KLK4_HUMAN
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 03-AUG-2022, entry version 180.
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="http://atlasgeneticsoncology.org/Genes/KLK4ID41084ch19q13.html";
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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; 9.
DR IntAct; Q9Y5K2; 4.
DR STRING; 9606.ENSP00000326159; -.
DR BindingDB; Q9Y5K2; -.
DR ChEMBL; CHEMBL4446; -.
DR GuidetoPHARMACOLOGY; 2374; -.
DR MEROPS; S01.251; -.
DR GlyGen; Q9Y5K2; 1 site.
DR PhosphoSitePlus; Q9Y5K2; -.
DR BioMuta; KLK4; -.
DR DMDM; 317373372; -.
DR EPD; Q9Y5K2; -.
DR MassIVE; Q9Y5K2; -.
DR PaxDb; Q9Y5K2; -.
DR PeptideAtlas; Q9Y5K2; -.
DR PRIDE; Q9Y5K2; -.
DR Antibodypedia; 18932; 292 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 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; TEDEFFC; -.
DR OrthoDB; 1314811at2759; -.
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; 8 hits in 1068 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 123 other tissues.
DR ExpressionAtlas; Q9Y5K2; baseline and differential.
DR Genevisible; Q9Y5K2; HS.
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; -; 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 Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
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:7JQK"
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
