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Protein

Collectin-12

Gene

Colec12

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

Functioni

Scavenger receptor that displays several functions associated with host defense. Promotes binding and phagocytosis of Gram-positive, Gram-negative bacteria and yeast. Binds also to sialyl Lewis X or a trisaccharide and asialo-orosomucoid (ASOR). Mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells (By similarity). 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 (By similarity).By similarity1 Publication

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 – 6911Carbohydrate
Metal bindingi694 – 6941Calcium 3
Binding sitei694 – 6941Carbohydrate
Metal bindingi696 – 6961Calcium 3
Binding sitei696 – 6961Carbohydrate
Metal bindingi697 – 6971Calcium 2
Metal bindingi706 – 7061Calcium 2; via carbonyl oxygen
Metal bindingi706 – 7061Calcium 3
Binding sitei706 – 7061Carbohydrate
Metal bindingi707 – 7071Calcium 2
Metal bindingi718 – 7181Calcium 3
Binding sitei718 – 7181Carbohydrate
Metal bindingi719 – 7191Calcium 3
Binding sitei719 – 7191Carbohydrate; via carbonyl oxygen
Metal bindingi731 – 7311Calcium 1

GO - Molecular functioni

  • carbohydrate binding Source: MGI
  • low-density lipoprotein particle binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • signaling pattern recognition receptor activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

Calcium, Lectin, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-3000480. Scavenging by Class A Receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Collectin-12
Alternative name(s):
Collectin placenta protein 1
Short name:
CL-P1
Scavenger receptor with C-type lectin
Gene namesi
Name:Colec12
Synonyms:Clp1, Srcl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:2152907. Colec12.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3737CytoplasmicSequence analysisAdd
BLAST
Transmembranei38 – 5821Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini59 – 742684ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

  • collagen trimer Source: UniProtKB-KW
  • extracellular exosome Source: MGI
  • integral component of membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 742742Collectin-12PRO_0000318682Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi67 – 671N-linked (GlcNAc...)1 Publication
Glycosylationi159 – 1591N-linked (GlcNAc...)1 Publication
Glycosylationi160 – 1601N-linked (GlcNAc...); atypical1 Publication
Glycosylationi168 – 1681N-linked (GlcNAc...)1 Publication
Glycosylationi271 – 2711N-linked (GlcNAc...)1 Publication
Disulfide bondi607 ↔ 618PROSITE-ProRule annotation1 Publication
Disulfide bondi635 ↔ 730PROSITE-ProRule annotation1 Publication
Disulfide bondi708 ↔ 722PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ8K4Q8.
PaxDbiQ8K4Q8.
PRIDEiQ8K4Q8.

PTM databases

PhosphoSiteiQ8K4Q8.

Expressioni

Tissue specificityi

Expressed in vascular endothelial cells in the heart, in perivascular macrophage and smooth muscle cells. Expressed in plaques-surrounding reactive astrocytes located in cerebral cortex and hippocampus and in leptomeningeal vessels showing characteristics of cerebral amyloid angiopathy (CAA) in a double transgenic mouse model of Alzheimer disease (at protein level). Strongly expressed in lung. Moderately expressed in heart, skeletal muscle, spleen, liver, brain, colon, testis, stomach and kidney. Expressed in neonatal astrocytes. Expressed in reactive astrocytes and vascular/perivascular cells in the brain of a double transgenic mouse model of Alzheimer disease.3 Publications

Developmental stagei

Expressed in embryo at 9 dpc, increases progressively to a peak at 14 dpc and gradually decreases until 19 dpc.1 Publication

Inductioni

Up-regulated in activated microglia and by fibrillar beta amyloid peptide in activated astrocytes.1 Publication

Gene expression databases

BgeeiQ8K4Q8.
CleanExiMM_COLEC12.
GenevisibleiQ8K4Q8. MM.

Interactioni

Subunit structurei

The extracellular domain forms a stable trimer (By similarity). The extracellular domain interacts with fibrillar beta amyloid peptide.By similarity2 Publications

Protein-protein interaction databases

IntActiQ8K4Q8. 1 interaction.
MINTiMINT-4120297.
STRINGi10090.ENSMUSP00000043220.

Structurei

Secondary structure

1
742
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi612 – 6143Combined sources
Beta strandi617 – 6215Combined sources
Helixi628 – 63710Combined sources
Helixi648 – 6569Combined sources
Beta strandi660 – 6623Combined sources
Beta strandi664 – 6696Combined sources
Beta strandi671 – 6733Combined sources
Turni698 – 7025Combined sources
Beta strandi708 – 7114Combined sources
Helixi713 – 7153Combined sources
Beta strandi717 – 7204Combined sources
Beta strandi726 – 7338Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OX9X-ray1.95A/B/C/D603-742[»]
ProteinModelPortaliQ8K4Q8.
SMRiQ8K4Q8. Positions 607-737.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8K4Q8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini452 – 51160Collagen-like 1Add
BLAST
Domaini527 – 58660Collagen-like 2Add
BLAST
Domaini614 – 731118C-type lectinPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili73 – 14270Sequence analysisAdd
BLAST
Coiled coili205 – 25450Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 C-type lectin domain.PROSITE-ProRule annotation
Contains 2 collagen-like domains.Curated

Keywords - Domaini

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

Phylogenomic databases

eggNOGiENOG410IIUI. Eukaryota.
ENOG41101BT. LUCA.
GeneTreeiENSGT00820000126981.
HOGENOMiHOG000111886.
HOVERGENiHBG107745.
InParanoidiQ8K4Q8.
KOiK10062.
OMAiEQQWIKK.
OrthoDBiEOG74XS65.
PhylomeDBiQ8K4Q8.
TreeFamiTF332426.

Family and domain databases

Gene3Di3.10.100.10. 2 hits.
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. 3 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.

Q8K4Q8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKDDFAEEEE VQSFGYKRFG IQEGTQCTKC KNNWALKFSI VLLYILCALL
60 70 80 90 100
TITVAILGYK VVEKMDNVTD GMETSHQTYD NKLTAVESDL KKLGDQAGKK
110 120 130 140 150
ALSTNSELST FRSDILDLRQ QLQEITEKTS KNKDTLEKLQ ANGDSLVDRQ
160 170 180 190 200
SQLKETLQNN SFLITTVNKT LQAYNGYVTN LQQDTSVLQG NLQSQMYSQS
210 220 230 240 250
VVIMNLNNLN LTQVQQRNLI SNLQQSVDDT SLAIQRIKND FQNLQQVFLQ
260 270 280 290 300
AKKDTDWLKE KVQSLQTLAA NNSALAKANN DTLEDMNSQL SSFTGQMDNI
310 320 330 340 350
TTISQANEQS LKDLQDLHKD TENRTAVKFS QLEERFQVFE TDIVNIISNI
360 370 380 390 400
SYTAHHLRTL TSNLNDVRTT CTDTLTRHTD DLTSLNNTLV NIRLDSISLR
410 420 430 440 450
MQQDMMRSKL DTEVANLSVV MEEMKLVDSK HGQLIKNFTI LQGPPGPRGP
460 470 480 490 500
KGDRGSQGPP GPTGNKGQKG EKGEPGPPGP AGERGTIGPV GPPGERGSKG
510 520 530 540 550
SKGSQGPKGS RGSPGKPGPQ GPSGDPGPPG PPGKDGLPGP QGPPGFQGLQ
560 570 580 590 600
GTVGEPGVPG PRGLPGLPGV PGMPGPKGPP GPPGPSGAME PLALQNEPTP
610 620 630 640 650
ASEVNGCPPH WKNFTDKCYY FSLEKEIFED AKLFCEDKSS HLVFINSREE
660 670 680 690 700
QQWIKKHTVG RESHWIGLTD SEQESEWKWL DGSPVDYKNW KAGQPDNWGS
710 720 730 740
GHGPGEDCAG LIYAGQWNDF QCDEINNFIC EKEREAVPSS IL
Length:742
Mass (Da):81,304
Last modified:October 1, 2002 - v1
Checksum:i1537C490E5911C45
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221Q → H in BAB82497 (PubMed:11718900).Curated
Sequence conflicti31 – 311K → I in BAB82497 (PubMed:11718900).Curated
Sequence conflicti69 – 691T → S in BAB82497 (PubMed:11718900).Curated
Sequence conflicti182 – 1821Q → L in BAC31361 (PubMed:16141072).Curated
Sequence conflicti186 – 1861S → N in BAB82497 (PubMed:11718900).Curated
Sequence conflicti368 – 3681R → W in BAB82497 (PubMed:11718900).Curated
Sequence conflicti628 – 6281F → L in BAB82497 (PubMed:11718900).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB038519 mRNA. Translation: BAB82497.1.
AB078434 mRNA. Translation: BAC05523.1.
AK042772 mRNA. Translation: BAC31361.1.
AK158366 mRNA. Translation: BAE34474.1.
BC057936 mRNA. Translation: AAH57936.1.
CCDSiCCDS37732.1.
RefSeqiNP_569716.2. NM_130449.2.
UniGeneiMm.218571.

Genome annotation databases

EnsembliENSMUST00000040069; ENSMUSP00000043220; ENSMUSG00000036103.
GeneIDi140792.
KEGGimmu:140792.
UCSCiuc008eak.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB038519 mRNA. Translation: BAB82497.1.
AB078434 mRNA. Translation: BAC05523.1.
AK042772 mRNA. Translation: BAC31361.1.
AK158366 mRNA. Translation: BAE34474.1.
BC057936 mRNA. Translation: AAH57936.1.
CCDSiCCDS37732.1.
RefSeqiNP_569716.2. NM_130449.2.
UniGeneiMm.218571.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OX9X-ray1.95A/B/C/D603-742[»]
ProteinModelPortaliQ8K4Q8.
SMRiQ8K4Q8. Positions 607-737.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8K4Q8. 1 interaction.
MINTiMINT-4120297.
STRINGi10090.ENSMUSP00000043220.

PTM databases

PhosphoSiteiQ8K4Q8.

Proteomic databases

MaxQBiQ8K4Q8.
PaxDbiQ8K4Q8.
PRIDEiQ8K4Q8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000040069; ENSMUSP00000043220; ENSMUSG00000036103.
GeneIDi140792.
KEGGimmu:140792.
UCSCiuc008eak.2. mouse.

Organism-specific databases

CTDi81035.
MGIiMGI:2152907. Colec12.

Phylogenomic databases

eggNOGiENOG410IIUI. Eukaryota.
ENOG41101BT. LUCA.
GeneTreeiENSGT00820000126981.
HOGENOMiHOG000111886.
HOVERGENiHBG107745.
InParanoidiQ8K4Q8.
KOiK10062.
OMAiEQQWIKK.
OrthoDBiEOG74XS65.
PhylomeDBiQ8K4Q8.
TreeFamiTF332426.

Enzyme and pathway databases

ReactomeiR-MMU-3000480. Scavenging by Class A Receptors.

Miscellaneous databases

ChiTaRSiColec12. mouse.
EvolutionaryTraceiQ8K4Q8.
NextBioi369985.
PROiQ8K4Q8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K4Q8.
CleanExiMM_COLEC12.
GenevisibleiQ8K4Q8. MM.

Family and domain databases

Gene3Di3.10.100.10. 2 hits.
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. 3 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a mouse scavenger receptor with C-type lectin (SRCL), a novel member of the scavenger receptor family."
    Nakamura K., Funakoshi H., Tokunaga F., Nakamura T.
    Biochim. Biophys. Acta 1522:53-58(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
    Tissue: Embryo.
  2. "cDNA cloning of mouse CL-P1 gene."
    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.
    Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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/6J.
    Tissue: Cerebellum and Inner ear.
  4. "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: NMRI.
    Tissue: Mammary tumor.
  5. "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: TISSUE SPECIFICITY.
  6. "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, INDUCTION, TISSUE SPECIFICITY.
  7. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
    Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
    Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-67; ASN-159; ASN-160; ASN-168 AND ASN-271.
    Tissue: Myoblast.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Lung.
  9. "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 (1.95 ANGSTROMS) OF 603-742 IN COMPLEX WITH GLYCAN LEWIS X AND CALCIUM IONS, DISULFIDE BONDS.

Entry informationi

Entry nameiCOL12_MOUSE
AccessioniPrimary (citable) accession number: Q8K4Q8
Secondary accession number(s): Q3TYT8, Q8C979, Q8VIF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 1, 2002
Last modified: December 9, 2015
This is version 118 of the entry and version 1 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

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.