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Q5KU26

- COL12_HUMAN

UniProt

Q5KU26 - COL12_HUMAN

Protein

Collectin-12

Gene

COLEC12

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    Functioni

    Scavenger receptor that displays several functions associated with host defense. Promotes binding and phagocytosis of Gram-positive, Gram-negative bacteria and yeast. Mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. Binds to several carbohydrates including Gal-type ligands, D-galactose, L- and D-fucose, GalNAc, T and Tn antigens in a calcium-dependent manner and internalizes specifically GalNAc in nurse-like cells. Binds also to sialyl Lewis X or a trisaccharide and asialo-orosomucoid (ASOR). May also play a role in the clearance of amyloid beta in Alzheimer disease.5 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi644 – 6441Calcium 1; via carbonyl oxygen
    Metal bindingi646 – 6461Calcium 1
    Metal bindingi650 – 6501Calcium 1
    Metal bindingi670 – 6701Calcium 2
    Metal bindingi674 – 6741Calcium 2
    Binding sitei691 – 6911CarbohydrateBy similarity
    Metal bindingi694 – 6941Calcium 3
    Binding sitei694 – 6941CarbohydrateBy similarity
    Metal bindingi696 – 6961Calcium 3
    Binding sitei696 – 6961CarbohydrateBy similarity
    Metal bindingi697 – 6971Calcium 2
    Metal bindingi706 – 7061Calcium 2; via carbonyl oxygen
    Metal bindingi706 – 7061Calcium 3
    Binding sitei706 – 7061CarbohydrateBy similarity
    Metal bindingi707 – 7071Calcium 2
    Metal bindingi718 – 7181Calcium 3
    Binding sitei718 – 7181CarbohydrateBy similarity
    Metal bindingi719 – 7191Calcium 3
    Binding sitei719 – 7191Carbohydrate; via carbonyl oxygenBy similarity
    Metal bindingi731 – 7311Calcium 1

    GO - Molecular functioni

    1. galactose binding Source: UniProtKB
    2. low-density lipoprotein particle binding Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. scavenger receptor activity Source: UniProtKB
    5. signaling pattern recognition receptor activity Source: UniProtKB

    GO - Biological processi

    1. carbohydrate mediated signaling Source: UniProtKB
    2. defense response Source: UniProtKB
    3. innate immune response Source: UniProtKB
    4. pattern recognition receptor signaling pathway Source: GOC
    5. phagocytosis, recognition Source: UniProtKB
    6. protein homooligomerization Source: UniProtKB
    7. receptor-mediated endocytosis Source: GOC

    Keywords - Molecular functioni

    Receptor

    Keywords - Ligandi

    Calcium, Lectin, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_163699. Scavenging by Class A Receptors.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collectin-12
    Alternative name(s):
    Collectin placenta protein 1
    Short name:
    CL-P1
    Short name:
    hCL-P1
    Nurse cell scavenger receptor 2
    Scavenger receptor class A member 4
    Scavenger receptor with C-type lectin
    Gene namesi
    Name:COLEC12
    Synonyms:CLP1, NSR2, SCARA4, SRCL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:16016. COLEC12.

    Subcellular locationi

    Membrane 1 Publication; Single-pass type II membrane protein 1 Publication
    Note: Forms clusters on the cell surface.

    GO - Cellular componenti

    1. collagen trimer Source: UniProtKB-KW
    2. endocytic vesicle membrane Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. integral component of membrane Source: UniProtKB
    5. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26738.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 742742Collectin-12PRO_0000318681Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi67 – 671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi159 – 1591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi168 – 1681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi271 – 2711N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi607 ↔ 6181 PublicationPROSITE-ProRule annotation
    Disulfide bondi635 ↔ 7301 PublicationPROSITE-ProRule annotation
    Disulfide bondi708 ↔ 7221 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ5KU26.
    PaxDbiQ5KU26.
    PRIDEiQ5KU26.

    PTM databases

    PhosphoSiteiQ5KU26.

    Expressioni

    Tissue specificityi

    Expressed in perivascular macrophages. Expressed in plaques-surrounding reactive astrocytes and in perivascular astrocytes associated with cerebral amyloid angiopathy (CAA) in the temporal cortex of Alzheimer patient (at protein level). Strongly expressed in placenta. Moderately expressed in heart, skeletal muscle, small intestine and lung. Weakly expressed in brain, colon, thymus and kidney. Expressed in nurse-like cells. Expressed in reactive astrocytes and vascular/perivascular cells in the brain of Alzheimer patient.4 Publications

    Gene expression databases

    BgeeiQ5KU26.
    CleanExiHS_CLP1.
    HS_COLEC12.
    GenevestigatoriQ5KU26.

    Organism-specific databases

    HPAiHPA047917.

    Interactioni

    Subunit structurei

    The extracellular domain forms a stable trimer. The extracellular domain interacts with fibrillar beta amyloid peptide.3 Publications

    Protein-protein interaction databases

    BioGridi123353. 2 interactions.
    IntActiQ5KU26. 1 interaction.
    STRINGi9606.ENSP00000383115.

    Structurei

    Secondary structure

    1
    742
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi612 – 6143
    Beta strandi617 – 6215
    Helixi628 – 63710
    Helixi648 – 65710
    Beta strandi664 – 6696
    Beta strandi671 – 6733
    Turni692 – 7009
    Beta strandi708 – 7114
    Beta strandi717 – 7204
    Beta strandi726 – 7338

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2OX8X-ray2.50A/B/C/D607-742[»]
    ProteinModelPortaliQ5KU26.
    SMRiQ5KU26. Positions 607-734.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5KU26.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 3737CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini59 – 742684ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei38 – 5821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini443 – 47230Collagen-like 1Add
    BLAST
    Domaini473 – 52957Collagen-like 2Add
    BLAST
    Domaini530 – 58960Collagen-like 3Add
    BLAST
    Domaini614 – 731118C-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili73 – 14169Sequence AnalysisAdd
    BLAST
    Coiled coili215 – 328114Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 C-type lectin domain.PROSITE-ProRule annotation
    Contains 3 collagen-like domains.Curated

    Keywords - Domaini

    Coiled coil, Collagen, Repeat, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG147335.
    HOGENOMiHOG000111886.
    HOVERGENiHBG107745.
    InParanoidiQ5KU26.
    KOiK10062.
    OMAiEQQWIKK.
    OrthoDBiEOG74XS65.
    PhylomeDBiQ5KU26.
    TreeFamiTF332426.

    Family and domain databases

    Gene3Di3.10.100.10. 1 hit.
    InterProiIPR001304. C-type_lectin.
    IPR016186. C-type_lectin-like.
    IPR018378. C-type_lectin_CS.
    IPR016187. C-type_lectin_fold.
    IPR008160. Collagen.
    [Graphical view]
    PfamiPF01391. Collagen. 2 hits.
    PF00059. Lectin_C. 1 hit.
    [Graphical view]
    SMARTiSM00034. CLECT. 1 hit.
    [Graphical view]
    SUPFAMiSSF56436. SSF56436. 1 hit.
    PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
    PS50041. C_TYPE_LECTIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q5KU26-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKDDFAEEEE VQSFGYKRFG IQEGTQCTKC KNNWALKFSI ILLYILCALL    50
    TITVAILGYK VVEKMDNVTG GMETSRQTYD DKLTAVESDL KKLGDQTGKK 100
    AISTNSELST FRSDILDLRQ QLREITEKTS KNKDTLEKLQ ASGDALVDRQ 150
    SQLKETLENN SFLITTVNKT LQAYNGYVTN LQQDTSVLQG NLQNQMYSHN 200
    VVIMNLNNLN LTQVQQRNLI TNLQRSVDDT SQAIQRIKND FQNLQQVFLQ 250
    AKKDTDWLKE KVQSLQTLAA NNSALAKANN DTLEDMNSQL NSFTGQMENI 300
    TTISQANEQN LKDLQDLHKD AENRTAIKFN QLEERFQLFE TDIVNIISNI 350
    SYTAHHLRTL TSNLNEVRTT CTDTLTKHTD DLTSLNNTLA NIRLDSVSLR 400
    MQQDLMRSRL DTEVANLSVI MEEMKLVDSK HGQLIKNFTI LQGPPGPRGP 450
    RGDRGSQGPP GPTGNKGQKG EKGEPGPPGP AGERGPIGPA GPPGERGGKG 500
    SKGSQGPKGS RGSPGKPGPQ GSSGDPGPPG PPGKEGLPGP QGPPGFQGLQ 550
    GTVGEPGVPG PRGLPGLPGV PGMPGPKGPP GPPGPSGAVV PLALQNEPTP 600
    APEDNGCPPH WKNFTDKCYY FSVEKEIFED AKLFCEDKSS HLVFINTREE 650
    QQWIKKQMVG RESHWIGLTD SERENEWKWL DGTSPDYKNW KAGQPDNWGH 700
    GHGPGEDCAG LIYAGQWNDF QCEDVNNFIC EKDRETVLSS AL 742
    Length:742
    Mass (Da):81,515
    Last modified:May 18, 2010 - v3
    Checksum:i85A003C1D6A83949
    GO

    Sequence cautioni

    The sequence BAB39148.1 differs from that shown. Reason: Probable cloning artifact.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121Q → P in BAB39148. (PubMed:11162630)Curated
    Sequence conflicti16 – 161Y → F in BAB39148. (PubMed:11162630)Curated
    Sequence conflicti22 – 221Q → H in BAB39148. (PubMed:11162630)Curated
    Sequence conflicti28 – 281T → P in BAB39148. (PubMed:11162630)Curated
    Sequence conflicti31 – 311K → H in BAB39148. (PubMed:11162630)Curated
    Sequence conflicti72 – 721M → V in BAD83592. (PubMed:12761161)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti91 – 911K → E.1 Publication
    Corresponds to variant rs17855029 [ dbSNP | Ensembl ].
    VAR_038853
    Natural varianti487 – 4871I → V.
    Corresponds to variant rs8098850 [ dbSNP | Ensembl ].
    VAR_038854
    Natural varianti522 – 5221S → P.5 Publications
    Corresponds to variant rs2305025 [ dbSNP | Ensembl ].
    VAR_038855
    Natural varianti606 – 6061G → S.3 Publications
    Corresponds to variant rs2305027 [ dbSNP | Ensembl ].
    VAR_038856

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB038518 mRNA. Translation: BAB39147.1.
    AB052103 mRNA. Translation: BAB39148.1. Sequence problems.
    AB005145 mRNA. Translation: BAB72147.1.
    AB034251 mRNA. Translation: BAD83592.1.
    AP000915 Genomic DNA. No translation available.
    AP005240 Genomic DNA. No translation available.
    BC060789 mRNA. Translation: AAH60789.1.
    AL713657 mRNA. Translation: CAD28466.1.
    CCDSiCCDS32782.1.
    PIRiJC7595.
    RefSeqiNP_569057.1. NM_130386.2.
    UniGeneiHs.464422.

    Genome annotation databases

    EnsembliENST00000400256; ENSP00000383115; ENSG00000158270.
    GeneIDi81035.
    KEGGihsa:81035.
    UCSCiuc002kkm.3. human.

    Polymorphism databases

    DMDMi296439391.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB038518 mRNA. Translation: BAB39147.1 .
    AB052103 mRNA. Translation: BAB39148.1 . Sequence problems.
    AB005145 mRNA. Translation: BAB72147.1 .
    AB034251 mRNA. Translation: BAD83592.1 .
    AP000915 Genomic DNA. No translation available.
    AP005240 Genomic DNA. No translation available.
    BC060789 mRNA. Translation: AAH60789.1 .
    AL713657 mRNA. Translation: CAD28466.1 .
    CCDSi CCDS32782.1.
    PIRi JC7595.
    RefSeqi NP_569057.1. NM_130386.2.
    UniGenei Hs.464422.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2OX8 X-ray 2.50 A/B/C/D 607-742 [» ]
    ProteinModelPortali Q5KU26.
    SMRi Q5KU26. Positions 607-734.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123353. 2 interactions.
    IntActi Q5KU26. 1 interaction.
    STRINGi 9606.ENSP00000383115.

    PTM databases

    PhosphoSitei Q5KU26.

    Polymorphism databases

    DMDMi 296439391.

    Proteomic databases

    MaxQBi Q5KU26.
    PaxDbi Q5KU26.
    PRIDEi Q5KU26.

    Protocols and materials databases

    DNASUi 81035.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000400256 ; ENSP00000383115 ; ENSG00000158270 .
    GeneIDi 81035.
    KEGGi hsa:81035.
    UCSCi uc002kkm.3. human.

    Organism-specific databases

    CTDi 81035.
    GeneCardsi GC18M000309.
    HGNCi HGNC:16016. COLEC12.
    HPAi HPA047917.
    MIMi 607621. gene.
    neXtProti NX_Q5KU26.
    PharmGKBi PA26738.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG147335.
    HOGENOMi HOG000111886.
    HOVERGENi HBG107745.
    InParanoidi Q5KU26.
    KOi K10062.
    OMAi EQQWIKK.
    OrthoDBi EOG74XS65.
    PhylomeDBi Q5KU26.
    TreeFami TF332426.

    Enzyme and pathway databases

    Reactomei REACT_163699. Scavenging by Class A Receptors.

    Miscellaneous databases

    ChiTaRSi COLEC12. human.
    EvolutionaryTracei Q5KU26.
    GenomeRNAii 81035.
    NextBioi 71376.
    PROi Q5KU26.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q5KU26.
    CleanExi HS_CLP1.
    HS_COLEC12.
    Genevestigatori Q5KU26.

    Family and domain databases

    Gene3Di 3.10.100.10. 1 hit.
    InterProi IPR001304. C-type_lectin.
    IPR016186. C-type_lectin-like.
    IPR018378. C-type_lectin_CS.
    IPR016187. C-type_lectin_fold.
    IPR008160. Collagen.
    [Graphical view ]
    Pfami PF01391. Collagen. 2 hits.
    PF00059. Lectin_C. 1 hit.
    [Graphical view ]
    SMARTi SM00034. CLECT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56436. SSF56436. 1 hit.
    PROSITEi PS00615. C_TYPE_LECTIN_1. 1 hit.
    PS50041. C_TYPE_LECTIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and functional characterization of a human scavenger receptor with C-type lectin (SRCL), a novel member of a scavenger receptor family."
      Nakamura K., Funakoshi H., Miyamoto K., Tokunaga F., Nakamura T.
      Biochem. Biophys. Res. Commun. 280:1028-1035(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS PRO-522 AND SER-606.
      Tissue: Placenta.
    2. "The membrane-type collectin CL-P1 is a scavenger receptor on vascular endothelial cells."
      Ohtani K., Suzuki Y., Eda S., Kawai T., Kase T., Keshi H., Sakai Y., Fukuoh A., Sakamoto T., Itabe H., Suzutani T., Ogasawara M., Yoshida I., Wakamiya N.
      J. Biol. Chem. 276:44222-44228(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, VARIANT PRO-522.
      Tissue: Lung and Placenta.
    3. "SRCL/CL-P1 recognizes GalNAc and a carcinoma-associated antigen, Tn antigen."
      Yoshida T., Tsuruta Y., Iwasaki M., Yamane S., Ochi T., Suzuki R.
      J. Biochem. 133:271-277(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, VARIANT PRO-522.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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], VARIANTS GLU-91; PRO-522 AND SER-606.
      Tissue: Placenta.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 326-742.
      Tissue: Brain.
    7. "Haplotype analysis of the human collectin placenta 1 (hCL-P1) gene."
      Ohmori H., Makita Y., Funamizu M., Chiba S., Ohtani K., Suzuki Y., Wakamiya N., Hata A.
      J. Hum. Genet. 48:82-85(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PRO-522 AND SER-606.
    8. "Selective binding of the scavenger receptor C-type lectin to Lewis X trisaccharide and related glycan ligands."
      Coombs P.J., Graham S.A., Drickamer K., Taylor M.E.
      J. Biol. Chem. 280:22993-22999(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    9. "Possible role of scavenger receptor SRCL in the clearance of amyloid-beta in Alzheimer's disease."
      Nakamura K., Ohya W., Funakoshi H., Sakaguchi G., Kato A., Takeda M., Kudo T., Nakamura T.
      J. Neurosci. Res. 84:874-890(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FIBRILLAR BETA AMYLOID PEPTIDE, FUNCTION IN CLEARANCE OF AMYLOID BETA, TISSUE SPECIFICITY.
    10. "Scavenger receptor C-type lectin binds to the leukocyte cell surface glycan Lewis X by a novel mechanism."
      Feinberg H., Taylor M.E., Weis W.I.
      J. Biol. Chem. 282:17250-17258(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 603-742 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BONDS.

    Entry informationi

    Entry nameiCOL12_HUMAN
    AccessioniPrimary (citable) accession number: Q5KU26
    Secondary accession number(s): Q6P9F2
    , Q8TCR2, Q8WZA4, Q9BY85, Q9BYH7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 87 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3