ID KLK4_HUMAN Reviewed; 254 AA. AC Q9Y5K2; Q4VB16; Q96RU5; Q9GZL6; Q9UBJ6; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 2. DT 27-MAR-2024, entry version 189. DE RecName: Full=Kallikrein-4; DE EC=3.4.21.-; DE AltName: Full=Enamel matrix serine proteinase 1; DE AltName: Full=Kallikrein-like protein 1; DE Short=KLK-L1; DE AltName: Full=Prostase; DE AltName: Full=Serine protease 17; DE Flags: Precursor; GN Name=KLK4; Synonyms=EMSP1, PRSS17, PSTS; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). RX PubMed=10077646; DOI=10.1073/pnas.96.6.3114; RA Nelson P.S., Gan L., Ferguson C., Moss P., Gelinas R., Hood L., Wang K.; RT "Molecular cloning and characterization of prostase, an androgen-regulated RT serine protease with prostate-restricted expression."; RL Proc. Natl. Acad. Sci. U.S.A. 96:3114-3119(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-197. RX PubMed=10485467; RA Yousef G.M., Obiezu C.V., Luo L.-Y., Black M.H., Diamandis E.P.; RT "Prostase/KLK-L1 is a new member of the human kallikrein gene family, is RT expressed in prostate and breast tissues, and is hormonally regulated."; RL Cancer Res. 59:4252-4256(1999). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-197. RX PubMed=10438493; DOI=10.1074/jbc.274.33.23210; RA Stephenson S.A., Verity K., Ashworth L.K., Clements J.A.; RT "Localization of a new prostate-specific antigen-related serine protease RT gene, KLK4, is evidence for an expanded human kallikrein gene family RT cluster on chromosome 19q13.3-13.4."; RL J. Biol. Chem. 274:23210-23214(1999). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11054574; DOI=10.1016/s0378-1119(00)00382-6; RA Gan L., Lee I., Smith R., Argonza-Barrett R., Lei H., McCuaig J., Moss P., RA Paeper B., Wang K.; RT "Sequencing and expression analysis of the serine protease gene cluster RT located in chromosome 19q13 region."; RL Gene 257:119-130(2000). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND VARIANT GLN-197. RX PubMed=10863090; DOI=10.1016/s0378-1119(00)00203-1; RA Hu J.C.-C., Zhang C., Sun X., Yang Y., Cao X., Ryu O., Simmer J.P.; RT "Characterization of the mouse and human PRSS17 genes, their relationship RT to other serine proteases, and the expression of PRSS17 in developing mouse RT incisors."; RL Gene 251:1-8(2000). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT GLN-197, AND RP ALTERNATIVE SPLICING. RC TISSUE=Prostatic carcinoma; RX PubMed=11506707; DOI=10.1089/104454901750361497; RA Korkmaz K.S., Korkmaz C.G., Pretlow T.G., Saatcioglu F.; RT "Distinctly different gene structure of KLK4/KLK-L1/prostase/ARM1 compared RT with other members of the kallikrein family: intracellular localization, RT alternative cDNA forms, and Regulation by multiple hormones."; RL DNA Cell Biol. 20:435-445(2001). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-197. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-254 (ISOFORM 1), AND VARIANT GLN-197. RA Simmer J.P., Ryu O.H., Qian Q., Zhang C., Cao X., Sun X., Hu C.-C.; RT "Cloning and characterization of a cDNA encoding human EMSP1."; RL (In) Goldberg M. (eds.); RL Chemistry and biology of mineralized tissues, pp.1-1, American Academy of RL Orthopaedic Surgeons, Vittel (2000). RN [10] RP PROTEIN SEQUENCE OF 31-35, X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF RP 31-253, ACTIVE SITE, ZINC-BINDING SITES, DISULFIDE BONDS, AND VARIANT RP GLN-197. RX PubMed=16950394; DOI=10.1016/j.jmb.2006.08.003; RA Debela M., Magdolen V., Grimminger V., Sommerhoff C., Messerschmidt A., RA Huber R., Friedrich R., Bode W., Goettig P.; RT "Crystal structures of human tissue kallikrein 4: activity modulation by a RT specific zinc binding site."; RL J. Mol. Biol. 362:1094-1107(2006). RN [11] RP FUNCTION, INVOLVEMENT IN AI2A1, AND VARIANT ALA-22. RX PubMed=15235027; DOI=10.1136/jmg.2003.017657; RA Hart P.S., Hart T.C., Michalec M.D., Ryu O.H., Simmons D., Hong S., RA Wright J.T.; RT "Mutation in kallikrein 4 causes autosomal recessive hypomaturation RT amelogenesis imperfecta."; RL J. Med. Genet. 41:545-549(2004). CC -!- FUNCTION: Has a major role in enamel formation (PubMed:15235027). CC Required during the maturation stage of tooth development for clearance CC of enamel proteins and normal structural patterning of the crystalline CC matrix (By similarity). {ECO:0000250|UniProtKB:Q9Z0M1, CC ECO:0000269|PubMed:15235027}. CC -!- INTERACTION: CC Q9Y5K2; P20155: SPINK2; NbExp=4; IntAct=EBI-10224152, EBI-10200479; CC Q9Y5K2; Q06418: TYRO3; NbExp=3; IntAct=EBI-10224152, EBI-3951628; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9Y5K2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y5K2-2; Sequence=VSP_056629, VSP_056630; CC -!- TISSUE SPECIFICITY: Expressed in prostate. CC -!- PTM: N-glycosylated. The N-glycan structures are of complex diantennary CC or triantennary type, which may be further modified with up to 2 sialic CC acid residues. {ECO:0000250|UniProtKB:Q9Z0M1}. CC -!- DISEASE: Amelogenesis imperfecta, hypomaturation type, 2A1 (AI2A1) CC [MIM:204700]: A defect of enamel formation. The disorder involves both CC primary and secondary dentitions. The teeth have a shiny agar jelly CC appearance and the enamel is softer than normal. Brown pigment is CC present in middle layers of enamel. {ECO:0000269|PubMed:15235027}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00274}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/41084/KLK4"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF113140; AAD21580.1; -; mRNA. DR EMBL; AF113141; AAD21581.1; -; Genomic_DNA. DR EMBL; AF135023; AAD26424.2; -; Genomic_DNA. DR EMBL; AF148532; AAD38019.1; -; Genomic_DNA. DR EMBL; AF243527; AAG33357.1; -; Genomic_DNA. DR EMBL; AF228497; AAF70620.1; -; Genomic_DNA. DR EMBL; AF259969; AAF81227.1; -; mRNA. DR EMBL; AF259971; AAK71706.1; -; mRNA. DR EMBL; AC037199; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC069325; AAH69325.1; -; mRNA. DR EMBL; BC069403; AAH69403.1; -; mRNA. DR EMBL; BC069429; AAH69429.1; -; mRNA. DR EMBL; BC069489; AAH69489.1; -; mRNA. DR EMBL; BC096175; AAH96175.1; -; mRNA. DR EMBL; BC096178; AAH96178.1; -; mRNA. DR EMBL; AF126401; AAG43246.1; -; mRNA. DR CCDS; CCDS12809.1; -. [Q9Y5K2-1] DR RefSeq; NP_001289890.1; NM_001302961.1. DR RefSeq; NP_004908.4; NM_004917.4. DR PDB; 2BDG; X-ray; 1.95 A; A/B=31-253. DR PDB; 2BDH; X-ray; 3.00 A; A/B/C/D=31-253. DR PDB; 2BDI; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=31-253. DR PDB; 4K1E; X-ray; 1.30 A; A=31-253. DR PDB; 4K8Y; X-ray; 1.00 A; A=31-253. DR PDB; 4KEL; X-ray; 1.15 A; A=31-253. DR PDB; 4KGA; X-ray; 2.32 A; A/B=31-253. DR PDB; 6KBR; X-ray; 2.00 A; A=1-254. DR PDB; 6NVB; X-ray; 1.64 A; A/B/C/D=31-254. DR PDB; 6O21; X-ray; 1.15 A; A=31-253. DR PDB; 7JOD; X-ray; 1.33 A; E=31-253. DR PDB; 7JOE; X-ray; 2.60 A; E=31-253. DR PDB; 7JOS; X-ray; 2.10 A; A/C/E/G/I/K/M=31-253. DR PDB; 7JOW; X-ray; 1.91 A; E=31-253. DR PDB; 7JQK; X-ray; 1.33 A; E=31-253. DR PDB; 7JQN; X-ray; 1.50 A; E=31-253. DR PDB; 7JQO; X-ray; 1.60 A; E=31-253. DR PDB; 7JQV; X-ray; 2.10 A; E=31-253. DR PDBsum; 2BDG; -. DR PDBsum; 2BDH; -. DR PDBsum; 2BDI; -. DR PDBsum; 4K1E; -. DR PDBsum; 4K8Y; -. DR PDBsum; 4KEL; -. DR PDBsum; 4KGA; -. DR PDBsum; 6KBR; -. DR PDBsum; 6NVB; -. DR PDBsum; 6O21; -. DR PDBsum; 7JOD; -. DR PDBsum; 7JOE; -. DR PDBsum; 7JOS; -. DR PDBsum; 7JOW; -. DR PDBsum; 7JQK; -. DR PDBsum; 7JQN; -. DR PDBsum; 7JQO; -. DR PDBsum; 7JQV; -. DR AlphaFoldDB; Q9Y5K2; -. DR SMR; Q9Y5K2; -. DR BioGRID; 114982; 10. DR IntAct; Q9Y5K2; 4. DR STRING; 9606.ENSP00000326159; -. DR BindingDB; Q9Y5K2; -. DR ChEMBL; CHEMBL4446; -. DR GuidetoPHARMACOLOGY; 2374; -. DR MEROPS; S01.251; -. DR GlyCosmos; Q9Y5K2; 1 site, No reported glycans. DR GlyGen; Q9Y5K2; 1 site. DR PhosphoSitePlus; Q9Y5K2; -. DR BioMuta; KLK4; -. DR DMDM; 317373372; -. DR EPD; Q9Y5K2; -. DR MassIVE; Q9Y5K2; -. DR PaxDb; 9606-ENSP00000326159; -. DR PeptideAtlas; Q9Y5K2; -. DR Antibodypedia; 18932; 317 antibodies from 35 providers. DR DNASU; 9622; -. DR Ensembl; ENST00000431178.2; ENSP00000399448.2; ENSG00000167749.12. [Q9Y5K2-2] DR GeneID; 9622; -. DR KEGG; hsa:9622; -. DR UCSC; uc002pty.2; human. [Q9Y5K2-1] DR AGR; HGNC:6365; -. DR CTD; 9622; -. DR DisGeNET; 9622; -. DR GeneCards; KLK4; -. DR HGNC; HGNC:6365; KLK4. DR HPA; ENSG00000167749; Tissue enriched (prostate). DR MalaCards; KLK4; -. DR MIM; 204700; phenotype. DR MIM; 603767; gene. DR neXtProt; NX_Q9Y5K2; -. DR OpenTargets; ENSG00000167749; -. DR Orphanet; 100033; Hypomaturation amelogenesis imperfecta. DR PharmGKB; PA30154; -. DR VEuPathDB; HostDB:ENSG00000167749; -. DR eggNOG; KOG3627; Eukaryota. DR GeneTree; ENSGT01020000230389; -. DR HOGENOM; CLU_006842_1_7_1; -. DR InParanoid; Q9Y5K2; -. DR OMA; LICKGSL; -. DR OrthoDB; 4629979at2759; -. DR PhylomeDB; Q9Y5K2; -. DR TreeFam; TF331065; -. DR BRENDA; 3.4.21.B12; 2681. DR PathwayCommons; Q9Y5K2; -. DR SignaLink; Q9Y5K2; -. DR SIGNOR; Q9Y5K2; -. DR BioGRID-ORCS; 9622; 9 hits in 1146 CRISPR screens. DR ChiTaRS; KLK4; human. DR EvolutionaryTrace; Q9Y5K2; -. DR GeneWiki; KLK4; -. DR GenomeRNAi; 9622; -. DR Pharos; Q9Y5K2; Tchem. DR PRO; PR:Q9Y5K2; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q9Y5K2; Protein. DR Bgee; ENSG00000167749; Expressed in prostate gland and 125 other cell types or tissues. DR ExpressionAtlas; Q9Y5K2; baseline and differential. DR GO; GO:0005576; C:extracellular region; TAS:ProtInc. DR GO; GO:0030141; C:secretory granule; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc. DR GO; GO:0097186; P:amelogenesis; IMP:UniProtKB. DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW. DR GO; GO:0022617; P:extracellular matrix disassembly; IBA:GO_Central. DR GO; GO:0006508; P:proteolysis; NAS:UniProtKB. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR018114; TRYPSIN_HIS. DR InterPro; IPR033116; TRYPSIN_SER. DR PANTHER; PTHR24264:SF15; RIKEN CDNA 2210010C04 GENE; 1. DR PANTHER; PTHR24264; TRYPSIN-RELATED; 1. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. DR Genevisible; Q9Y5K2; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Amelogenesis imperfecta; KW Biomineralization; Direct protein sequencing; Disulfide bond; Glycoprotein; KW Hydrolase; Metal-binding; Protease; Reference proteome; Secreted; KW Serine protease; Signal; Zinc; Zymogen. FT SIGNAL 1..26 FT /evidence="ECO:0000255" FT PROPEP 27..30 FT /evidence="ECO:0000305|PubMed:16950394" FT /id="PRO_0000027937" FT CHAIN 31..254 FT /note="Kallikrein-4" FT /id="PRO_0000027938" FT DOMAIN 31..252 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT ACT_SITE 71 FT /note="Charge relay system" FT /evidence="ECO:0000269|PubMed:16950394" FT ACT_SITE 116 FT /note="Charge relay system" FT /evidence="ECO:0000269|PubMed:16950394" FT ACT_SITE 207 FT /note="Charge relay system" FT /evidence="ECO:0000269|PubMed:16950394" FT BINDING 40 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:16950394" FT BINDING 91 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:16950394" FT CARBOHYD 169 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 37..167 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274, FT ECO:0000269|PubMed:16950394" FT DISULFID 56..72 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274, FT ECO:0000269|PubMed:16950394" FT DISULFID 141..241 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274, FT ECO:0000269|PubMed:16950394" FT DISULFID 148..213 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274, FT ECO:0000269|PubMed:16950394" FT DISULFID 178..192 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274, FT ECO:0000269|PubMed:16950394" FT DISULFID 203..228 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274, FT ECO:0000269|PubMed:16950394" FT VAR_SEQ 1..49 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11506707" FT /id="VSP_056629" FT VAR_SEQ 160..254 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11506707" FT /id="VSP_056630" FT VARIANT 22 FT /note="S -> A (in dbSNP:rs1654551)" FT /evidence="ECO:0000269|PubMed:15235027" FT /id="VAR_028364" FT VARIANT 159 FT /note="G -> D (in dbSNP:rs34626614)" FT /id="VAR_033009" FT VARIANT 197 FT /note="H -> Q (in dbSNP:rs2569527)" FT /evidence="ECO:0000269|PubMed:10438493, FT ECO:0000269|PubMed:10485467, ECO:0000269|PubMed:10863090, FT ECO:0000269|PubMed:11506707, ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16950394, ECO:0000269|Ref.9" FT /id="VAR_028365" FT STRAND 45..50 FT /evidence="ECO:0007829|PDB:4K8Y" FT STRAND 53..62 FT /evidence="ECO:0007829|PDB:4K8Y" FT STRAND 65..68 FT /evidence="ECO:0007829|PDB:4K8Y" FT HELIX 70..72 FT /evidence="ECO:0007829|PDB:4K8Y" FT STRAND 75..82 FT /evidence="ECO:0007829|PDB:4K8Y" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:4K8Y" FT HELIX 88..90 FT /evidence="ECO:0007829|PDB:4K8Y" FT STRAND 95..99 FT /evidence="ECO:0007829|PDB:4K8Y" FT STRAND 101..104 FT /evidence="ECO:0007829|PDB:4K8Y" FT TURN 106..109 FT /evidence="ECO:0007829|PDB:4K8Y" FT STRAND 118..121 FT /evidence="ECO:0007829|PDB:4K8Y" FT STRAND 130..132 FT /evidence="ECO:0007829|PDB:7JOD" FT STRAND 147..154 FT /evidence="ECO:0007829|PDB:4K8Y" FT STRAND 157..160 FT /evidence="ECO:0007829|PDB:2BDH" FT STRAND 166..172 FT /evidence="ECO:0007829|PDB:4K8Y" FT HELIX 175..182 FT /evidence="ECO:0007829|PDB:4K8Y" FT TURN 183..185 FT /evidence="ECO:0007829|PDB:4K8Y" FT STRAND 190..193 FT /evidence="ECO:0007829|PDB:4K8Y" FT STRAND 210..213 FT /evidence="ECO:0007829|PDB:4K8Y" FT STRAND 216..227 FT /evidence="ECO:0007829|PDB:4K8Y" FT STRAND 235..239 FT /evidence="ECO:0007829|PDB:4K8Y" FT HELIX 240..242 FT /evidence="ECO:0007829|PDB:4K8Y" FT HELIX 244..252 FT /evidence="ECO:0007829|PDB:4K8Y" SQ SEQUENCE 254 AA; 27032 MW; 9C5E4722AFF70CB8 CRC64; MATAGNPWGW FLGYLILGVA GSLVSGSCSQ IINGEDCSPH SQPWQAALVM ENELFCSGVL VHPQWVLSAA HCFQNSYTIG LGLHSLEADQ EPGSQMVEAS LSVRHPEYNR PLLANDLMLI KLDESVSESD TIRSISIASQ CPTAGNSCLV SGWGLLANGR MPTVLQCVNV SVVSEEVCSK LYDPLYHPSM FCAGGGHDQK DSCNGDSGGP LICNGYLQGL VSFGKAPCGQ VGVPGVYTNL CKFTEWIEKT VQAS //