CATF_HUMAN
ID CATF_HUMAN Reviewed; 484 AA.
AC Q9UBX1; B2R964; O95240; Q9NSU4; Q9UKQ5;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Cathepsin F;
DE Short=CATSF;
DE EC=3.4.22.41;
DE Flags: Precursor;
GN Name=CTSF;
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 [MRNA].
RC TISSUE=Prostate;
RX PubMed=10318784; DOI=10.1074/jbc.274.20.13800;
RA Santamaria I., Velasco G., Pendas A.M., Paz A., Lopez-Otin C.;
RT "Molecular cloning and structural and functional characterization of human
RT cathepsin F, a new cysteine proteinase of the papain family with a long
RT propeptide domain.";
RL J. Biol. Chem. 274:13800-13809(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=10198209; DOI=10.1006/bbrc.1999.0461;
RA Naegler D.K., Sulea T., Menard R.;
RT "Full-length cDNA of human cathepsin F predicts the presence of a cystatin
RT domain at the N-terminus of the cysteine protease zymogen.";
RL Biochem. Biophys. Res. Commun. 257:313-318(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10661872; DOI=10.1515/bc.1999.185;
RA Wex T., Wex H., Broemme D.;
RT "The human cathepsin F gene -- a fusion product between an ancestral
RT cathepsin and cystatin gene.";
RL Biol. Chem. 380:1439-1442(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10362521; DOI=10.1006/bbrc.1999.0700;
RA Wex T., Levy B., Wex H., Bromme D.;
RT "Human cathepsins F and W: a new subgroup of cathepsins.";
RL Biochem. Biophys. Res. Commun. 259:401-407(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RA Deussing J., Tisljar K., Papazoglou A., Peters C.;
RT "Cathepsin F, a novel cysteine protease with an extremely long
RT propeptide.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Testis;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 147-484, AND CHARACTERIZATION.
RC TISSUE=Brain, and Smooth muscle;
RX PubMed=9822672; DOI=10.1074/jbc.273.48.32000;
RA Wang B., Shi G.-P., Yao P.M., Li Z., Chapman H.A., Broemme D.;
RT "Human cathepsin F. Molecular cloning, functional expression, tissue
RT localization, and enzymatic characterization.";
RL J. Biol. Chem. 273:32000-32008(1998).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-484.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-367; ASN-378 AND ASN-440.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 271-484, ACTIVE SITE, AND
RP DISULFIDE BONDS.
RX PubMed=12225749; DOI=10.1016/s0022-2836(02)00780-5;
RA Somoza J.R., Palmer J.T., Ho J.D.;
RT "The crystal structure of human cathepsin F and its implications for the
RT development of novel immunomodulators.";
RL J. Mol. Biol. 322:559-568(2002).
RN [12]
RP VARIANTS CLN13 CYS-231; ARG-321; ALA-458 AND LEU-480.
RX PubMed=23297359; DOI=10.1093/hmg/dds558;
RA Smith K.R., Dahl H.H., Canafoglia L., Andermann E., Damiano J., Morbin M.,
RA Bruni A.C., Giaccone G., Cossette P., Saftig P., Groetzinger J.,
RA Schwake M., Andermann F., Staropoli J.F., Sims K.B., Mole S.E.,
RA Franceschetti S., Alexander N.A., Cooper J.D., Chapman H.A., Carpenter S.,
RA Berkovic S.F., Bahlo M.;
RT "Cathepsin F mutations cause Type B Kufs disease, an adult-onset neuronal
RT ceroid lipofuscinosis.";
RL Hum. Mol. Genet. 22:1417-1423(2013).
CC -!- FUNCTION: Thiol protease which is believed to participate in
CC intracellular degradation and turnover of proteins. Has also been
CC implicated in tumor invasion and metastasis.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=The recombinant enzyme cleaves synthetic substrates with Phe
CC and Leu (better than Val) in P2, with high specificity constant
CC (kcat/Km) comparable to that of cathepsin L.; EC=3.4.22.41;
CC -!- SUBCELLULAR LOCATION: Lysosome.
CC -!- TISSUE SPECIFICITY: High expression levels in heart, skeletal muscle,
CC brain, testis and ovary; moderate levels in prostate, placenta, liver
CC and colon; and no detectable expression in peripheral leukocytes and
CC thymus.
CC -!- DISEASE: Ceroid lipofuscinosis, neuronal, 13 (Kufs type) (CLN13)
CC [MIM:615362]: A form of neuronal ceroid lipofuscinosis characterized by
CC adult onset of progressive cognitive decline and motor dysfunction
CC leading to dementia and often early death. Some patients develop
CC seizures. Neuronal ceroid lipofuscinoses are progressive
CC neurodegenerative, lysosomal storage diseases characterized by
CC intracellular accumulation of autofluorescent liposomal material. CLN13
CC inheritance is autosomal recessive. {ECO:0000269|PubMed:23297359}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089}.
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; AJ007331; CAB42883.1; -; mRNA.
DR EMBL; AF088886; AAD26616.2; -; mRNA.
DR EMBL; AF132894; AAD41790.1; -; Genomic_DNA.
DR EMBL; AF136279; AAF13146.1; -; mRNA.
DR EMBL; AF071748; AAC78838.1; -; mRNA.
DR EMBL; AF071749; AAC78839.1; -; mRNA.
DR EMBL; AK313657; BAG36411.1; -; mRNA.
DR EMBL; BC011682; AAH11682.1; -; mRNA.
DR EMBL; BC036451; AAH36451.1; -; mRNA.
DR EMBL; AL137742; CAB70900.1; -; mRNA.
DR CCDS; CCDS8144.1; -.
DR RefSeq; NP_003784.2; NM_003793.3.
DR PDB; 1M6D; X-ray; 1.70 A; A/B=271-484.
DR PDBsum; 1M6D; -.
DR AlphaFoldDB; Q9UBX1; -.
DR SMR; Q9UBX1; -.
DR BioGRID; 114261; 42.
DR IntAct; Q9UBX1; 8.
DR STRING; 9606.ENSP00000310832; -.
DR BindingDB; Q9UBX1; -.
DR ChEMBL; CHEMBL2517; -.
DR DrugBank; DB02243; 4-Morpholin-4-Yl-Piperidine-1-Carboxylic Acid [1-(3-Benzenesulfonyl-1-Propyl-Allylcarbamoyl)-2-Phenylethyl]-Amide.
DR DrugBank; DB01871; [1-(1-Benzyl-3-Hydroxy-2-Oxo-Propylcarbamoyl)-2-Phenyl-Ethyl]-Carbamic Acid Benzyl Ester.
DR DrugBank; DB01810; [1-(1-Methyl-4,5-Dioxo-Pent-2-Enylcarbamoyl)-2-Phenyl-Ethyl]-Carbamic Acid Benzyl Ester.
DR DrugBank; DB08775; Benzoyl-tyrosine-alanine-fluoro-methyl ketone.
DR DrugBank; DB03536; Benzyl N-[(2S)-5-(diaminomethylamino)-1-[[(2S)-4-fluoro-3-oxobutan-2-yl]amino]-1-oxopentan-2-yl]carbamate.
DR DrugBank; DB07913; HOMOPHENYLALANINYLMETHANE.
DR DrugBank; DB03691; WRR-112.
DR DrugBank; DB03573; WRR-99.
DR DrugCentral; Q9UBX1; -.
DR GuidetoPHARMACOLOGY; 2347; -.
DR MEROPS; C01.018; -.
DR GlyConnect; 1080; 4 N-Linked glycans (2 sites).
DR GlyGen; Q9UBX1; 5 sites, 3 N-linked glycans (2 sites).
DR iPTMnet; Q9UBX1; -.
DR PhosphoSitePlus; Q9UBX1; -.
DR BioMuta; CTSF; -.
DR DMDM; 12643325; -.
DR EPD; Q9UBX1; -.
DR jPOST; Q9UBX1; -.
DR MassIVE; Q9UBX1; -.
DR MaxQB; Q9UBX1; -.
DR PaxDb; Q9UBX1; -.
DR PeptideAtlas; Q9UBX1; -.
DR PRIDE; Q9UBX1; -.
DR ProteomicsDB; 84089; -.
DR Antibodypedia; 30202; 288 antibodies from 34 providers.
DR DNASU; 8722; -.
DR Ensembl; ENST00000310325.10; ENSP00000310832.5; ENSG00000174080.12.
DR GeneID; 8722; -.
DR KEGG; hsa:8722; -.
DR MANE-Select; ENST00000310325.10; ENSP00000310832.5; NM_003793.4; NP_003784.2.
DR UCSC; uc001oip.4; human.
DR CTD; 8722; -.
DR DisGeNET; 8722; -.
DR GeneCards; CTSF; -.
DR HGNC; HGNC:2531; CTSF.
DR HPA; ENSG00000174080; Low tissue specificity.
DR MalaCards; CTSF; -.
DR MIM; 603539; gene.
DR MIM; 615362; phenotype.
DR neXtProt; NX_Q9UBX1; -.
DR OpenTargets; ENSG00000174080; -.
DR Orphanet; 352709; CLN13 disease.
DR PharmGKB; PA27031; -.
DR VEuPathDB; HostDB:ENSG00000174080; -.
DR eggNOG; KOG1542; Eukaryota.
DR GeneTree; ENSGT00940000162141; -.
DR HOGENOM; CLU_012184_10_0_1; -.
DR InParanoid; Q9UBX1; -.
DR OMA; RGHMQAC; -.
DR OrthoDB; 1264766at2759; -.
DR PhylomeDB; Q9UBX1; -.
DR TreeFam; TF314550; -.
DR BRENDA; 3.4.22.41; 2681.
DR PathwayCommons; Q9UBX1; -.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR SignaLink; Q9UBX1; -.
DR BioGRID-ORCS; 8722; 28 hits in 1082 CRISPR screens.
DR ChiTaRS; CTSF; human.
DR EvolutionaryTrace; Q9UBX1; -.
DR GeneWiki; Cathepsin_F; -.
DR GenomeRNAi; 8722; -.
DR Pharos; Q9UBX1; Tchem.
DR PRO; PR:Q9UBX1; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9UBX1; protein.
DR Bgee; ENSG00000174080; Expressed in right hemisphere of cerebellum and 205 other tissues.
DR ExpressionAtlas; Q9UBX1; baseline and differential.
DR Genevisible; Q9UBX1; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0006508; P:proteolysis; TAS:ProtInc.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disease variant; Disulfide bond; Glycoprotein; Hydrolase;
KW Lysosome; Neurodegeneration; Neuronal ceroid lipofuscinosis; Protease;
KW Reference proteome; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..270
FT /note="Activation peptide"
FT /id="PRO_0000026202"
FT CHAIN 271..484
FT /note="Cathepsin F"
FT /id="PRO_0000026203"
FT ACT_SITE 295
FT /evidence="ECO:0000269|PubMed:12225749"
FT ACT_SITE 431
FT /evidence="ECO:0000269|PubMed:12225749"
FT ACT_SITE 451
FT /evidence="ECO:0000250"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT DISULFID 292..333
FT /evidence="ECO:0000269|PubMed:12225749"
FT DISULFID 326..366
FT /evidence="ECO:0000269|PubMed:12225749"
FT DISULFID 424..472
FT /evidence="ECO:0000250"
FT VARIANT 153
FT /note="Q -> R (in dbSNP:rs11550508)"
FT /id="VAR_051513"
FT VARIANT 231
FT /note="Y -> C (in CLN13; dbSNP:rs143889283)"
FT /evidence="ECO:0000269|PubMed:23297359"
FT /id="VAR_070159"
FT VARIANT 321
FT /note="Q -> R (in CLN13; dbSNP:rs397514731)"
FT /evidence="ECO:0000269|PubMed:23297359"
FT /id="VAR_070160"
FT VARIANT 458
FT /note="G -> A (in CLN13; dbSNP:rs397514732)"
FT /evidence="ECO:0000269|PubMed:23297359"
FT /id="VAR_070161"
FT VARIANT 480
FT /note="S -> L (in CLN13; dbSNP:rs397514733)"
FT /evidence="ECO:0000269|PubMed:23297359"
FT /id="VAR_070162"
FT CONFLICT 305
FT /note="E -> K (in Ref. 5; AAF13146)"
FT /evidence="ECO:0000305"
FT CONFLICT 442..484
FT /note="SDVPFWAIKNSWGTDWGEKGYYYLHRGSGACGVNTMASSAVVD -> EFRCL
FT SCIQPGHRQGWDHSISGPLEGK (in Ref. 9)"
FT /evidence="ECO:0000305"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:1M6D"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:1M6D"
FT HELIX 295..312
FT /evidence="ECO:0007829|PDB:1M6D"
FT HELIX 320..326
FT /evidence="ECO:0007829|PDB:1M6D"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:1M6D"
FT HELIX 338..348
FT /evidence="ECO:0007829|PDB:1M6D"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:1M6D"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:1M6D"
FT STRAND 378..382
FT /evidence="ECO:0007829|PDB:1M6D"
FT HELIX 387..397
FT /evidence="ECO:0007829|PDB:1M6D"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:1M6D"
FT HELIX 407..411
FT /evidence="ECO:0007829|PDB:1M6D"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:1M6D"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:1M6D"
FT STRAND 431..441
FT /evidence="ECO:0007829|PDB:1M6D"
FT STRAND 444..450
FT /evidence="ECO:0007829|PDB:1M6D"
FT STRAND 462..469
FT /evidence="ECO:0007829|PDB:1M6D"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:1M6D"
FT TURN 474..477
FT /evidence="ECO:0007829|PDB:1M6D"
FT STRAND 479..482
FT /evidence="ECO:0007829|PDB:1M6D"
SQ SEQUENCE 484 AA; 53366 MW; 1D5D551B489D822B CRC64;
MAPWLQLLSL LGLLPGAVAA PAQPRAASFQ AWGPPSPELL APTRFALEMF NRGRAAGTRA
VLGLVRGRVR RAGQGSLYSL EATLEEPPCN DPMVCRLPVS KKTLLCSFQV LDELGRHVLL
RKDCGPVDTK VPGAGEPKSA FTQGSAMISS LSQNHPDNRN ETFSSVISLL NEDPLSQDLP
VKMASIFKNF VITYNRTYES KEEARWRLSV FVNNMVRAQK IQALDRGTAQ YGVTKFSDLT
EEEFRTIYLN TLLRKEPGNK MKQAKSVGDL APPEWDWRSK GAVTKVKDQG MCGSCWAFSV
TGNVEGQWFL NQGTLLSLSE QELLDCDKMD KACMGGLPSN AYSAIKNLGG LETEDDYSYQ
GHMQSCNFSA EKAKVYINDS VELSQNEQKL AAWLAKRGPI SVAINAFGMQ FYRHGISRPL
RPLCSPWLID HAVLLVGYGN RSDVPFWAIK NSWGTDWGEK GYYYLHRGSG ACGVNTMASS
AVVD
