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Q8IZD4

- DCP1B_HUMAN

UniProt

Q8IZD4 - DCP1B_HUMAN

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Protein

mRNA-decapping enzyme 1B

Gene
DCP1B
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May play a role in the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. May remove the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP By similarity.

GO - Molecular functioni

  1. hydrolase activity Source: UniProtKB-KW
  2. protein binding Source: IntAct

GO - Biological processi

  1. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Reactome
  2. gene expression Source: Reactome
  3. mRNA metabolic process Source: Reactome
  4. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  5. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB-KW
  6. RNA metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nonsense-mediated mRNA decay

Enzyme and pathway databases

ReactomeiREACT_20518. mRNA decay by 5' to 3' exoribonuclease.

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA-decapping enzyme 1B (EC:3.-.-.-)
Gene namesi
Name:DCP1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:24451. DCP1B.

Subcellular locationi

Cytoplasm. Nucleus By similarity 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. intracellular membrane-bounded organelle Source: HPA
  4. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134889143.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 617616mRNA-decapping enzyme 1BPRO_0000402799Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei191 – 1911Phosphotyrosine1 Publication
Modified residuei448 – 4481Phosphoserine1 Publication
Modified residuei511 – 5111Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8IZD4.
PaxDbiQ8IZD4.
PRIDEiQ8IZD4.

PTM databases

PhosphoSiteiQ8IZD4.

Expressioni

Gene expression databases

ArrayExpressiQ8IZD4.
BgeeiQ8IZD4.
CleanExiHS_DCP1B.
GenevestigatoriQ8IZD4.

Organism-specific databases

HPAiHPA039709.

Interactioni

Subunit structurei

Binds DCP1A. Part of a complex containing enzymes involved in mRNA decay, including DCP2, LSM1, LSM3 and CNOT6.

Binary interactionsi

WithEntry#Exp.IntActNotes
DCP2Q8IU603EBI-521595,EBI-521577

Protein-protein interaction databases

BioGridi128216. 16 interactions.
DIPiDIP-31289N.
IntActiQ8IZD4. 8 interactions.
MINTiMINT-1190113.
STRINGi9606.ENSP00000280665.

Structurei

3D structure databases

ProteinModelPortaliQ8IZD4.
SMRiQ8IZD4. Positions 13-134, 573-606.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi252 – 26110Poly-Gln

Sequence similaritiesi

Belongs to the DCP1 family.

Phylogenomic databases

eggNOGiNOG314415.
HOGENOMiHOG000090228.
HOVERGENiHBG103159.
InParanoidiQ8IZD4.
KOiK12611.
OMAiDEYTKCK.
OrthoDBiEOG75QR3K.
PhylomeDBiQ8IZD4.
TreeFamiTF320504.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR010334. DCP1.
IPR011993. PH_like_dom.
[Graphical view]
PANTHERiPTHR16290. PTHR16290. 1 hit.
PfamiPF06058. DCP1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8IZD4-1 [UniParc]FASTAAdd to Basket

« Hide

MAAVAAGGLV GKGRDISLAA LQRHDPYINR IVDVASQVAL YTFGHRANEW    50
EKTDVEGTLF VYTRSASPKH GFTIMNRLSM ENRTEPITKD LDFQLQDPFL 100
LYRNARLSIY GIWFYDKEEC QRIAELMKNL TQYEQLKAHQ GTGAGISPVI 150
LNSGEGKEVD ILRMLIKAKD EYTKCKTCSE PKKITSSSAI YDNPNLIKPI 200
PVKPSENQQQ RIPQPNQTLD PEPQHLSLTA LFGKQDKATC QETVEPPQTL 250
HQQQQQQQQQ QEKLPIRQGV VRSLSYEEPR RHSPPIEKQL CPAIQKLMVR 300
SADLHPLSEL PENRPCENGS THSAGEFFTG PVQPGSPHNI GTSRGVQNAS 350
RTQNLFEKLQ STPGAANKCD PSTPAPASSA ALNRSRAPTS VTPVAPGKGL 400
AQPPQAYFNG SLPPQTVGHQ AHGREQSTLP RQTLPISGSQ TGSSGVISPQ 450
ELLKKLQIVQ QEQQLHASNR PALAAKFPVL AQSSGTGKPL ESWINKTPNT 500
EQQTPLFQVI SPQRIPATAA PSLLMSPMVF AQPTSVPPKE RESGLLPVGG 550
QEPPAAATSL LLPIQSPEPS VITSSPLTKL QLQEALLYLI QNDDNFLNII 600
YEAYLFSMTQ AAMKKTM 617
Length:617
Mass (Da):67,723
Last modified:January 11, 2011 - v2
Checksum:i00B9D9592BAC3B64
GO

Sequence cautioni

The sequence AAH15368.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti195 – 1951N → D.
Corresponds to variant rs12423058 [ dbSNP | Ensembl ].
VAR_047395
Natural varianti216 – 2161N → S.
Corresponds to variant rs34730825 [ dbSNP | Ensembl ].
VAR_047396
Natural varianti301 – 3011S → T.
Corresponds to variant rs2470449 [ dbSNP | Ensembl ].
VAR_047397
Natural varianti344 – 3441R → H.
Corresponds to variant rs715146 [ dbSNP | Ensembl ].
VAR_047398

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511H → HQ in AAN62764. 1 Publication
Sequence conflicti251 – 2511H → HQ in BAB71118. 1 Publication
Sequence conflicti251 – 2511H → HQ in AAH15368. 1 Publication
Sequence conflicti251 – 2511H → HQ in AAH43437. 1 Publication
Sequence conflicti426 – 4261Q → R in BAB71118. 1 Publication
Sequence conflicti435 – 4351P → A in AAH43437. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY146652 mRNA. Translation: AAN62764.1.
AK056200 mRNA. Translation: BAB71118.1.
AC005342 Genomic DNA. No translation available.
BC015368 mRNA. Translation: AAH15368.2. Different initiation.
BC043437 mRNA. Translation: AAH43437.1.
CCDSiCCDS31727.1.
RefSeqiNP_689853.3. NM_152640.3.
XP_006719034.1. XM_006718971.1.
UniGeneiHs.130934.

Genome annotation databases

EnsembliENST00000280665; ENSP00000280665; ENSG00000151065.
GeneIDi196513.
KEGGihsa:196513.
UCSCiuc001qjx.1. human.

Polymorphism databases

DMDMi317373353.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY146652 mRNA. Translation: AAN62764.1 .
AK056200 mRNA. Translation: BAB71118.1 .
AC005342 Genomic DNA. No translation available.
BC015368 mRNA. Translation: AAH15368.2 . Different initiation.
BC043437 mRNA. Translation: AAH43437.1 .
CCDSi CCDS31727.1.
RefSeqi NP_689853.3. NM_152640.3.
XP_006719034.1. XM_006718971.1.
UniGenei Hs.130934.

3D structure databases

ProteinModelPortali Q8IZD4.
SMRi Q8IZD4. Positions 13-134, 573-606.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 128216. 16 interactions.
DIPi DIP-31289N.
IntActi Q8IZD4. 8 interactions.
MINTi MINT-1190113.
STRINGi 9606.ENSP00000280665.

PTM databases

PhosphoSitei Q8IZD4.

Polymorphism databases

DMDMi 317373353.

Proteomic databases

MaxQBi Q8IZD4.
PaxDbi Q8IZD4.
PRIDEi Q8IZD4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000280665 ; ENSP00000280665 ; ENSG00000151065 .
GeneIDi 196513.
KEGGi hsa:196513.
UCSCi uc001qjx.1. human.

Organism-specific databases

CTDi 196513.
GeneCardsi GC12M002055.
H-InvDB HIX0201841.
HGNCi HGNC:24451. DCP1B.
HPAi HPA039709.
MIMi 609843. gene.
neXtProti NX_Q8IZD4.
PharmGKBi PA134889143.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG314415.
HOGENOMi HOG000090228.
HOVERGENi HBG103159.
InParanoidi Q8IZD4.
KOi K12611.
OMAi DEYTKCK.
OrthoDBi EOG75QR3K.
PhylomeDBi Q8IZD4.
TreeFami TF320504.

Enzyme and pathway databases

Reactomei REACT_20518. mRNA decay by 5' to 3' exoribonuclease.

Miscellaneous databases

GeneWikii DCP1B.
GenomeRNAii 196513.
NextBioi 89512.
PROi Q8IZD4.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8IZD4.
Bgeei Q8IZD4.
CleanExi HS_DCP1B.
Genevestigatori Q8IZD4.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR010334. DCP1.
IPR011993. PH_like_dom.
[Graphical view ]
PANTHERi PTHR16290. PTHR16290. 1 hit.
Pfami PF06058. DCP1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay."
    Lykke-Andersen J.
    Mol. Cell. Biol. 22:8114-8121(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH DCP1A.
  2. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Teratocarcinoma.
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: Testis and Uterus.
  5. "Cytoplasmic foci are sites of mRNA decay in human cells."
    Cougot N., Babajko S., Seraphin B.
    J. Cell Biol. 165:31-40(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH DCP1A.
  6. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-191, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448 AND SER-511, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDCP1B_HUMAN
AccessioniPrimary (citable) accession number: Q8IZD4
Secondary accession number(s): Q86XH9, Q96BP8, Q96MZ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: January 11, 2011
Last modified: September 3, 2014
This is version 103 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

Complete proteome, 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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