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Q64010

- CRK_MOUSE

UniProt

Q64010 - CRK_MOUSE

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Protein
Adapter molecule crk
Gene
Crk, Crko
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk-I. Crk-II mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4. May regulate the EFNA5-EPHA3 signaling.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei237 – 2371Proline switch By similarity

GO - Molecular functioni

  1. SH3/SH2 adaptor activity Source: BHF-UCL
  2. ephrin receptor binding Source: UniProtKB
  3. protein binding Source: IntAct
  4. protein phosphorylated amino acid binding Source: MGI

GO - Biological processi

  1. ephrin receptor signaling pathway Source: UniProtKB
  2. positive regulation of signal transduction Source: GOC
  3. regulation of Rac protein signal transduction Source: Ensembl
  4. regulation of Rho GTPase activity Source: UniProtKB
  5. regulation of actin cytoskeleton organization Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_198374. Regulation of actin dynamics for phagocytic cup formation.
REACT_198634. Regulation of signaling by CBL.

Names & Taxonomyi

Protein namesi
Recommended name:
Adapter molecule crk
Alternative name(s):
Proto-oncogene c-Crk
p38
Gene namesi
Name:Crk
Synonyms:Crko
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:88508. Crk.

Subcellular locationi

Cytoplasm By similarity. Cell membrane By similarity
Note: Translocated to the plasma membrane upon cell adhesion By similarity.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 304303Adapter molecule crk
PRO_0000079352Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei41 – 411Phosphoserine By similarity
Modified residuei74 – 741Phosphoserine By similarity
Modified residuei83 – 831Phosphoserine By similarity
Modified residuei221 – 2211Phosphotyrosine; by ABL11 Publication
Modified residuei239 – 2391Phosphotyrosine By similarity

Post-translational modificationi

Isoform Crk-II is phosphorylated by KIT. Phosphorylated on Tyr-221 upon cell adhesion. Results in the negative regulation of the association with SH2- and SH3-binding partners, possibly by the formation of an intramolecular interaction of phosphorylated Tyr-221 with the SH2 domain. This leads finally to the down-regulation of the Crk signaling pathway.2 Publications
Proline isomerization at Pro-237 by PPIA acts as a switch between two conformations: an autoinhibitory conformation in the cis form, where the tandem SH3 domains interact intramolecularly, and an activated conformation in the trans form By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ64010.
PaxDbiQ64010.
PRIDEiQ64010.

PTM databases

PhosphoSiteiQ64010.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

ArrayExpressiQ64010.
BgeeiQ64010.
CleanExiMM_CRK.
GenevestigatoriQ64010.

Interactioni

Subunit structurei

Interacts with ABL1, C3G, DOCK3, MAP4K1, MAPK8 and SOS via its first SH3 domain. Interacts (via SH2 domain) with BCAR1, CBL, CBLB, PXN, IRS4 and GAB1 upon stimulus-induced tyrosine phosphorylation. Interacts (via SH2 domain) with several tyrosine-phosphorylated growth factor receptors such as EGFR and INSR. Interacts with FLT1 (tyrosine-phosphorylated). Interacts with DOCK1 and DOCK4. Interacts with SHB. Interacts with PEAK1. Interacts with FASLG. Isoform Crk-II interacts with KIT. Interacts with EPHA3; upon activation of EPHA3 by the ligand EFNA5 and EPHA3 tyrosine kinase activity-dependent. Interacts with EPHA3 (phosphorylated); mediates EFNA5-EPHA3 signaling through RHOA GTPase activation. Interacts with FLT4 (tyrosine-phosphorylated). Isoform Crk-II (via SH2 domain) interacts with PDGFRA (tyrosine phosphorylated) and PDGFRB (tyrosine phosphorylated). Part of a collagen stimulated complex involved in cell migration composed of CDC42, CRK, TNK2 and p130cas/BCAR1. Interacts (via SH2 domain) with the 'Tyr-9' phosphorylated form of PDPK1. Interacts with CBLC.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
IGF1RP080693EBI-2906540,EBI-475981From a different organism.

Protein-protein interaction databases

BioGridi198887. 25 interactions.
DIPiDIP-57059N.
IntActiQ64010. 22 interactions.
MINTiMINT-4599411.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi136 – 1416
Beta strandi147 – 1504
Beta strandi158 – 1636
Beta strandi165 – 1739
Beta strandi179 – 1835
Helixi184 – 1863
Beta strandi187 – 1893
Beta strandi238 – 2447
Beta strandi252 – 2543
Beta strandi262 – 2687
Beta strandi271 – 2733
Beta strandi275 – 2795
Beta strandi282 – 2865
Helixi288 – 2903
Beta strandi291 – 2944

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B07X-ray2.50A134-190[»]
1CKAX-ray1.50A134-190[»]
1CKBX-ray1.90A134-190[»]
1JU5NMR-B217-228[»]
1M30NMR-A134-191[»]
1M3ANMR-A135-191[»]
1M3BNMR-A134-191[»]
1M3CNMR-A132-191[»]
2GGRNMR-A230-304[»]
ProteinModelPortaliQ64010.
SMRiQ64010. Positions 1-304.

Miscellaneous databases

EvolutionaryTraceiQ64010.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 118106SH2
Add
BLAST
Domaini132 – 19261SH3 1
Add
BLAST
Domaini237 – 29660SH3 2
Add
BLAST

Domaini

The C-terminal SH3 domain function as a negative modulator for transformation and the N-terminal SH3 domain appears to function as a positive regulator for transformation By similarity.
The SH2 domain mediates interaction with tyrosine phosphorylated proteins. Mediates interaction with SHB.

Sequence similaritiesi

Belongs to the CRK family.
Contains 1 SH2 domain.
Contains 2 SH3 domains.

Keywords - Domaini

Repeat, SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiNOG292767.
GeneTreeiENSGT00390000001475.
HOGENOMiHOG000236288.
HOVERGENiHBG105616.
InParanoidiQ64010.
KOiK04438.
OMAiVIYERRF.
OrthoDBiEOG7NW69P.
PhylomeDBiQ64010.
TreeFamiTF321436.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR000980. SH2.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 3 hits.
SSF55550. SSF55550. 2 hits.
PROSITEiPS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Crk-II (identifier: Q64010-1) [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

MAGNFDSEER SSWYWGRLSR QEAVALLQGQ RHGVFLVRDS STSPGDYVLS    50
VSENSRVSHY IINSSGPRPP VPPSPAQPPP GVSPSRLRIG DQEFDSLPAL 100
LEFYKIHYLD TTTLIEPVAR SRQGSGVILR QEEAEYVRAL FDFNGNDEED 150
LPFKKGDILR IRDKPEEQWW NAEDSEGKRG MIPVPYVEKY RPASASVSAL 200
IGGNQEGSHP QPLGGPEPGP YAQPSVNTPL PNLQNGPIYA RVIQKRVPNA 250
YDKTALALEV GELVKVTKIN VSGQWEGECN GKRGHFPFTH VRLLDQQNPD 300
EDFS 304
Length:304
Mass (Da):33,815
Last modified:November 1, 1996 - v1
Checksum:i5491896FC7A89065
GO
Isoform Crk-I (identifier: Q64010-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     205-304: Missing.

Show »
Length:204
Mass (Da):22,847
Checksum:i35B7AC1188657461
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei205 – 304100Missing in isoform Crk-I.
VSP_004174Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S72408 mRNA. Translation: AAB30755.1.
AK028488 mRNA. Translation: BAC25976.1.
CCDSiCCDS25055.1. [Q64010-1]
RefSeqiNP_598417.2. NM_133656.5. [Q64010-1]
UniGeneiMm.280125.

Genome annotation databases

EnsembliENSMUST00000017920; ENSMUSP00000017920; ENSMUSG00000017776. [Q64010-1]
GeneIDi12928.
KEGGimmu:12928.
UCSCiuc007keq.1. mouse. [Q64010-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S72408 mRNA. Translation: AAB30755.1 .
AK028488 mRNA. Translation: BAC25976.1 .
CCDSi CCDS25055.1. [Q64010-1 ]
RefSeqi NP_598417.2. NM_133656.5. [Q64010-1 ]
UniGenei Mm.280125.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B07 X-ray 2.50 A 134-190 [» ]
1CKA X-ray 1.50 A 134-190 [» ]
1CKB X-ray 1.90 A 134-190 [» ]
1JU5 NMR - B 217-228 [» ]
1M30 NMR - A 134-191 [» ]
1M3A NMR - A 135-191 [» ]
1M3B NMR - A 134-191 [» ]
1M3C NMR - A 132-191 [» ]
2GGR NMR - A 230-304 [» ]
ProteinModelPortali Q64010.
SMRi Q64010. Positions 1-304.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198887. 25 interactions.
DIPi DIP-57059N.
IntActi Q64010. 22 interactions.
MINTi MINT-4599411.

PTM databases

PhosphoSitei Q64010.

Proteomic databases

MaxQBi Q64010.
PaxDbi Q64010.
PRIDEi Q64010.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000017920 ; ENSMUSP00000017920 ; ENSMUSG00000017776 . [Q64010-1 ]
GeneIDi 12928.
KEGGi mmu:12928.
UCSCi uc007keq.1. mouse. [Q64010-1 ]

Organism-specific databases

CTDi 1398.
MGIi MGI:88508. Crk.

Phylogenomic databases

eggNOGi NOG292767.
GeneTreei ENSGT00390000001475.
HOGENOMi HOG000236288.
HOVERGENi HBG105616.
InParanoidi Q64010.
KOi K04438.
OMAi VIYERRF.
OrthoDBi EOG7NW69P.
PhylomeDBi Q64010.
TreeFami TF321436.

Enzyme and pathway databases

Reactomei REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
REACT_198634. Regulation of signaling by CBL.

Miscellaneous databases

EvolutionaryTracei Q64010.
NextBioi 282592.
PROi Q64010.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q64010.
Bgeei Q64010.
CleanExi MM_CRK.
Genevestigatori Q64010.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR000980. SH2.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTi SM00252. SH2. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 3 hits.
SSF55550. SSF55550. 2 hits.
PROSITEi PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The C-terminal SH3 domain of the mouse c-Crk protein negatively regulates tyrosine-phosphorylation of Crk associated p130 in rat 3Y1 cells."
    Ogawa S., Toyoshima H., Kozutsumi H., Hagiwara K., Sakai R., Tanaka T., Hirano N., Mano H., Yazaki Y., Hirai H.
    Oncogene 9:1669-1678(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CRK-I AND CRK-II).
    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 CRK-II).
    Strain: C57BL/6J.
    Tissue: Skin.
  3. "c-Abl kinase regulates the protein binding activity of c-Crk."
    Feller S.M., Knudsen B., Hanafusa H.
    EMBO J. 13:2341-2351(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-221, INTERACTION WITH ABL1.
  4. "An eps homology (EH) domain protein that binds to the ral-GTPase target, RalBP1."
    Yamaguchi A., Urano T., Goi T., Feig L.A.
    J. Biol. Chem. 272:31230-31234(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH REPS1.
    Tissue: Muscle.
  5. "Identification of vascular endothelial growth factor receptor-1 tyrosine phosphorylation sites and binding of SH2 domain-containing molecules."
    Ito N., Wernstedt C., Engstrom U., Claesson-Welsh L.
    J. Biol. Chem. 273:23410-23418(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FLT1.
  6. "ASAP1, a phospholipid-dependent arf GTPase-activating protein that associates with and is phosphorylated by Src."
    Brown M.T., Andrade J., Radhakrishna H., Donaldson J.G., Cooper J.A., Randazzo P.A.
    Mol. Cell. Biol. 18:7038-7051(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDEF1/ASAP1.
  7. "Isolation and characterization of novel presenilin binding protein."
    Kashiwa A., Yoshida H., Lee S., Paladino T., Liu Y., Chen Q., Dargusch R., Schubert D., Kimura H.
    J. Neurochem. 75:109-116(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DOCK3.
    Tissue: Brain.
  8. "Ephrin-A5 induces rounding, blebbing and de-adhesion of EphA3-expressing 293T and melanoma cells by CrkII and Rho-mediated signalling."
    Lawrenson I.D., Wimmer-Kleikamp S.H., Lock P., Schoenwaelder S.M., Down M., Boyd A.W., Alewood P.F., Lackmann M.
    J. Cell Sci. 115:1059-1072(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPHA3.
  9. "Identification of Tyr900 in the kinase domain of c-Kit as a Src-dependent phosphorylation site mediating interaction with c-Crk."
    Lennartsson J., Wernstedt C., Engstrom U., Hellman U., Ronnstrand L.
    Exp. Cell Res. 288:110-118(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KIT, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION.
  10. "The roles of Cbl-b and c-Cbl in insulin-stimulated glucose transport."
    Liu J., DeYoung S.M., Hwang J.B., O'Leary E.E., Saltiel A.R.
    J. Biol. Chem. 278:36754-36762(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBLB.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk."
    Wu X., Knudsen B., Feller S.M., Zheng J., Sali A., Cowburn D., Hanafusa H., Kuriyan J.
    Structure 3:215-226(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 134-190.
  14. "Exploiting the basis of proline recognition by SH3 and WW domains: design of N-substituted inhibitors."
    Nguyen J.T., Turck C.W., Cohen F.E., Zuckermann R.N., Lim W.A.
    Science 282:2088-2092(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 133-191.

Entry informationi

Entry nameiCRK_MOUSE
AccessioniPrimary (citable) accession number: Q64010
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: September 3, 2014
This is version 138 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

External Data

Dasty 3

Similar proteinsi