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O35627

- NR1I3_MOUSE

UniProt

O35627 - NR1I3_MOUSE

Protein

Nuclear receptor subfamily 1 group I member 3

Gene

Nr1i3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Binds and transactivates the retinoic acid response elements that control expression of the retinoic acid receptor beta 2 and alcohol dehydrogenase 3 genes. Transactivates both the phenobarbital responsive element module of the human CYP2B6 gene and the CYP3A4 xenobiotic response element By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei171 – 1711Important for TCPOBOP recognition
    Sitei175 – 1751Important for TCPOBOP recognition
    Sitei216 – 2161Important for TCPOBOP recognition
    Sitei227 – 2271Important for TCPOBOP recognition
    Sitei244 – 2441Important for TCPOBOP recognition
    Sitei336 – 3361Important for TCPOBOP recognition

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi18 – 9376Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri21 – 4121NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri57 – 8125NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: MGI
    2. protein binding Source: UniProtKB
    3. sequence-specific DNA binding Source: InterPro
    4. steroid hormone receptor activity Source: InterPro
    5. thyroid hormone receptor activity Source: InterPro
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. negative regulation of transcription, DNA-templated Source: MGI
    2. regulation of transcription, DNA-templated Source: MGI

    Keywords - Molecular functioni

    Activator, Receptor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear receptor subfamily 1 group I member 3
    Alternative name(s):
    Constitutive androstane receptor
    Short name:
    CAR
    Orphan nuclear receptor MB67
    Gene namesi
    Name:Nr1i3
    Synonyms:Car
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1346307. Nr1i3.

    Subcellular locationi

    Nucleus. Cytoplasm. Cytoplasmcytoskeleton By similarity
    Note: Recruited to the cytoplasm by DNAJC7.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoskeleton Source: UniProtKB-SubCell
    3. cytosol Source: MGI
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi171 – 1711F → W: Diminished binding of coactivator NCOA2 in the presence of TCPOBOP. 1 Publication
    Mutagenesisi175 – 1751N → F: Diminished binding of coactivator NCOA2 in the presence of TCPOBOP. 1 Publication
    Mutagenesisi216 – 2161L → F: Diminished binding of coactivator NCOA2 in the presence of TCPOBOP. 1 Publication
    Mutagenesisi227 – 2271F → W: Diminished binding of coactivator NCOA2 in the presence of TCPOBOP. 1 Publication
    Mutagenesisi234 – 2341Y → A: No effect on binding of coactivator NCOA2 in the presence of TCPOBOP. 1 Publication
    Mutagenesisi244 – 2441F → A: Diminished binding of coactivator NCOA2 in the presence of TCPOBOP. 1 Publication
    Mutagenesisi336 – 3361Y → A: Diminished binding of coactivator NCOA2 in the presence of TCPOBOP. 1 Publication
    Mutagenesisi346 – 3461L → F: Dramatic increase in binding NCOA2. Little effect on binding of coactivator NCOA2 in the presence of TCPOBOP. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 358358Nuclear receptor subfamily 1 group I member 3PRO_0000053554Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei48 – 481Phosphothreonine; by PKCBy similarity

    Post-translational modificationi

    Phosphorylated at Thr-48 by PKC, dephosphorylation of Thr-48 is required for nuclear translocation and activation.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiO35627.

    PTM databases

    PhosphoSiteiO35627.

    Expressioni

    Tissue specificityi

    Predominantly expressed in liver.

    Gene expression databases

    BgeeiO35627.
    CleanExiMM_NR1I3.
    GenevestigatoriO35627.

    Interactioni

    Subunit structurei

    Heterodimer of NR1I3 and RXR. Interacts with PSMC4. Interacts with ECT2. Directly interacts with DNAJC7; this complex may also include HSP90.4 Publications

    Protein-protein interaction databases

    BioGridi198489. 12 interactions.

    Structurei

    Secondary structure

    1
    358
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi118 – 13417
    Turni135 – 1373
    Helixi138 – 1447
    Helixi149 – 1524
    Beta strandi160 – 1623
    Helixi164 – 18724
    Helixi190 – 1934
    Helixi197 – 21620
    Helixi217 – 2193
    Turni222 – 2254
    Beta strandi226 – 2294
    Beta strandi232 – 2343
    Helixi236 – 2416
    Helixi246 – 26015
    Helixi266 – 27712
    Helixi288 – 30821
    Turni309 – 3124
    Helixi318 – 33518
    Helixi337 – 3437
    Helixi345 – 3495
    Helixi351 – 3577

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XLSX-ray2.96E/F/G/H117-358[»]
    1XNXX-ray2.90A/B109-358[»]
    ProteinModelPortaliO35627.
    SMRiO35627. Positions 21-356.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO35627.

    Family & Domainsi

    Domaini

    Composed by a short N-terminal domain followed by the DNA binding, hinge, and ligand binding/dimerization domains.

    Sequence similaritiesi

    Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri21 – 4121NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri57 – 8125NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG251788.
    GeneTreeiENSGT00720000108423.
    HOGENOMiHOG000220844.
    HOVERGENiHBG108655.
    InParanoidiQ3V008.
    KOiK08541.
    OMAiPRDRFLY.
    OrthoDBiEOG7SXW4K.
    TreeFamiTF316304.

    Family and domain databases

    Gene3Di1.10.565.10. 2 hits.
    3.30.50.10. 1 hit.
    InterProiIPR008946. Nucl_hormone_rcpt_ligand-bd.
    IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
    IPR001723. Str_hrmn_rcpt.
    IPR001728. ThyrH_rcpt.
    IPR001628. Znf_hrmn_rcpt.
    IPR013088. Znf_NHR/GATA.
    [Graphical view]
    PfamiPF00104. Hormone_recep. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view]
    PRINTSiPR00398. STRDHORMONER.
    PR00047. STROIDFINGER.
    PR00546. THYROIDHORMR.
    SMARTiSM00430. HOLI. 1 hit.
    SM00399. ZnF_C4. 1 hit.
    [Graphical view]
    SUPFAMiSSF48508. SSF48508. 1 hit.
    PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
    PS51030. NUCLEAR_REC_DBD_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform CAR1 (identifier: O35627-1) [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

    MTAMLTLETM ASEEEYGPRN CVVCGDRATG YHFHALTCEG CKGFFRRTVS    50
    KTIGPICPFA GRCEVSKAQR RHCPACRLQK CLNVGMRKDM ILSAEALALR 100
    RARQAQRRAE KASLQLNQQQ KELVQILLGA HTRHVGPMFD QFVQFKPPAY 150
    LFMHHRPFQP RGPVLPLLTH FADINTFMVQ QIIKFTKDLP LFRSLTMEDQ 200
    ISLLKGAAVE ILHISLNTTF CLQTENFFCG PLCYKMEDAV HAGFQYEFLE 250
    SILHFHKNLK GLHLQEPEYV LMAATALFSP DRPGVTQREE IDQLQEEMAL 300
    ILNNHIMEQQ SRLQSRFLYA KLMGLLADLR SINNAYSYEL QRLEELSAMT 350
    PLLGEICS 358
    Length:358
    Mass (Da):40,913
    Last modified:July 27, 2011 - v2
    Checksum:iA11C92B1EC2C06A7
    GO
    Isoform CAR2 (identifier: O35627-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         281-286: DRPGVT → GFCMQS
         287-358: Missing.

    Note: Does not seem to act as a transactivator. Lacks the C-terminal portion of the ligand binding/dimerization domain.

    Show »
    Length:286
    Mass (Da):32,544
    Checksum:iDAEF17A3369F529E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti138 – 1381M → L in AAC53349. (PubMed:9295294)Curated
    Sequence conflicti138 – 1381M → L in AAC53350. (PubMed:9295294)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei281 – 2866DRPGVT → GFCMQS in isoform CAR2. 1 PublicationVSP_003671
    Alternative sequencei287 – 35872Missing in isoform CAR2. 1 PublicationVSP_003672Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF009327 mRNA. Translation: AAC53349.1.
    AF009328 mRNA. Translation: AAC53350.1.
    AK133515 mRNA. Translation: BAE21697.1.
    CH466520 Genomic DNA. Translation: EDL39126.1.
    CCDSiCCDS15480.1. [O35627-1]
    CCDS56654.1. [O35627-2]
    RefSeqiNP_001229991.1. NM_001243062.1. [O35627-2]
    NP_001229992.1. NM_001243063.1.
    NP_033933.2. NM_009803.5. [O35627-1]
    UniGeneiMm.486506.

    Genome annotation databases

    EnsembliENSMUST00000005820; ENSMUSP00000005820; ENSMUSG00000005677. [O35627-1]
    ENSMUST00000075469; ENSMUSP00000074915; ENSMUSG00000005677. [O35627-2]
    GeneIDi12355.
    KEGGimmu:12355.
    UCSCiuc007dnf.2. mouse. [O35627-1]
    uc007dng.2. mouse. [O35627-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF009327 mRNA. Translation: AAC53349.1 .
    AF009328 mRNA. Translation: AAC53350.1 .
    AK133515 mRNA. Translation: BAE21697.1 .
    CH466520 Genomic DNA. Translation: EDL39126.1 .
    CCDSi CCDS15480.1. [O35627-1 ]
    CCDS56654.1. [O35627-2 ]
    RefSeqi NP_001229991.1. NM_001243062.1. [O35627-2 ]
    NP_001229992.1. NM_001243063.1.
    NP_033933.2. NM_009803.5. [O35627-1 ]
    UniGenei Mm.486506.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XLS X-ray 2.96 E/F/G/H 117-358 [» ]
    1XNX X-ray 2.90 A/B 109-358 [» ]
    ProteinModelPortali O35627.
    SMRi O35627. Positions 21-356.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198489. 12 interactions.

    Chemistry

    BindingDBi O35627.
    ChEMBLi CHEMBL3069.
    GuidetoPHARMACOLOGYi 607.

    PTM databases

    PhosphoSitei O35627.

    Proteomic databases

    PRIDEi O35627.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000005820 ; ENSMUSP00000005820 ; ENSMUSG00000005677 . [O35627-1 ]
    ENSMUST00000075469 ; ENSMUSP00000074915 ; ENSMUSG00000005677 . [O35627-2 ]
    GeneIDi 12355.
    KEGGi mmu:12355.
    UCSCi uc007dnf.2. mouse. [O35627-1 ]
    uc007dng.2. mouse. [O35627-2 ]

    Organism-specific databases

    CTDi 9970.
    MGIi MGI:1346307. Nr1i3.

    Phylogenomic databases

    eggNOGi NOG251788.
    GeneTreei ENSGT00720000108423.
    HOGENOMi HOG000220844.
    HOVERGENi HBG108655.
    InParanoidi Q3V008.
    KOi K08541.
    OMAi PRDRFLY.
    OrthoDBi EOG7SXW4K.
    TreeFami TF316304.

    Miscellaneous databases

    ChiTaRSi NR1I3. mouse.
    EvolutionaryTracei O35627.
    NextBioi 281020.
    PROi O35627.
    SOURCEi Search...

    Gene expression databases

    Bgeei O35627.
    CleanExi MM_NR1I3.
    Genevestigatori O35627.

    Family and domain databases

    Gene3Di 1.10.565.10. 2 hits.
    3.30.50.10. 1 hit.
    InterProi IPR008946. Nucl_hormone_rcpt_ligand-bd.
    IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
    IPR001723. Str_hrmn_rcpt.
    IPR001728. ThyrH_rcpt.
    IPR001628. Znf_hrmn_rcpt.
    IPR013088. Znf_NHR/GATA.
    [Graphical view ]
    Pfami PF00104. Hormone_recep. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view ]
    PRINTSi PR00398. STRDHORMONER.
    PR00047. STROIDFINGER.
    PR00546. THYROIDHORMR.
    SMARTi SM00430. HOLI. 1 hit.
    SM00399. ZnF_C4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48508. SSF48508. 1 hit.
    PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
    PS51030. NUCLEAR_REC_DBD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Differential transactivation by two isoforms of the orphan nuclear hormone receptor CAR."
      Choi H.-S., Chung M., Tzameli I., Simha D., Lee Y.-K., Seol W., Moore D.D.
      J. Biol. Chem. 272:23565-23571(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CAR1 AND CAR2).
      Tissue: Liver.
    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] (ISOFORM CAR1).
      Strain: C57BL/6J.
      Tissue: Ovary and Uterus.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "P450 gene induction by structurally diverse xenochemicals: central role of nuclear receptors CAR, PXR, and PPAR."
      Waxman D.J.
      Arch. Biochem. Biophys. 369:11-23(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "A component of the 26S proteasome binds on orphan member of the nuclear hormone receptor superfamily."
      Choi H.S., Seol W., Moore D.D.
      J. Steroid Biochem. Mol. Biol. 56:23-30(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PSMC4.
    6. "Cytoplasmic accumulation of the nuclear receptor CAR by a tetratricopeptide repeat protein in HepG2 cells."
      Kobayashi K., Sueyoshi T., Inoue K., Moore R., Negishi M.
      Mol. Pharmacol. 64:1069-1075(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DNAJC7 AND HSP90, SUBCELLULAR LOCATION.
    7. "Overexpression of the Rho-guanine nucleotide exchange factor ECT2 inhibits nuclear translocation of nuclear receptor CAR in the mouse liver."
      Hosseinpour F., Timsit Y., Koike C., Matsui K., Yamamoto Y., Moore R., Negishi M.
      FEBS Lett. 581:4937-4942(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ECT2, SUBCELLULAR LOCATION.
    8. "The nuclear xenobiotic receptor CAR: structural determinants of constitutive activation and heterodimerization."
      Suino K., Peng L., Reynolds R., Li Y., Cha J.Y., Repa J.J., Kliewer S.A., Xu H.E.
      Mol. Cell 16:893-905(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 227-458 IN COMPLEX WITH H.SAPIENS RXRA; R.NORVEGICUS NCOA2 AND AGONIST INSECTICIDE CONTAMINANT TCPOBOP, MUTAGENESIS OF PHE-171; ASN-175; LEU-216; PHE-227; TYR-234; PHE-244; TYR-336 AND LEU-346.

    Entry informationi

    Entry nameiNR1I3_MOUSE
    AccessioniPrimary (citable) accession number: O35627
    Secondary accession number(s): O35628, Q3V008
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 134 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, 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

    External Data

    Dasty 3