SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P01901

- HA1B_MOUSE

UniProt

P01901 - HA1B_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
H-2 class I histocompatibility antigen, K-B alpha chain
Gene
H2-K1, H2-K
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in the presentation of foreign antigens to the immune system.

GO - Molecular functioni

  1. peptide antigen binding Source: MGI
  2. protein binding Source: IntAct
  3. receptor binding Source: RefGenome

GO - Biological processi

  1. antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent Source: MGI
  2. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: MGI
  3. defense response to bacterium Source: MGI
  4. immune response Source: InterPro
  5. inner ear development Source: MGI
  6. positive regulation of T cell mediated cytotoxicity Source: MGI
Complete GO annotation...

Keywords - Biological processi

Immunity

Enzyme and pathway databases

ReactomeiREACT_197102. ER-Phagosome pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
H-2 class I histocompatibility antigen, K-B alpha chain
Short name:
H-2K(B)
Gene namesi
Name:H2-K1
Synonyms:H2-K
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:95904. H2-K1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 305284Extracellular Reviewed prediction
Add
BLAST
Transmembranei306 – 32823Helical; Reviewed prediction
Add
BLAST
Topological domaini329 – 36941Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. MHC class I protein complex Source: UniProtKB-KW
  2. external side of plasma membrane Source: MGI
  3. integral component of lumenal side of endoplasmic reticulum membrane Source: Reactome
  4. phagocytic vesicle membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane, MHC I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21211 Publication
Add
BLAST
Chaini22 – 369348H-2 class I histocompatibility antigen, K-B alpha chain1 Publication
PRO_0000018928Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi107 – 1071N-linked (GlcNAc...)2 Publications
Disulfide bondi122 ↔ 185
Glycosylationi197 – 1971N-linked (GlcNAc...)1 Publication
Disulfide bondi224 ↔ 280
Modified residuei354 – 3541Phosphoserine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP01901.
PaxDbiP01901.
PRIDEiP01901.

Expressioni

Gene expression databases

ArrayExpressiP01901.
BgeeiP01901.
CleanExiMM_H2-K1.
GenevestigatoriP01901.

Interactioni

Subunit structurei

Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin).

Binary interactionsi

WithEntry#Exp.IntActNotes
FesP168793EBI-1265227,EBI-771815

Protein-protein interaction databases

DIPiDIP-6189N.
IntActiP01901. 3 interactions.
MINTiMINT-241080.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 3310
Beta strandi38 – 403
Beta strandi42 – 498
Beta strandi52 – 587
Beta strandi61 – 633
Beta strandi67 – 704
Helixi71 – 755
Helixi78 – 10528
Beta strandi110 – 1123
Beta strandi115 – 12410
Beta strandi126 – 1283
Beta strandi130 – 13910
Beta strandi142 – 1476
Turni149 – 1524
Beta strandi154 – 1585
Helixi159 – 17113
Helixi173 – 18210
Helixi184 – 19512
Helixi197 – 2004
Beta strandi207 – 2148
Beta strandi216 – 23217
Beta strandi235 – 2406
Beta strandi243 – 2453
Turni246 – 2483
Beta strandi249 – 2513
Beta strandi258 – 2603
Beta strandi262 – 27110
Helixi275 – 2773
Beta strandi278 – 2836
Beta strandi287 – 2893
Beta strandi291 – 2933

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BQHX-ray2.80A/D22-295[»]
1FO0X-ray2.50H22-296[»]
1FZJX-ray1.90A22-295[»]
1FZKX-ray1.70A22-295[»]
1FZMX-ray1.80A22-295[»]
1FZOX-ray1.80A22-295[»]
1G6RX-ray2.80H/I22-295[»]
1G7PX-ray1.50A22-295[»]
1G7QX-ray1.60A22-295[»]
1KBGX-ray2.20H22-295[»]
1KJ2X-ray2.71H/I22-298[»]
1KJ3X-ray2.30H/I22-299[»]
1KPUX-ray1.50A22-295[»]
1KPVX-ray1.71A22-295[»]
1LEGX-ray1.75A22-295[»]
1LEKX-ray2.15A22-295[»]
1LK2X-ray1.35A22-295[»]
1MWAX-ray2.40H/I22-295[»]
1N59X-ray2.95A/C22-297[»]
1NAMX-ray2.70H22-296[»]
1NANX-ray2.30H/L22-299[»]
1OSZX-ray2.10A22-295[»]
1P1ZX-ray3.26A22-295[»]
1P4LX-ray2.90A22-295[»]
1RJYX-ray1.90A/D22-301[»]
1RJZX-ray2.60A/D22-301[»]
1RK0X-ray2.61A22-295[»]
1RK1X-ray2.10A22-295[»]
1S7QX-ray1.99A22-369[»]
1S7RX-ray2.95A/D22-369[»]
1S7SX-ray1.99A22-369[»]
1S7TX-ray2.30A/D22-369[»]
1T0MX-ray2.00A/D22-299[»]
1T0NX-ray1.80A/D22-299[»]
1VACX-ray2.50A22-295[»]
1VADX-ray2.50A22-295[»]
1WBZX-ray2.00A/C22-296[»]
2CKBX-ray3.00H/I22-295[»]
2CLVX-ray1.90A/H22-300[»]
2CLZX-ray1.90A/H22-300[»]
2FO4X-ray2.70A22-295[»]
2MHAX-ray2.50A/C22-291[»]
2OL3X-ray2.90H22-300[»]
2QRIX-ray2.00A/B22-301[»]
2QRSX-ray2.00A/B22-301[»]
2QRTX-ray1.80A/B22-301[»]
2VAAX-ray2.30A22-295[»]
2VABX-ray2.50A22-295[»]
2ZSVX-ray1.80A/C22-299[»]
2ZSWX-ray2.80A/C/E/G22-299[»]
3C8KX-ray2.90A22-295[»]
3CVHX-ray2.90A/M22-295[»]
3P4MX-ray2.50A/D22-298[»]
3P4NX-ray2.50A/D22-298[»]
3P4OX-ray2.30A/D22-298[»]
3P9LX-ray2.00A/D22-299[»]
3P9MX-ray2.00A/D22-298[»]
3PABX-ray2.20A/D22-299[»]
3RGVX-ray2.90C22-296[»]
3ROLX-ray2.60A/C22-296[»]
3ROOX-ray2.00A/C22-296[»]
3TIDX-ray1.65A22-297[»]
3TIEX-ray2.25A/D22-297[»]
4HKJX-ray3.00A/E/I/M22-301[»]
4HS3X-ray2.10A22-297[»]
4PV8X-ray2.31A/C22-299[»]
4PV9X-ray2.00A/C22-299[»]
ProteinModelPortaliP01901.
SMRiP01901. Positions 22-295.

Miscellaneous databases

EvolutionaryTraceiP01901.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini206 – 29489Ig-like C1-type
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 11190Alpha-1
Add
BLAST
Regioni112 – 20392Alpha-2
Add
BLAST
Regioni204 – 29592Alpha-3
Add
BLAST
Regioni296 – 30510Connecting peptide

Sequence similaritiesi

Belongs to the MHC class I family.

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG42056.
HOVERGENiHBG016709.
InParanoidiP01901.
KOiK06751.
OMAiAYLEDEC.
PhylomeDBiP01901.
TreeFamiTF336617.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.30.500.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
IPR011161. MHC_I-like_Ag-recog.
IPR011162. MHC_I/II-like_Ag-recog.
IPR027648. MHC_I_a.
IPR001039. MHC_I_a_a1/a2.
IPR010579. MHC_I_a_C.
[Graphical view]
PfamiPF07654. C1-set. 1 hit.
PF00129. MHC_I. 1 hit.
PF06623. MHC_I_C. 1 hit.
[Graphical view]
PRINTSiPR01638. MHCCLASSI.
SMARTiSM00407. IGc1. 1 hit.
[Graphical view]
SUPFAMiSSF54452. SSF54452. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P01901-1 [UniParc]FASTAAdd to Basket

« Hide

MVPCTLLLLL AAALAPTQTR AGPHSLRYFV TAVSRPGLGE PRYMEVGYVD    50
DTEFVRFDSD AENPRYEPRA RWMEQEGPEY WERETQKAKG NEQSFRVDLR 100
TLLGYYNQSK GGSHTIQVIS GCEVGSDGRL LRGYQQYAYD GCDYIALNED 150
LKTWTAADMA ALITKHKWEQ AGEAERLRAY LEGTCVEWLR RYLKNGNATL 200
LRTDSPKAHV THHSRPEDKV TLRCWALGFY PADITLTWQL NGEELIQDME 250
LVETRPAGDG TFQKWASVVV PLGKEQYYTC HVYHQGLPEP LTLRWEPPPS 300
TVSNMATVAV LVVLGAAIVT GAVVAFVMKM RRRNTGGKGG DYALAPGSQT 350
SDLSLPDCKV MVHDPHSLA 369
Length:369
Mass (Da):41,302
Last modified:July 21, 1986 - v1
Checksum:i3D2F125318193443
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti217 – 2171E → D AA sequence 1 Publication
Sequence conflicti289 – 2891E → Q AA sequence 1 Publication
Sequence conflicti334 – 3341N → A AA sequence 1 Publication
Sequence conflicti364 – 3641D → P AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J00400 mRNA. Translation: AAA39648.1.
U47328 mRNA. Translation: AAB17606.1.
V00746, V00747 Genomic DNA. Translation: CAA24119.2.
CCDSiCCDS50069.1.
PIRiA90980. HLMSKB.
RefSeqiNP_001001892.2. NM_001001892.2.
UniGeneiMm.422886.
Mm.439675.
Mm.440940.
Mm.466882.

Genome annotation databases

EnsembliENSMUST00000025181; ENSMUSP00000025181; ENSMUSG00000061232.
GeneIDi14972.
KEGGimmu:14972.
UCSCiuc008cap.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J00400 mRNA. Translation: AAA39648.1 .
U47328 mRNA. Translation: AAB17606.1 .
V00746 , V00747 Genomic DNA. Translation: CAA24119.2 .
CCDSi CCDS50069.1.
PIRi A90980. HLMSKB.
RefSeqi NP_001001892.2. NM_001001892.2.
UniGenei Mm.422886.
Mm.439675.
Mm.440940.
Mm.466882.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BQH X-ray 2.80 A/D 22-295 [» ]
1FO0 X-ray 2.50 H 22-296 [» ]
1FZJ X-ray 1.90 A 22-295 [» ]
1FZK X-ray 1.70 A 22-295 [» ]
1FZM X-ray 1.80 A 22-295 [» ]
1FZO X-ray 1.80 A 22-295 [» ]
1G6R X-ray 2.80 H/I 22-295 [» ]
1G7P X-ray 1.50 A 22-295 [» ]
1G7Q X-ray 1.60 A 22-295 [» ]
1KBG X-ray 2.20 H 22-295 [» ]
1KJ2 X-ray 2.71 H/I 22-298 [» ]
1KJ3 X-ray 2.30 H/I 22-299 [» ]
1KPU X-ray 1.50 A 22-295 [» ]
1KPV X-ray 1.71 A 22-295 [» ]
1LEG X-ray 1.75 A 22-295 [» ]
1LEK X-ray 2.15 A 22-295 [» ]
1LK2 X-ray 1.35 A 22-295 [» ]
1MWA X-ray 2.40 H/I 22-295 [» ]
1N59 X-ray 2.95 A/C 22-297 [» ]
1NAM X-ray 2.70 H 22-296 [» ]
1NAN X-ray 2.30 H/L 22-299 [» ]
1OSZ X-ray 2.10 A 22-295 [» ]
1P1Z X-ray 3.26 A 22-295 [» ]
1P4L X-ray 2.90 A 22-295 [» ]
1RJY X-ray 1.90 A/D 22-301 [» ]
1RJZ X-ray 2.60 A/D 22-301 [» ]
1RK0 X-ray 2.61 A 22-295 [» ]
1RK1 X-ray 2.10 A 22-295 [» ]
1S7Q X-ray 1.99 A 22-369 [» ]
1S7R X-ray 2.95 A/D 22-369 [» ]
1S7S X-ray 1.99 A 22-369 [» ]
1S7T X-ray 2.30 A/D 22-369 [» ]
1T0M X-ray 2.00 A/D 22-299 [» ]
1T0N X-ray 1.80 A/D 22-299 [» ]
1VAC X-ray 2.50 A 22-295 [» ]
1VAD X-ray 2.50 A 22-295 [» ]
1WBZ X-ray 2.00 A/C 22-296 [» ]
2CKB X-ray 3.00 H/I 22-295 [» ]
2CLV X-ray 1.90 A/H 22-300 [» ]
2CLZ X-ray 1.90 A/H 22-300 [» ]
2FO4 X-ray 2.70 A 22-295 [» ]
2MHA X-ray 2.50 A/C 22-291 [» ]
2OL3 X-ray 2.90 H 22-300 [» ]
2QRI X-ray 2.00 A/B 22-301 [» ]
2QRS X-ray 2.00 A/B 22-301 [» ]
2QRT X-ray 1.80 A/B 22-301 [» ]
2VAA X-ray 2.30 A 22-295 [» ]
2VAB X-ray 2.50 A 22-295 [» ]
2ZSV X-ray 1.80 A/C 22-299 [» ]
2ZSW X-ray 2.80 A/C/E/G 22-299 [» ]
3C8K X-ray 2.90 A 22-295 [» ]
3CVH X-ray 2.90 A/M 22-295 [» ]
3P4M X-ray 2.50 A/D 22-298 [» ]
3P4N X-ray 2.50 A/D 22-298 [» ]
3P4O X-ray 2.30 A/D 22-298 [» ]
3P9L X-ray 2.00 A/D 22-299 [» ]
3P9M X-ray 2.00 A/D 22-298 [» ]
3PAB X-ray 2.20 A/D 22-299 [» ]
3RGV X-ray 2.90 C 22-296 [» ]
3ROL X-ray 2.60 A/C 22-296 [» ]
3ROO X-ray 2.00 A/C 22-296 [» ]
3TID X-ray 1.65 A 22-297 [» ]
3TIE X-ray 2.25 A/D 22-297 [» ]
4HKJ X-ray 3.00 A/E/I/M 22-301 [» ]
4HS3 X-ray 2.10 A 22-297 [» ]
4PV8 X-ray 2.31 A/C 22-299 [» ]
4PV9 X-ray 2.00 A/C 22-299 [» ]
ProteinModelPortali P01901.
SMRi P01901. Positions 22-295.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-6189N.
IntActi P01901. 3 interactions.
MINTi MINT-241080.

Proteomic databases

MaxQBi P01901.
PaxDbi P01901.
PRIDEi P01901.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000025181 ; ENSMUSP00000025181 ; ENSMUSG00000061232 .
GeneIDi 14972.
KEGGi mmu:14972.
UCSCi uc008cap.1. mouse.

Organism-specific databases

CTDi 14972.
MGIi MGI:95904. H2-K1.

Phylogenomic databases

eggNOGi NOG42056.
HOVERGENi HBG016709.
InParanoidi P01901.
KOi K06751.
OMAi AYLEDEC.
PhylomeDBi P01901.
TreeFami TF336617.

Enzyme and pathway databases

Reactomei REACT_197102. ER-Phagosome pathway.

Miscellaneous databases

ChiTaRSi H2-K1. mouse.
EvolutionaryTracei P01901.
NextBioi 287336.
PROi P01901.
SOURCEi Search...

Gene expression databases

ArrayExpressi P01901.
Bgeei P01901.
CleanExi MM_H2-K1.
Genevestigatori P01901.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
3.30.500.10. 1 hit.
InterProi IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
IPR011161. MHC_I-like_Ag-recog.
IPR011162. MHC_I/II-like_Ag-recog.
IPR027648. MHC_I_a.
IPR001039. MHC_I_a_a1/a2.
IPR010579. MHC_I_a_C.
[Graphical view ]
Pfami PF07654. C1-set. 1 hit.
PF00129. MHC_I. 1 hit.
PF06623. MHC_I_C. 1 hit.
[Graphical view ]
PRINTSi PR01638. MHCCLASSI.
SMARTi SM00407. IGc1. 1 hit.
[Graphical view ]
SUPFAMi SSF54452. SSF54452. 1 hit.
PROSITEi PS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence of the H-2K(b) gene: evidence for gene conversion as a mechanism for the generation of polymorphism in histocompatibility antigens."
    Weiss E., Golden L., Zakut R., Mellor A., Fahrner K., Kvist S., Flavell R.A.
    EMBO J. 2:453-462(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Nucleotide sequences of three H-2K and three H-2D complementary DNA clones coding mouse class I MHC heavy chain proteins."
    Wang M., Stepkowski S.M., Hebert J.S., Tian L., Yu J., Kahan B.D.
    Ann. Transplant. 1:26-31(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/10.
  3. "Isolation of a cDNA clone for the murine transplantation antigen H-2Kb."
    Reyes A.A., Schold M., Itakura K., Wallace R.B.
    Proc. Natl. Acad. Sci. U.S.A. 79:3270-3274(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 87-369.
  4. "Amino acid sequence of the carboxyl-terminal hydrophilic region of the H-2Kb MHC alloantigen. Completion of the entire primary structure of the H-2Kb molecule."
    Uehara H., Coligan J.E., Nathenson S.G.
    Biochemistry 20:5940-5945(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-367, GLYCOSYLATION AT ASN-107 AND ASN-197.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-107.
  7. "Crystal structures of two viral peptides in complex with murine MHC class I H-2Kb."
    Fremont D.H., Matsumura M., Stura E.A., Peterson P.A., Wilson I.A.
    Science 257:919-927(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 22-295.
  8. "Structural basis of CD8 coreceptor function revealed by crystallographic analysis of a murine CD8alphaalpha ectodomain fragment in complex with H-2Kb."
    Kern P.S., Teng M.K., Smolyar A., Liu J.H., Liu J., Hussey R.E., Spoerl R., Chang H.-C., Reinherz E.L., Wang J.-H.
    Immunity 9:519-530(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-295 IN COMPLEX WITH CD8A.
  9. "Crystal structure of an MHC class I presented glycopeptide that generates carbohydrate-specific CTL."
    Speir J.A., Abdel-Motal U.M., Jondal M., Wilson I.A.
    Immunity 10:51-61(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 22-295.

Entry informationi

Entry nameiHA1B_MOUSE
AccessioniPrimary (citable) accession number: P01901
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 3, 2014
This is version 145 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, Direct protein sequencing, 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