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Protein

Carboxypeptidase M

Gene

CPM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. It is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins.1 Publication

Catalytic activityi

Cleavage of C-terminal arginine or lysine residues from polypeptides.

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Enzyme regulationi

Inhibited by O-phenanthroline and MGTA and activated by cobalt.

Kineticsi

  1. KM=59 µM for synthetic dansyl-Ala-Arg1 Publication
  2. KM=57 µM for placental peptide hormones1 Publication

pH dependencei

Optimum pH is 7.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi83 – 831Zinc
Metal bindingi86 – 861Zinc
Metal bindingi190 – 1901Zinc
Sitei277 – 2771Probable structural role
Active sitei281 – 2811Nucleophile

GO - Molecular functioni

  1. carboxypeptidase activity Source: ProtInc
  2. metallocarboxypeptidase activity Source: ProtInc
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. anatomical structure morphogenesis Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.17.12. 2681.
SABIO-RKP14384.

Protein family/group databases

MEROPSiM14.006.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase M (EC:3.4.17.12)
Short name:
CPM
Gene namesi
Name:CPM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:2311. CPM.

Subcellular locationi

Cell membrane 1 Publication; Lipid-anchorGPI-anchor 1 Publication

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. cell surface Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  4. plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi277 – 2771E → A: 5-fold decrease in substrate affinity. 22-fold decrease in specific affinity. 104-fold decrease in catalytic efficiency. Greatly reduced heat stability. 1 Publication
Mutagenesisi277 – 2771E → Q: 2-fold decrease in substrate affinity. Small increase in specific affinity. Reduced heat stability by 50%. 1 Publication
Mutagenesisi281 – 2811E → Q: Abolishes enzyme activity. 1 Publication
Mutagenesisi423 – 4231S → A or T: Expressed on cell membrane. Released from membrane by PI-PLC. 1 Publication
Mutagenesisi423 – 4231S → P: Little expression on cell membrane. Perinuclear localization. Not released from membrane by PI-PLC. 1 Publication

Organism-specific databases

PharmGKBiPA26828.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17172 PublicationsAdd
BLAST
Chaini18 – 423406Carboxypeptidase MPRO_0000004391Add
BLAST
Propeptidei424 – 44320Removed in mature formCuratedPRO_0000251910Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi38 – 381N-linked (GlcNAc...)1 Publication
Glycosylationi115 – 1151N-linked (GlcNAc...)2 Publications
Disulfide bondi138 ↔ 2851 Publication
Glycosylationi164 – 1641N-linked (GlcNAc...)1 Publication
Disulfide bondi242 ↔ 2841 Publication
Disulfide bondi341 ↔ 4101 Publication
Glycosylationi363 – 3631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi384 – 3841N-linked (GlcNAc...)Sequence Analysis
Lipidationi423 – 4231GPI-anchor amidated serine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiP14384.
PaxDbiP14384.
PRIDEiP14384.

PTM databases

PhosphoSiteiP14384.

Expressioni

Gene expression databases

BgeeiP14384.
CleanExiHS_CPM.
ExpressionAtlasiP14384. baseline and differential.
GenevestigatoriP14384.

Organism-specific databases

HPAiHPA002657.

Interactioni

Protein-protein interaction databases

BioGridi107760. 2 interactions.
IntActiP14384. 3 interactions.
STRINGi9606.ENSP00000339157.

Structurei

Secondary structure

1
443
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 3814Combined sources
Turni39 – 413Combined sources
Beta strandi42 – 509Combined sources
Beta strandi56 – 6510Combined sources
Beta strandi75 – 806Combined sources
Helixi88 – 10316Combined sources
Turni104 – 1063Combined sources
Helixi108 – 1169Combined sources
Beta strandi118 – 1236Combined sources
Helixi127 – 1326Combined sources
Beta strandi159 – 1613Combined sources
Helixi169 – 18012Combined sources
Beta strandi183 – 1853Combined sources
Beta strandi188 – 1903Combined sources
Beta strandi192 – 1998Combined sources
Helixi205 – 2073Combined sources
Helixi209 – 2113Combined sources
Helixi219 – 23113Combined sources
Turni234 – 2385Combined sources
Beta strandi243 – 2453Combined sources
Beta strandi252 – 2554Combined sources
Turni256 – 2583Combined sources
Helixi265 – 2717Combined sources
Beta strandi279 – 2879Combined sources
Helixi290 – 2923Combined sources
Helixi293 – 2986Combined sources
Helixi301 – 3088Combined sources
Helixi309 – 3124Combined sources
Beta strandi314 – 3207Combined sources
Beta strandi331 – 3344Combined sources
Beta strandi350 – 3534Combined sources
Beta strandi357 – 3659Combined sources
Beta strandi367 – 3693Combined sources
Beta strandi372 – 3787Combined sources
Beta strandi383 – 3864Combined sources
Turni415 – 4184Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UWYX-ray3.00A18-443[»]
ProteinModelPortaliP14384.
SMRiP14384. Positions 18-419.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14384.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M14 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2866.
GeneTreeiENSGT00760000119124.
HOGENOMiHOG000232185.
HOVERGENiHBG003410.
InParanoidiP14384.
KOiK01296.
OMAiMNFPNGI.
PhylomeDBiP14384.
TreeFamiTF315592.

Family and domain databases

Gene3Di2.60.40.1120. 1 hit.
InterProiIPR008969. CarboxyPept-like_regulatory.
IPR014766. CarboxyPept_regulatory_dom.
IPR027062. CPM.
IPR000834. Peptidase_M14.
[Graphical view]
PANTHERiPTHR11532:SF53. PTHR11532:SF53. 1 hit.
PfamiPF00246. Peptidase_M14. 1 hit.
[Graphical view]
PRINTSiPR00765. CRBOXYPTASEA.
SMARTiSM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMiSSF49464. SSF49464. 1 hit.
PROSITEiPS00132. CARBOXYPEPT_ZN_1. 1 hit.
PS00133. CARBOXYPEPT_ZN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P14384-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDFPCLWLGL LLPLVAALDF NYHRQEGMEA FLKTVAQNYS SVTHLHSIGK
60 70 80 90 100
SVKGRNLWVL VVGRFPKEHR IGIPEFKYVA NMHGDETVGR ELLLHLIDYL
110 120 130 140 150
VTSDGKDPEI TNLINSTRIH IMPSMNPDGF EAVKKPDCYY SIGRENYNQY
160 170 180 190 200
DLNRNFPDAF EYNNVSRQPE TVAVMKWLKT ETFVLSANLH GGALVASYPF
210 220 230 240 250
DNGVQATGAL YSRSLTPDDD VFQYLAHTYA SRNPNMKKGD ECKNKMNFPN
260 270 280 290 300
GVTNGYSWYP LQGGMQDYNY IWAQCFEITL ELSCCKYPRE EKLPSFWNNN
310 320 330 340 350
KASLIEYIKQ VHLGVKGQVF DQNGNPLPNV IVEVQDRKHI CPYRTNKYGE
360 370 380 390 400
YYLLLLPGSY IINVTVPGHD PHITKVIIPE KSQNFSALKK DILLPFQGQL
410 420 430 440
DSIPVSNPSC PMIPLYRNLP DHSAATKPSL FLFLVSLLHI FFK
Length:443
Mass (Da):50,514
Last modified:July 10, 2001 - v2
Checksum:i98EB0C94E201B901
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti24 – 241R → H.
Corresponds to variant rs7978197 [ dbSNP | Ensembl ].
VAR_048600
Natural varianti133 – 1331V → I.
Corresponds to variant rs7309831 [ dbSNP | Ensembl ].
VAR_048601

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04970 mRNA. Translation: AAA35651.2.
AF262947
, AF262940, AF262941, AF262942, AF262943, AF262944, AF262945, AF262946 Genomic DNA. Translation: AAG47641.1.
AF368463 mRNA. Translation: AAK69717.1.
AK313180 mRNA. Translation: BAG35997.1.
BC022276 mRNA. Translation: AAH22276.1.
CCDSiCCDS8987.1.
PIRiA32619.
RefSeqiNP_001005502.1. NM_001005502.2.
NP_001865.1. NM_001874.4.
NP_938079.1. NM_198320.3.
UniGeneiHs.654387.

Genome annotation databases

EnsembliENST00000338356; ENSP00000339157; ENSG00000135678.
ENST00000546373; ENSP00000447255; ENSG00000135678.
ENST00000551568; ENSP00000448517; ENSG00000135678.
GeneIDi1368.
KEGGihsa:1368.
UCSCiuc001sup.3. human.

Polymorphism databases

DMDMi14916957.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04970 mRNA. Translation: AAA35651.2.
AF262947
, AF262940, AF262941, AF262942, AF262943, AF262944, AF262945, AF262946 Genomic DNA. Translation: AAG47641.1.
AF368463 mRNA. Translation: AAK69717.1.
AK313180 mRNA. Translation: BAG35997.1.
BC022276 mRNA. Translation: AAH22276.1.
CCDSiCCDS8987.1.
PIRiA32619.
RefSeqiNP_001005502.1. NM_001005502.2.
NP_001865.1. NM_001874.4.
NP_938079.1. NM_198320.3.
UniGeneiHs.654387.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UWYX-ray3.00A18-443[»]
ProteinModelPortaliP14384.
SMRiP14384. Positions 18-419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107760. 2 interactions.
IntActiP14384. 3 interactions.
STRINGi9606.ENSP00000339157.

Chemistry

BindingDBiP14384.
ChEMBLiCHEMBL3038.

Protein family/group databases

MEROPSiM14.006.

PTM databases

PhosphoSiteiP14384.

Polymorphism databases

DMDMi14916957.

Proteomic databases

MaxQBiP14384.
PaxDbiP14384.
PRIDEiP14384.

Protocols and materials databases

DNASUi1368.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000338356; ENSP00000339157; ENSG00000135678.
ENST00000546373; ENSP00000447255; ENSG00000135678.
ENST00000551568; ENSP00000448517; ENSG00000135678.
GeneIDi1368.
KEGGihsa:1368.
UCSCiuc001sup.3. human.

Organism-specific databases

CTDi1368.
GeneCardsiGC12M069244.
HGNCiHGNC:2311. CPM.
HPAiHPA002657.
MIMi114860. gene.
neXtProtiNX_P14384.
PharmGKBiPA26828.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2866.
GeneTreeiENSGT00760000119124.
HOGENOMiHOG000232185.
HOVERGENiHBG003410.
InParanoidiP14384.
KOiK01296.
OMAiMNFPNGI.
PhylomeDBiP14384.
TreeFamiTF315592.

Enzyme and pathway databases

BRENDAi3.4.17.12. 2681.
SABIO-RKP14384.

Miscellaneous databases

ChiTaRSiCPM. human.
EvolutionaryTraceiP14384.
GeneWikiiCPM_(gene).
GenomeRNAii1368.
NextBioi5541.
PROiP14384.
SOURCEiSearch...

Gene expression databases

BgeeiP14384.
CleanExiHS_CPM.
ExpressionAtlasiP14384. baseline and differential.
GenevestigatoriP14384.

Family and domain databases

Gene3Di2.60.40.1120. 1 hit.
InterProiIPR008969. CarboxyPept-like_regulatory.
IPR014766. CarboxyPept_regulatory_dom.
IPR027062. CPM.
IPR000834. Peptidase_M14.
[Graphical view]
PANTHERiPTHR11532:SF53. PTHR11532:SF53. 1 hit.
PfamiPF00246. Peptidase_M14. 1 hit.
[Graphical view]
PRINTSiPR00765. CRBOXYPTASEA.
SMARTiSM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMiSSF49464. SSF49464. 1 hit.
PROSITEiPS00132. CARBOXYPEPT_ZN_1. 1 hit.
PS00133. CARBOXYPEPT_ZN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and sequencing of the cDNA for human membrane-bound carboxypeptidase M. Comparison with carboxypeptidases A, B, H, and N."
    Tan F., Chan S.J., Steiner D.F., Schilling J.W., Skidgel R.A.
    J. Biol. Chem. 264:13165-13170(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-48.
    Tissue: Placenta.
  2. Skidgel R.A.
    Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Type 2 diabetes locus on 12q15: further mapping and mutation screening of two candidate genes."
    Bektas A., Hughes J.N., Warram J.H., Krolewski A.S., Doria A.
    Diabetes 50:204-208(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Molecular structure and alternative splicing of the human carboxypeptidase M gene."
    Pessoa L.G., Guerreiro da S.I., Baptista H.A., Pesquero J.L., Paiva A.C.M., Bader M., Pesquero J.B.
    Biol. Chem. 383:263-269(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  6. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  7. "Effect of mutation of two critical glutamic acid residues on the activity and stability of human carboxypeptidase M and characterization of its signal for glycosylphosphatidylinositol anchoring."
    Tan F., Balsitis S., Black J.K., Bloechl A., Mao J.-F., Becker R.P., Schacht D., Skidgel R.A.
    Biochem. J. 370:567-578(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 18-21, GPI-ANCHOR AT SER-423, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF GLU-277; GLU-281 AND SER-423.
  8. "Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins."
    Elortza F., Nuehse T.S., Foster L.J., Stensballe A., Peck S.C., Jensen O.N.
    Mol. Cell. Proteomics 2:1261-1270(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment."
    Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S., Brodbeck U., Peck S.C., Jensen O.N.
    J. Proteome Res. 5:935-943(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-115 AND ASN-164.
    Tissue: Liver.
  11. "Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity."
    Reverter D., Maskos K., Tan F., Skidgel R.A., Bode W.
    J. Mol. Biol. 338:257-269(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 18-443, DISULFIDE BONDS, GLYCOSYLATION AT ASN-38 AND ASN-115.

Entry informationi

Entry nameiCBPM_HUMAN
AccessioniPrimary (citable) accession number: P14384
Secondary accession number(s): B2R800, Q9H2K9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 31, 1989
Last sequence update: July 10, 2001
Last modified: March 31, 2015
This is version 154 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.