Thioredoxin/glutathione_Rdtase.
    [Graphical view]
    PfamiPF00462. Glutaredoxin. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 1 hit.
    SSF52833. SSF52833. 1 hit.
    SSF55424. SSF55424. 1 hit.
    TIGRFAMsiTIGR02180. GRX_euk. 1 hit.
    TIGR01438. TGR. 1 hit.
    PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
    PS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q99MD6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MEKPPSPPPP PRAQTSPGLG KVGVLPNRRL GAVRGGLMSS PPGRRARLAS
    60 70 80 90 100
    PGTSRPSSEA REELRRRLRD LIEGNRVMIF SKSYCPHSTR VKELFSSLGV
    110 120 130 140 150
    VYNILELDQV DDGASVQEVL TEISNQKTVP NIFVNKVHVG GCDRTFQAHQ
    160 170 180 190 200
    NGLLQKLLQD DSAHDYDLII IGGGSGGLSC AKEAANLGKK VMVLDFVVPS
    210 220 230 240 250
    PQGTTWGLGG TCVNVGCIPK KLMHQAALLG HALQDAKKYG WEYNQQVKHN
    260 270 280 290 300
    WEAMTEAIQS HIGSLNWGYR VTLREKGVTY VNSFGEFVDL HKIKATNKKG
    310 320 330 340 350
    QETFYTASKF VIATGERPRY LGIQGDKEYC ITSDDLFSLP YCPGCTLVVG
    360 370 380 390 400
    ASYVGLECAG FLAGLGLDVT VMVRSVLLRG FDQEMAEKVG SYLEQQGVKF
    410 420 430 440 450
    QRKFTPILVQ QLEKGLPGKL KVVAKSTEGP ETVEGIYNTV LLAIGRDSCT
    460 470 480 490 500
    RKIGLEKIGV KINEKNGKIP VNDVEQTNVP HVYAIGDILD GKPELTPVAI
    510 520 530 540 550
    QAGKLLARRL FGVSLEKCDY INIPTTVFTP LEYGCCGLSE EKAIEMYKKE
    560 570 580 590 600
    NLEVYHTLFW PLEWTVAGRD NNTCYAKIIC NKFDNERVVG FHLLGPNAGE
    610 620 630 640 650
    ITQGFAAAMK CGLTKQLLDD TIGIHPTCGE VFTTLEITKS SGLDITQKGC

    UG
    Length:652
    Mass (Da):71,319
    Last modified:May 29, 2013 - v3
    Checksum:iAC6342C64DDEC1BC
    GO

    Sequence cautioni

    The sequence AAH76605.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
    The sequence AAH76605.1 differs from that shown. Reason: Erroneous termination at position 651. Translated as Sec.Curated
    The sequence AAK31172.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence BAB28419.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
    The sequence BAB28419.1 differs from that shown. Reason: Frameshift at positions 29 and 38. Curated
    The sequence BAB28419.1 differs from that shown. Reason: Erroneous termination at position 651. Translated as Sec.Curated
    The sequence BAC37890.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
    The sequence BAC37890.1 differs from that shown. Reason: Erroneous termination at position 651. Translated as Sec.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81P → R in BAB28419 (PubMed:16141072).Curated
    Sequence conflicti16 – 161S → W in BAB28419 (PubMed:16141072).Curated

    Non-standard residue

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-standard residuei651 – 6511Selenocysteine

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF349659 mRNA. Translation: AAK31172.1. Different initiation.
    AK012699 mRNA. Translation: BAB28419.1. Sequence problems.
    AK080362 mRNA. Translation: BAC37890.1. Sequence problems.
    BC076605 mRNA. Translation: AAH76605.1. Sequence problems.
    RefSeqiNP_001171529.1. NM_001178058.1.
    NP_694802.2. NM_153162.3.
    UniGeneiMm.229332.

    Genome annotation databases

    GeneIDi232223.
    KEGGimmu:232223.
    UCSCiuc009cwj.1. mouse.

    Keywords - Coding sequence diversityi

    Selenocysteine

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF349659 mRNA. Translation: AAK31172.1. Different initiation.
    AK012699 mRNA. Translation: BAB28419.1. Sequence problems.
    AK080362 mRNA. Translation: BAC37890.1. Sequence problems.
    BC076605 mRNA. Translation: AAH76605.1. Sequence problems.
    RefSeqiNP_001171529.1. NM_001178058.1.
    NP_694802.2. NM_153162.3.
    UniGeneiMm.229332.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LV3NMR-A60-161[»]
    ProteinModelPortaliQ99MD6.
    SMRiQ99MD6. Positions 68-645.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000000828.

    PTM databases

    iPTMnetiQ99MD6.
    PhosphoSiteiQ99MD6.

    Proteomic databases

    EPDiQ99MD6.
    MaxQBiQ99MD6.
    PaxDbiQ99MD6.
    PRIDEiQ99MD6.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi232223.
    KEGGimmu:232223.
    UCSCiuc009cwj.1. mouse.

    Organism-specific databases

    CTDi114112.
    MGIiMGI:2386711. Txnrd3.

    Phylogenomic databases

    eggNOGiKOG1752. Eukaryota.
    KOG4716. Eukaryota.
    COG1249. LUCA.
    HOGENOMiHOG000276712.
    HOVERGENiHBG004959.
    InParanoidiQ99MD6.
    KOiK00384.

    Enzyme and pathway databases

    BRENDAi1.8.1.B1. 3474.

    Miscellaneous databases

    NextBioi380996.
    PROiQ99MD6.
    SOURCEiSearch...

    Gene expression databases

    CleanExiMM_TXNRD3.

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    3.40.30.10. 1 hit.
    3.50.50.60. 2 hits.
    InterProiIPR023753. FAD/NAD-binding_dom.
    IPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR002109. Glutaredoxin.
    IPR011899. Glutaredoxin_euk/vir.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR012999. Pyr_OxRdtase_I_AS.
    IPR012336. Thioredoxin-like_fold.
    IPR006338. Thioredoxin/glutathione_Rdtase.
    [Graphical view]
    PfamiPF00462. Glutaredoxin. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 1 hit.
    SSF52833. SSF52833. 1 hit.
    SSF55424. SSF55424. 1 hit.
    TIGRFAMsiTIGR02180. GRX_euk. 1 hit.
    TIGR01438. TGR. 1 hit.
    PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
    PS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Selenoprotein oxidoreductase with specificity for thioredoxin and glutathione systems."
      Sun Q.-A., Kirnarsky L., Sherman S., Gladyshev V.N.
      Proc. Natl. Acad. Sci. U.S.A. 98:3673-3678(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, DOMAIN, 3D-STRUCTURE MODELING, SELENOCYSTEINE AT SEC-651.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6JImported.
      Tissue: EmbryoImported and ThymusImported.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6JImported.
      Tissue: BrainImported.
    4. "Redox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductases."
      Sun Q.-A., Wu Y., Zappacosta F., Jeang K.-T., Lee B.J., Hatfield D.L., Gladyshev V.N.
      J. Biol. Chem. 274:24522-24530(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 191-202 AND 550-561, TISSUE SPECIFICITY.
    5. "Reaction mechanism and regulation of mammalian thioredoxin/glutathione reductase."
      Sun Q.-A., Su D., Novoselov S.V., Carlson B.A., Hatfield D.L., Gladyshev V.N.
      Biochemistry 44:14528-14537(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN, MUTAGENESIS OF SEC-651 AND 651-SEC-GLY-652.
    6. "Mammalian selenoprotein thioredoxin-glutathione reductase. Roles in disulfide bond formation and sperm maturation."
      Su D., Novoselov S.V., Sun Q.-A., Moustafa M.E., Zhou Y., Oko R., Hatfield D.L., Gladyshev V.N.
      J. Biol. Chem. 280:26491-26498(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Heart, Kidney, Lung, Pancreas and Testis.
    8. "CUG start codon generates thioredoxin/glutathione reductase isoforms in mouse testes."
      Gerashchenko M.V., Su D., Gladyshev V.N.
      J. Biol. Chem. 285:4595-4602(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NON-AUG INITIATOR START CODON, TISSUE SPECIFICITY.
    9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-388, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiTRXR3_MOUSE
    AccessioniPrimary (citable) accession number: Q99MD6
    Secondary accession number(s): Q9CZE5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: May 29, 2013
    Last modified: May 11, 2016
    This is version 107 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The thioredoxin reductase active site is a redox-active disulfide bond. The selenocysteine residue is also essential for catalytic activity (By similarity).By similarity

    Caution

    This sequence initiates at a CTG codon.1 Publication

    Keywords - Technical termi

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

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.