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Q9LDI3

- CIPKO_ARATH

UniProt

Q9LDI3 - CIPKO_ARATH

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Protein
CBL-interacting serine/threonine-protein kinase 24
Gene
CIPK24, SnRK3.11, SOS2, At5g35410, F6I13.1, K21B8.3
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in the regulatory pathway for the control of intracellular Na+ and K+ homeostasis and salt tolerance. Activates the vacuolar H+/Ca2+ antiporter CAX1 and operates in synergy with CBL4/SOS3 to activate the plasma membrane Na+/H+ antiporter SOS1. CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner. Phosphorylates CBL1, CBL4 and CBL10.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Manganese.1 Publication

Kineticsi

  1. KM=131.2 µM for synthetic substrate1 Publication

Vmax=1304 pmol/min/mg enzyme

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei40 – 401ATP By similarity
Active sitei134 – 1341Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 259ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein binding Source: IntAct
  3. protein kinase activity Source: TAIR
  4. protein serine/threonine kinase activity Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. response to salt stress Source: TAIR
  2. signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Manganese, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT5G35410-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
CBL-interacting serine/threonine-protein kinase 24 (EC:2.7.11.1)
Alternative name(s):
Protein SALT OVERLY SENSITIVE 2
SNF1-related kinase 3.11
Gene namesi
Name:CIPK24
Synonyms:SnRK3.11, SOS2
Ordered Locus Names:At5g35410
ORF Names:F6I13.1, K21B8.3
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 5

Organism-specific databases

TAIRiAT5G35410.

Subcellular locationi

Cytoplasm. Nucleus
Note: Targeted to the cell membrane when interacting with CBL1 or CBL5 and to the tonoplast when interacting with CBL2 orCBL10.1 Publication

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
  2. plant-type vacuole membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi40 – 401K → N: Abolishes autophosphorylation. 1 Publication
Mutagenesisi156 – 1561S → D: Increases kinase activity. 1 Publication
Mutagenesisi168 – 1681T → D: Increases kinase activity. 1 Publication
Mutagenesisi175 – 1751Y → D: Increases kinase activity. 1 Publication
Mutagenesisi197 – 1971G → E: Abolishes autophosphorylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 446446CBL-interacting serine/threonine-protein kinase 24
PRO_0000085877Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei156 – 1561Phosphoserine By similarity
Modified residuei168 – 1681Phosphothreonine By similarity
Modified residuei169 – 1691Phosphothreonine By similarity

Post-translational modificationi

Autophosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9LDI3.
PRIDEiQ9LDI3.

Expressioni

Inductioni

Up-regulated in roots by salt stress.

Gene expression databases

GenevestigatoriQ9LDI3.

Interactioni

Subunit structurei

Interacts with CBL1, CBL2, CBL4/SOS3, CBL5, CBL9, CBL10 and with the protein phosphatase 2C ABI2.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI2O047194EBI-537551,EBI-537680
CAM4P258542EBI-537551,EBI-1235664
CAM7P592202EBI-537551,EBI-1236031
CBL1O814453EBI-537551,EBI-974530
CBL10Q7FRS85EBI-537551,EBI-2026616
CBL10Q7FRS8-24EBI-537551,EBI-2026677
CBL4O812239EBI-537551,EBI-537541
CML9Q9S7442EBI-537551,EBI-1236048
NDPK2O649033EBI-537551,EBI-349517

Protein-protein interaction databases

BioGridi18756. 20 interactions.
DIPiDIP-34745N.
IntActiQ9LDI3. 30 interactions.
MINTiMINT-274819.
STRINGi3702.AT5G35410.1-P.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi312 – 3165
Turni320 – 3223
Helixi324 – 3285
Beta strandi340 – 3434
Helixi347 – 36014
Beta strandi363 – 37614
Helixi381 – 3833
Beta strandi386 – 39510
Beta strandi398 – 40811
Helixi410 – 42314
Turni425 – 4273

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EHBX-ray2.10D304-446[»]
ProteinModelPortaliQ9LDI3.
SMRiQ9LDI3. Positions 6-430.

Miscellaneous databases

EvolutionaryTraceiQ9LDI3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 264254Protein kinase
Add
BLAST
Domaini305 – 32925NAF
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni152 – 17928Activation loop
Add
BLAST
Regioni336 – 36530PPI
Add
BLAST

Domaini

The activation loop within the kinase domain is the target of phosphorylation/activation by upstream protein kinases. The PPI motif mediates the interaction with the ABI (abscisic acid-insensitive) phosphatases. The C-terminal part (309-446) of the protein is required for the phosphorylation of CBL, but is not involved in autophosphorylation.2 Publications

Sequence similaritiesi

Contains 1 NAF domain.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233016.
InParanoidiQ9LDI3.
OMAiNAFEMIT.
PhylomeDBiQ9LDI3.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR018451. NAF/FISL_domain.
IPR004041. NAF_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF03822. NAF. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50816. NAF. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9LDI3-1 [UniParc]FASTAAdd to Basket

« Hide

MTKKMRRVGK YEVGRTIGEG TFAKVKFARN TDTGDNVAIK IMAKSTILKN    50
RMVDQIKREI SIMKIVRHPN IVRLYEVLAS PSKIYIVLEF VTGGELFDRI 100
VHKGRLEESE SRKYFQQLVD AVAHCHCKGV YHRDLKPENL LLDTNGNLKV 150
SDFGLSALPQ EGVELLRTTC GTPNYVAPEV LSGQGYDGSA ADIWSCGVIL 200
FVILAGYLPF SETDLPGLYR KINAAEFSCP PWFSAEVKFL IHRILDPNPK 250
TRIQIQGIKK DPWFRLNYVP IRAREEEEVN LDDIRAVFDG IEGSYVAENV 300
ERNDEGPLMM NAFEMITLSQ GLNLSALFDR RQDFVKRQTR FVSRREPSEI 350
IANIEAVANS MGFKSHTRNF KTRLEGLSSI KAGQLAVVIE IYEVAPSLFM 400
VDVRKAAGET LEYHKFYKKL CSKLENIIWR ATEGIPKSEI LRTITF 446
Length:446
Mass (Da):50,635
Last modified:October 1, 2000 - v1
Checksum:i99FDF3A778E1093D
GO

Sequence cautioni

The sequence AAF67384.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF237670 Genomic DNA. Translation: AAF62923.1.
AF395081 mRNA. Translation: AAK72257.1.
AB025611 Genomic DNA. Translation: BAA98146.1.
AF262044 Genomic DNA. Translation: AAF67384.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED93966.1.
AY099621 mRNA. Translation: AAM20472.1.
BT002138 mRNA. Translation: AAN72149.1.
RefSeqiNP_198391.1. NM_122932.4.
UniGeneiAt.7930.

Genome annotation databases

EnsemblPlantsiAT5G35410.1; AT5G35410.1; AT5G35410.
GeneIDi833502.
KEGGiath:AT5G35410.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF237670 Genomic DNA. Translation: AAF62923.1 .
AF395081 mRNA. Translation: AAK72257.1 .
AB025611 Genomic DNA. Translation: BAA98146.1 .
AF262044 Genomic DNA. Translation: AAF67384.1 . Sequence problems.
CP002688 Genomic DNA. Translation: AED93966.1 .
AY099621 mRNA. Translation: AAM20472.1 .
BT002138 mRNA. Translation: AAN72149.1 .
RefSeqi NP_198391.1. NM_122932.4.
UniGenei At.7930.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EHB X-ray 2.10 D 304-446 [» ]
ProteinModelPortali Q9LDI3.
SMRi Q9LDI3. Positions 6-430.
ModBasei Search...

Protein-protein interaction databases

BioGridi 18756. 20 interactions.
DIPi DIP-34745N.
IntActi Q9LDI3. 30 interactions.
MINTi MINT-274819.
STRINGi 3702.AT5G35410.1-P.

Proteomic databases

PaxDbi Q9LDI3.
PRIDEi Q9LDI3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G35410.1 ; AT5G35410.1 ; AT5G35410 .
GeneIDi 833502.
KEGGi ath:AT5G35410.

Organism-specific databases

TAIRi AT5G35410.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233016.
InParanoidi Q9LDI3.
OMAi NAFEMIT.
PhylomeDBi Q9LDI3.

Enzyme and pathway databases

BioCyci ARA:AT5G35410-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q9LDI3.

Gene expression databases

Genevestigatori Q9LDI3.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR018451. NAF/FISL_domain.
IPR004041. NAF_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF03822. NAF. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50816. NAF. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The Arabidopsis thaliana SOS2 gene encodes a protein kinase that is required for salt tolerance."
    Liu J., Ishitani M., Halfter U., Kim C.-S., Zhu J.-K.
    Proc. Natl. Acad. Sci. U.S.A. 97:3730-3734(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, MUTAGENESIS OF LYS-40 AND GLY-197.
    Strain: cv. Columbia.
  2. "Molecular characterization of the CIPK gene family from Arabidopsis thaliana."
    Weinl S., Albrecht V., Kudla J.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Structural analysis of Arabidopsis thaliana chromosome 5. XI."
    Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., Tabata S.
    Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  5. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  6. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  7. "The Arabidopsis SOS2 protein kinase physically interacts with and is activated by the calcium-binding protein SOS3."
    Halfter U., Ishitani M., Zhu J.-K.
    Proc. Natl. Acad. Sci. U.S.A. 97:3735-3740(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CBL4, MUTAGENESIS OF THR-168.
  8. "Molecular characterization of functional domains in the protein kinase SOS2 that is required for plant salt tolerance."
    Guo Y., Halfter U., Ishitani M., Zhu J.-K.
    Plant Cell 13:1383-1400(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVATION DOMAINS.
  9. "Regulation of SOS1, a plasma membrane Na(+)/H(+) exchanger in Arabidopsis thaliana, by SOS2 and SOS3."
    Qiu Q.-S., Guo Y., Dietrich M.A., Schumaker K.S., Zhu J.-K.
    Proc. Natl. Acad. Sci. U.S.A. 99:8436-8441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Biochemical characterization of the Arabidopsis protein kinase SOS2 that functions in salt tolerance."
    Gong D., Guo Y., Jagendorf A.T., Zhu J.-K.
    Plant Physiol. 130:256-264(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-156 AND TYR-175.
  11. "A novel domain in the protein kinase SOS2 mediates interaction with the protein phosphatase 2C ABI2."
    Ohta M., Guo Y., Halfter U., Zhu J.-K.
    Proc. Natl. Acad. Sci. U.S.A. 100:11771-11776(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ABI2.
  12. Cited for: GENE FAMILY, NOMENCLATURE.
  13. "The protein kinase SOS2 activates the Arabidopsis H(+)/Ca(2+) antiporter CAX1 to integrate calcium transport and salt tolerance."
    Cheng N.-H., Pittman J.K., Zhu J.-K., Hirschi K.D.
    J. Biol. Chem. 279:2922-2926(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Calcium sensors and their interacting protein kinases: genomics of the Arabidopsis and rice CBL-CIPK signaling networks."
    Kolukisaoglu U., Weinl S., Blazevic D., Batistic O., Kudla J.
    Plant Physiol. 134:43-58(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBL1 AND CBL9.
  15. "The calcium sensor CBL10 mediates salt tolerance by regulating ion homeostasis in Arabidopsis."
    Kim B.G., Waadt R., Cheong Y.H., Pandey G.K., Dominguez-Solis J.R., Schueltke S., Lee S.C., Kudla J., Luan S.
    Plant J. 52:473-484(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBL1; CBL2; CBL5 AND CBL10, SUBCELLULAR LOCATION.
  16. "Phosphorylation of calcineurin B-like (CBL) calcium sensor proteins by their CBL-interacting protein kinases (CIPKs) is required for full activity of CBL-CIPK complexes toward their target proteins."
    Hashimoto K., Eckert C., Anschuetz U., Scholz M., Held K., Waadt R., Reyer A., Hippler M., Becker D., Kudla J.
    J. Biol. Chem. 287:7956-7968(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHORYLATION, INTERACTION WITH CBL1; CBL4 AND CBL10, DOMAIN.
  17. "The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3."
    Sanchez-Barrena M.J., Fujii H., Angulo I., Martinez-Ripoll M., Zhu J.-K., Albert A.
    Mol. Cell 26:427-435(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 304-446 IN COMPLEX WITH SOS3, INTERACTION WITH SOS3 AND ABI2.

Entry informationi

Entry nameiCIPKO_ARATH
AccessioniPrimary (citable) accession number: Q9LDI3
Secondary accession number(s): Q9LKR2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  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

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