ID CBPM_HUMAN Reviewed; 443 AA. AC P14384; B2R800; Q9H2K9; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2001, sequence version 2. DT 27-MAR-2024, entry version 218. DE RecName: Full=Carboxypeptidase M; DE Short=CPM; DE EC=3.4.17.12 {ECO:0000269|PubMed:12457462}; DE Flags: Precursor; GN Name=CPM; 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], AND PROTEIN SEQUENCE OF 18-48. RC TISSUE=Placenta; RX PubMed=2753907; DOI=10.1016/s0021-9258(18)51610-0; RA Tan F., Chan S.J., Steiner D.F., Schilling J.W., Skidgel R.A.; RT "Molecular cloning and sequencing of the cDNA for human membrane-bound RT carboxypeptidase M. Comparison with carboxypeptidases A, B, H, and N."; RL J. Biol. Chem. 264:13165-13170(1989). RN [2] RP SEQUENCE REVISION. RA Skidgel R.A.; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11147789; DOI=10.2337/diabetes.50.1.204; RA Bektas A., Hughes J.N., Warram J.H., Krolewski A.S., Doria A.; RT "Type 2 diabetes locus on 12q15: further mapping and mutation screening of RT two candidate genes."; RL Diabetes 50:204-208(2001). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=11934264; DOI=10.1515/bc.2002.028; RA Pessoa L.G., Guerreiro da S.I., Baptista H.A., Pesquero J.L., Paiva A.C.M., RA Bader M., Pesquero J.B.; RT "Molecular structure and alternative splicing of the human carboxypeptidase RT M gene."; RL Biol. Chem. 383:263-269(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; 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 [7] RP PROTEIN SEQUENCE OF 18-21, GPI-ANCHOR AT SER-423, BIOPHYSICOCHEMICAL RP PROPERTIES, FUNCTION, CATALYTIC ACTIVITY, SITE, SUBCELLULAR LOCATION, RP IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF GLU-277; GLU-281 RP AND SER-423. RX PubMed=12457462; DOI=10.1042/bj20021495; RA Tan F., Balsitis S., Black J.K., Bloechl A., Mao J.-F., Becker R.P., RA Schacht D., Skidgel R.A.; RT "Effect of mutation of two critical glutamic acid residues on the activity RT and stability of human carboxypeptidase M and characterization of its RT signal for glycosylphosphatidylinositol anchoring."; RL Biochem. J. 370:567-578(2003). RN [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-115 AND ASN-164. 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 [9] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 18-443 IN COMPLEX WITH ZINC IONS, RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-38 AND ASN-115. RX PubMed=15066430; DOI=10.1016/j.jmb.2004.02.058; RA Reverter D., Maskos K., Tan F., Skidgel R.A., Bode W.; RT "Crystal structure of human carboxypeptidase M, a membrane-bound enzyme RT that regulates peptide hormone activity."; RL J. Mol. Biol. 338:257-269(2004). CC -!- FUNCTION: Specifically removes C-terminal basic residues (Arg or Lys) CC from peptides and proteins. It is believed to play important roles in CC the control of peptide hormone and growth factor activity at the cell CC surface, and in the membrane-localized degradation of extracellular CC proteins. {ECO:0000269|PubMed:12457462}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Cleavage of C-terminal arginine or lysine residues from CC polypeptides.; EC=3.4.17.12; Evidence={ECO:0000269|PubMed:12457462}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:15066430}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:15066430}; CC -!- ACTIVITY REGULATION: Inhibited by O-phenanthroline and MGTA and CC activated by cobalt. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=59 uM for synthetic dansyl-Ala-Arg {ECO:0000269|PubMed:12457462}; CC KM=57 uM for placental peptide hormones CC {ECO:0000269|PubMed:12457462}; CC pH dependence: CC Optimum pH is 7.0. {ECO:0000269|PubMed:12457462}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12457462}; CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12457462}. CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}. 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; J04970; AAA35651.2; -; mRNA. DR EMBL; AF262947; AAG47641.1; -; Genomic_DNA. DR EMBL; AF262940; AAG47641.1; JOINED; Genomic_DNA. DR EMBL; AF262941; AAG47641.1; JOINED; Genomic_DNA. DR EMBL; AF262942; AAG47641.1; JOINED; Genomic_DNA. DR EMBL; AF262943; AAG47641.1; JOINED; Genomic_DNA. DR EMBL; AF262944; AAG47641.1; JOINED; Genomic_DNA. DR EMBL; AF262945; AAG47641.1; JOINED; Genomic_DNA. DR EMBL; AF262946; AAG47641.1; JOINED; Genomic_DNA. DR EMBL; AF368463; AAK69717.1; -; mRNA. DR EMBL; AK313180; BAG35997.1; -; mRNA. DR EMBL; BC022276; AAH22276.1; -; mRNA. DR CCDS; CCDS8987.1; -. DR PIR; A32619; A32619. DR RefSeq; NP_001005502.1; NM_001005502.2. DR RefSeq; NP_001865.1; NM_001874.4. DR RefSeq; NP_938079.1; NM_198320.3. DR PDB; 1UWY; X-ray; 3.00 A; A=18-443. DR PDBsum; 1UWY; -. DR AlphaFoldDB; P14384; -. DR SMR; P14384; -. DR BioGRID; 107760; 60. DR IntAct; P14384; 37. DR STRING; 9606.ENSP00000339157; -. DR BindingDB; P14384; -. DR ChEMBL; CHEMBL3038; -. DR GuidetoPHARMACOLOGY; 1596; -. DR MEROPS; M14.006; -. DR GlyCosmos; P14384; 5 sites, No reported glycans. DR GlyGen; P14384; 8 sites, 1 O-linked glycan (1 site). DR iPTMnet; P14384; -. DR PhosphoSitePlus; P14384; -. DR SwissPalm; P14384; -. DR BioMuta; CPM; -. DR DMDM; 14916957; -. DR EPD; P14384; -. DR jPOST; P14384; -. DR MassIVE; P14384; -. DR MaxQB; P14384; -. DR PaxDb; 9606-ENSP00000448517; -. DR PeptideAtlas; P14384; -. DR ProteomicsDB; 53049; -. DR Pumba; P14384; -. DR Antibodypedia; 975; 410 antibodies from 35 providers. DR DNASU; 1368; -. DR Ensembl; ENST00000338356.7; ENSP00000339157.3; ENSG00000135678.12. DR Ensembl; ENST00000546373.5; ENSP00000447255.1; ENSG00000135678.12. DR Ensembl; ENST00000551568.6; ENSP00000448517.1; ENSG00000135678.12. DR GeneID; 1368; -. DR KEGG; hsa:1368; -. DR MANE-Select; ENST00000551568.6; ENSP00000448517.1; NM_198320.5; NP_938079.1. DR UCSC; uc001sup.4; human. DR AGR; HGNC:2311; -. DR CTD; 1368; -. DR DisGeNET; 1368; -. DR GeneCards; CPM; -. DR HGNC; HGNC:2311; CPM. DR HPA; ENSG00000135678; Tissue enhanced (adipose). DR MIM; 114860; gene. DR neXtProt; NX_P14384; -. DR OpenTargets; ENSG00000135678; -. DR PharmGKB; PA26828; -. DR VEuPathDB; HostDB:ENSG00000135678; -. DR eggNOG; KOG2649; Eukaryota. DR GeneTree; ENSGT00940000158580; -. DR HOGENOM; CLU_006722_1_0_1; -. DR InParanoid; P14384; -. DR OMA; FSYHHQE; -. DR OrthoDB; 5490979at2759; -. DR PhylomeDB; P14384; -. DR TreeFam; TF315592; -. DR BRENDA; 3.4.17.12; 2681. DR PathwayCommons; P14384; -. DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins. DR SABIO-RK; P14384; -. DR SignaLink; P14384; -. DR SIGNOR; P14384; -. DR BioGRID-ORCS; 1368; 16 hits in 1167 CRISPR screens. DR ChiTaRS; CPM; human. DR EvolutionaryTrace; P14384; -. DR GeneWiki; CPM_(gene); -. DR GenomeRNAi; 1368; -. DR Pharos; P14384; Tchem. DR PRO; PR:P14384; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P14384; Protein. DR Bgee; ENSG00000135678; Expressed in lower lobe of lung and 183 other cell types or tissues. DR ExpressionAtlas; P14384; baseline and differential. DR GO; GO:0009986; C:cell surface; HDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW. DR GO; GO:0004180; F:carboxypeptidase activity; TAS:ProtInc. DR GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc. DR GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central. DR GO; GO:0016485; P:protein processing; IBA:GO_Central. DR CDD; cd03866; M14_CPM; 1. DR CDD; cd11308; Peptidase_M14NE-CP-C_like; 1. DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1. DR Gene3D; 3.40.630.10; Zn peptidases; 1. DR InterPro; IPR008969; CarboxyPept-like_regulatory. DR InterPro; IPR033842; CPM_N. DR InterPro; IPR000834; Peptidase_M14. DR PANTHER; PTHR11532:SF84; CARBOXYPEPTIDASE M; 1. DR PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 1. DR Pfam; PF13620; CarboxypepD_reg; 1. DR Pfam; PF00246; Peptidase_M14; 1. DR PRINTS; PR00765; CRBOXYPTASEA. DR SMART; SM00631; Zn_pept; 1. DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1. DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1. DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1. DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1. DR PROSITE; PS52035; PEPTIDASE_M14; 1. DR Genevisible; P14384; HS. PE 1: Evidence at protein level; KW 3D-structure; Carboxypeptidase; Cell membrane; Direct protein sequencing; KW Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane; KW Metal-binding; Metalloprotease; Protease; Reference proteome; Signal; Zinc. FT SIGNAL 1..17 FT /evidence="ECO:0000269|PubMed:12457462, FT ECO:0000269|PubMed:2753907" FT CHAIN 18..423 FT /note="Carboxypeptidase M" FT /id="PRO_0000004391" FT PROPEP 424..443 FT /note="Removed in mature form" FT /evidence="ECO:0000305" FT /id="PRO_0000251910" FT DOMAIN 21..311 FT /note="Peptidase M14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01379" FT ACT_SITE 281 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01379, FT ECO:0000305|PubMed:12457462" FT BINDING 83 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01379, FT ECO:0000269|PubMed:15066430, ECO:0007744|PDB:1UWY" FT BINDING 86 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01379, FT ECO:0000269|PubMed:15066430, ECO:0007744|PDB:1UWY" FT BINDING 190 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01379, FT ECO:0000269|PubMed:15066430, ECO:0007744|PDB:1UWY" FT SITE 277 FT /note="Probable structural role" FT /evidence="ECO:0000305|PubMed:12457462" FT LIPID 423 FT /note="GPI-anchor amidated serine" FT /evidence="ECO:0000269|PubMed:12457462" FT CARBOHYD 38 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:15066430" FT CARBOHYD 115 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:15066430, FT ECO:0000269|PubMed:19159218, ECO:0007744|PDB:1UWY" FT CARBOHYD 164 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 363 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 384 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 138..285 FT /evidence="ECO:0000269|PubMed:15066430, FT ECO:0007744|PDB:1UWY" FT DISULFID 242..284 FT /evidence="ECO:0000269|PubMed:15066430, FT ECO:0007744|PDB:1UWY" FT DISULFID 341..410 FT /evidence="ECO:0000269|PubMed:15066430, FT ECO:0007744|PDB:1UWY" FT VARIANT 24 FT /note="R -> H (in dbSNP:rs7978197)" FT /id="VAR_048600" FT VARIANT 133 FT /note="V -> I (in dbSNP:rs7309831)" FT /id="VAR_048601" FT MUTAGEN 277 FT /note="E->A: 5-fold decrease in substrate affinity. 22-fold FT decrease in specific affinity. 104-fold decrease in FT catalytic efficiency. Greatly reduced heat stability." FT /evidence="ECO:0000269|PubMed:12457462" FT MUTAGEN 277 FT /note="E->Q: 2-fold decrease in substrate affinity. Small FT increase in specific affinity. Reduced heat stability by FT 50%." FT /evidence="ECO:0000269|PubMed:12457462" FT MUTAGEN 281 FT /note="E->Q: Abolishes enzyme activity." FT /evidence="ECO:0000269|PubMed:12457462" FT MUTAGEN 423 FT /note="S->A,T: Expressed on cell membrane. Released from FT membrane by PI-PLC." FT /evidence="ECO:0000269|PubMed:12457462" FT MUTAGEN 423 FT /note="S->P: Little expression on cell membrane. FT Perinuclear localization. Not released from membrane by FT PI-PLC." FT /evidence="ECO:0000269|PubMed:12457462" FT HELIX 25..38 FT /evidence="ECO:0007829|PDB:1UWY" FT TURN 39..41 FT /evidence="ECO:0007829|PDB:1UWY" FT STRAND 42..50 FT /evidence="ECO:0007829|PDB:1UWY" FT STRAND 56..65 FT /evidence="ECO:0007829|PDB:1UWY" FT STRAND 75..80 FT /evidence="ECO:0007829|PDB:1UWY" FT HELIX 88..103 FT /evidence="ECO:0007829|PDB:1UWY" FT TURN 104..106 FT /evidence="ECO:0007829|PDB:1UWY" FT HELIX 108..116 FT /evidence="ECO:0007829|PDB:1UWY" FT STRAND 118..123 FT /evidence="ECO:0007829|PDB:1UWY" FT HELIX 127..132 FT /evidence="ECO:0007829|PDB:1UWY" FT STRAND 159..161 FT /evidence="ECO:0007829|PDB:1UWY" FT HELIX 169..180 FT /evidence="ECO:0007829|PDB:1UWY" FT STRAND 183..185 FT /evidence="ECO:0007829|PDB:1UWY" FT STRAND 188..190 FT /evidence="ECO:0007829|PDB:1UWY" FT STRAND 192..199 FT /evidence="ECO:0007829|PDB:1UWY" FT HELIX 205..207 FT /evidence="ECO:0007829|PDB:1UWY" FT HELIX 209..211 FT /evidence="ECO:0007829|PDB:1UWY" FT HELIX 219..231 FT /evidence="ECO:0007829|PDB:1UWY" FT TURN 234..238 FT /evidence="ECO:0007829|PDB:1UWY" FT STRAND 243..245 FT /evidence="ECO:0007829|PDB:1UWY" FT STRAND 252..255 FT /evidence="ECO:0007829|PDB:1UWY" FT TURN 256..258 FT /evidence="ECO:0007829|PDB:1UWY" FT HELIX 265..271 FT /evidence="ECO:0007829|PDB:1UWY" FT STRAND 279..287 FT /evidence="ECO:0007829|PDB:1UWY" FT HELIX 290..292 FT /evidence="ECO:0007829|PDB:1UWY" FT HELIX 293..298 FT /evidence="ECO:0007829|PDB:1UWY" FT HELIX 301..308 FT /evidence="ECO:0007829|PDB:1UWY" FT HELIX 309..312 FT /evidence="ECO:0007829|PDB:1UWY" FT STRAND 314..320 FT /evidence="ECO:0007829|PDB:1UWY" FT STRAND 331..334 FT /evidence="ECO:0007829|PDB:1UWY" FT STRAND 350..353 FT /evidence="ECO:0007829|PDB:1UWY" FT STRAND 357..365 FT /evidence="ECO:0007829|PDB:1UWY" FT STRAND 367..369 FT /evidence="ECO:0007829|PDB:1UWY" FT STRAND 372..378 FT /evidence="ECO:0007829|PDB:1UWY" FT STRAND 383..386 FT /evidence="ECO:0007829|PDB:1UWY" FT TURN 415..418 FT /evidence="ECO:0007829|PDB:1UWY" SQ SEQUENCE 443 AA; 50514 MW; 98EB0C94E201B901 CRC64; MDFPCLWLGL LLPLVAALDF NYHRQEGMEA FLKTVAQNYS SVTHLHSIGK SVKGRNLWVL VVGRFPKEHR IGIPEFKYVA NMHGDETVGR ELLLHLIDYL VTSDGKDPEI TNLINSTRIH IMPSMNPDGF EAVKKPDCYY SIGRENYNQY DLNRNFPDAF EYNNVSRQPE TVAVMKWLKT ETFVLSANLH GGALVASYPF DNGVQATGAL YSRSLTPDDD VFQYLAHTYA SRNPNMKKGD ECKNKMNFPN GVTNGYSWYP LQGGMQDYNY IWAQCFEITL ELSCCKYPRE EKLPSFWNNN KASLIEYIKQ VHLGVKGQVF DQNGNPLPNV IVEVQDRKHI CPYRTNKYGE YYLLLLPGSY IINVTVPGHD PHITKVIIPE KSQNFSALKK DILLPFQGQL DSIPVSNPSC PMIPLYRNLP DHSAATKPSL FLFLVSLLHI FFK //