ID   CD36_BOVIN              Reviewed;         472 AA.
AC   P26201; P79111; Q28154; Q3ZBT7;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 5.
DT   24-JAN-2024, entry version 167.
DE   RecName: Full=Platelet glycoprotein 4;
DE   AltName: Full=Glycoprotein IIIb;
DE            Short=GPIIIB;
DE   AltName: Full=PAS IV;
DE   AltName: Full=PAS-4;
DE   AltName: Full=Platelet glycoprotein IV;
DE            Short=GPIV;
DE   AltName: CD_antigen=CD36;
GN   Name=CD36; Synonyms=PAS4;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Holstein; TISSUE=Mammary gland;
RA   Hwangbo S., Ametani M., Kanno C.;
RT   "cDNA cloning of PAS-4 from bovine fat globule membrane.";
RL   Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND GLYCOSYLATION AT ASN-79; ASN-102; ASN-172;
RP   ASN-205; ASN-235; ASN-247; ASN-321 AND ASN-417.
RC   TISSUE=Mammary gland;
RX   PubMed=8950178; DOI=10.1016/s0167-4781(96)00143-1;
RA   Berglund L., Petersen T.E., Ramussen J.T.;
RT   "Structural characterization of bovine CD36 from the milk fat globule
RT   membrane.";
RL   Biochim. Biophys. Acta 1309:63-68(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 2-22, AND FUNCTION.
RC   TISSUE=Heart;
RX   PubMed=1697855; DOI=10.1016/s0021-9258(17)46221-1;
RA   Greenwalt D.E., Watt K.W.K., Hasler T., Howard R.J., Patel S.;
RT   "Structural, functional, and antigenic differences between bovine heart
RT   endothelial CD36 and human platelet CD36.";
RL   J. Biol. Chem. 265:16296-16299(1990).
RN   [5]
RP   PROTEIN SEQUENCE OF 4-22 AND 214-223.
RC   TISSUE=Mammary epithelium;
RX   PubMed=1699598; DOI=10.1021/bi00482a015;
RA   Greenwalt D.E., Watt K.W., So O.Y., Jiwani N.;
RT   "PAS IV, an integral membrane protein of mammary epithelial cells, is
RT   related to platelet and endothelial cell CD36 (GP IV).";
RL   Biochemistry 29:7054-7059(1990).
RN   [6]
RP   DISULFIDE BONDS.
RC   TISSUE=Milk;
RX   PubMed=9826197; DOI=10.1046/j.1432-1327.1998.2570488.x;
RA   Rasmussen J.T., Berglund L., Rasmussen M.S., Petersen T.E.;
RT   "Assignment of disulfide bridges in bovine CD36.";
RL   Eur. J. Biochem. 257:488-494(1998).
CC   -!- FUNCTION: Multifunctional glycoprotein that acts as a receptor for a
CC       broad range of ligands. Ligands can be of proteinaceous nature like
CC       thrombospondin, fibronectin, collagen or amyloid-beta as well as of
CC       lipidic nature such as oxidized low-density lipoprotein (oxLDL),
CC       anionic phospholipids, long-chain fatty acids and bacterial diacylated
CC       lipopeptides. They are generally multivalent and can therefore engage
CC       multiple receptors simultaneously, the resulting formation of CD36
CC       clusters initiates signal transduction and internalization of receptor-
CC       ligand complexes. The dependency on coreceptor signaling is strongly
CC       ligand specific. Cellular responses to these ligands are involved in
CC       angiogenesis, inflammatory response, fatty acid metabolism, taste and
CC       dietary fat processing in the intestine (By similarity). Binds long-
CC       chain fatty acids and facilitates their transport into cells, thus
CC       participating in muscle lipid utilization, adipose energy storage, and
CC       gut fat absorption (By similarity). Mechanistically, binding of fatty
CC       acids activates downstream kinase LYN, which phosphorylates the
CC       palmitoyltransferase ZDHHC5 and inactivates it, resulting in the
CC       subsequent depalmitoylation of CD36 and caveolar endocytosis (By
CC       similarity). In the small intestine, plays a role in proximal
CC       absorption of dietary fatty acid and cholesterol for optimal
CC       chylomicron formation, possibly through the activation of MAPK1/3
CC       (ERK1/2) signaling pathway (By similarity). Involved in oral fat
CC       perception and preferences (By similarity). Detection into the tongue
CC       of long-chain fatty acids leads to a rapid and sustained rise in flux
CC       and protein content of pancreatobiliary secretions (By similarity). In
CC       taste receptor cells, mediates the induction of an increase in
CC       intracellular calcium levels by long-chain fatty acids, leading to the
CC       activation of the gustatory neurons in the nucleus of the solitary
CC       tract (By similarity). Important factor in both ventromedial
CC       hypothalamus neuronal sensing of long-chain fatty acid and the
CC       regulation of energy and glucose homeostasis (By similarity). Receptor
CC       for thrombospondins, THBS1 and THBS2, mediating their antiangiogenic
CC       effects (By similarity). As a coreceptor for TLR4:TLR6 heterodimer,
CC       promotes inflammation in monocytes/macrophages. Upon ligand binding,
CC       such as oxLDL or amyloid-beta 42, interacts with the heterodimer
CC       TLR4:TLR6, the complex is internalized and triggers inflammatory
CC       response, leading to NF-kappa-B-dependent production of CXCL1, CXCL2
CC       and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via
CC       TICAM1 signaling pathway, as well as IL1B secretion, through the
CC       priming and activation of the NLRP3 inflammasome. Selective and
CC       nonredundant sensor of microbial diacylated lipopeptide that signal via
CC       TLR2:TLR6 heterodimer, this cluster triggers signaling from the cell
CC       surface, leading to the NF-kappa-B-dependent production of TNF, via
CC       MYD88 signaling pathway and subsequently is targeted to the Golgi in a
CC       lipid-raft dependent pathway (By similarity).
CC       {ECO:0000250|UniProtKB:P16671, ECO:0000250|UniProtKB:Q07969,
CC       ECO:0000250|UniProtKB:Q08857}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=butanoate(out) = butanoate(in); Xref=Rhea:RHEA:45248,
CC         ChEBI:CHEBI:17968; Evidence={ECO:0000250|UniProtKB:P16671};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45249;
CC         Evidence={ECO:0000250|UniProtKB:P16671};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoate(out) = (9Z)-octadecenoate(in);
CC         Xref=Rhea:RHEA:33655, ChEBI:CHEBI:30823;
CC         Evidence={ECO:0000250|UniProtKB:P16671};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33656;
CC         Evidence={ECO:0000250|UniProtKB:P16671};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoate(out) = (9Z,12Z)-
CC         octadecadienoate(in); Xref=Rhea:RHEA:45264, ChEBI:CHEBI:30245;
CC         Evidence={ECO:0000250|UniProtKB:P16671};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45265;
CC         Evidence={ECO:0000250|UniProtKB:P16671};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tetradecanoate(out) = tetradecanoate(in);
CC         Xref=Rhea:RHEA:45252, ChEBI:CHEBI:30807;
CC         Evidence={ECO:0000250|UniProtKB:P16671};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45253;
CC         Evidence={ECO:0000250|UniProtKB:P16671};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexadecanoate(out) = hexadecanoate(in); Xref=Rhea:RHEA:45256,
CC         ChEBI:CHEBI:7896; Evidence={ECO:0000250|UniProtKB:P16671};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45257;
CC         Evidence={ECO:0000250|UniProtKB:P16671};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tetracosanoate(out) = tetracosanoate(in);
CC         Xref=Rhea:RHEA:45260, ChEBI:CHEBI:31014;
CC         Evidence={ECO:0000250|UniProtKB:P16671};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45261;
CC         Evidence={ECO:0000250|UniProtKB:P16671};
CC   -!- SUBUNIT: Interacts with THBS1 and THBS2; the interactions mediate the
CC       THBS antiangiogenic activity. Upon interaction with a ligand, such as
CC       oxidized low-density lipoprotein (oxLDL) or amyloid-beta 42, rapidly
CC       forms a complex with TLR4 and TLR6; the complex is internalized and
CC       triggers an inflammatory signal. Through its C-terminus, interacts with
CC       PTK2, PXN and LYN, but not with SRC. LYN kinase activity is required
CC       for facilitating TLR4:TLR6 heterodimerization and signal initiation.
CC       Upon interaction with ligands such as diacylated lipopeptides,
CC       interacts with the TLR2:TLR6 heterodimer (By similarity). Interacts
CC       with CD9, CD81, FCER1G, ITGB2 and/or ITGB2; forming a membrane
CC       heteromeric complex required for the internalization of CD36 and its
CC       ligands (By similarity). Interacts (when palmitoylated) with ARF6; this
CC       interaction mediates CD36 transport to the plasma membrane (By
CC       similarity). {ECO:0000250|UniProtKB:P16671,
CC       ECO:0000250|UniProtKB:Q08857}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P16671};
CC       Multi-pass membrane protein {ECO:0000255}. Membrane raft
CC       {ECO:0000250|UniProtKB:P16671}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:P16671}. Apical cell membrane
CC       {ECO:0000250|UniProtKB:Q08857}. Note=Upon ligand-binding, internalized
CC       through dynamin-dependent endocytosis. {ECO:0000250|UniProtKB:P16671}.
CC   -!- PTM: Palmitoylated by ZDHHC5. Palmitoylation is required for proper
CC       localization at the plasma membrane. {ECO:0000250|UniProtKB:P16671}.
CC   -!- PTM: Ubiquitinated at Lys-469. Ubiquitination is induced by fatty acids
CC       such as oleic acid and leads to degradation by the proteasome.
CC       Ubiquitination and degradation are inhibited by insulin which blocks
CC       the effect of fatty acids. {ECO:0000250|UniProtKB:P16671,
CC       ECO:0000250|UniProtKB:Q08857}.
CC   -!- SIMILARITY: Belongs to the CD36 family. {ECO:0000305}.
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DR   EMBL; D45364; BAA08224.1; -; mRNA.
DR   EMBL; X91503; CAA62803.1; -; mRNA.
DR   EMBL; BC103112; AAI03113.1; -; mRNA.
DR   RefSeq; NP_001265550.1; NM_001278621.1.
DR   RefSeq; NP_776435.2; NM_174010.3.
DR   RefSeq; XP_005205381.1; XM_005205324.3.
DR   RefSeq; XP_005205382.1; XM_005205325.3.
DR   RefSeq; XP_005205383.1; XM_005205326.3.
DR   RefSeq; XP_010802458.1; XM_010804156.2.
DR   RefSeq; XP_010802459.1; XM_010804157.2.
DR   RefSeq; XP_015324298.1; XM_015468812.1.
DR   RefSeq; XP_015324300.1; XM_015468814.1.
DR   RefSeq; XP_015324301.1; XM_015468815.1.
DR   RefSeq; XP_015324304.1; XM_015468818.1.
DR   AlphaFoldDB; P26201; -.
DR   SMR; P26201; -.
DR   STRING; 9913.ENSBTAP00000066341; -.
DR   CarbonylDB; P26201; -.
DR   GlyConnect; 506; 37 N-Linked glycans.
DR   GlyCosmos; P26201; 8 sites, 64 glycans.
DR   iPTMnet; P26201; -.
DR   SwissPalm; P26201; -.
DR   PaxDb; 9913-ENSBTAP00000023750; -.
DR   PeptideAtlas; P26201; -.
DR   Ensembl; ENSBTAT00000023750.6; ENSBTAP00000023750.5; ENSBTAG00000017866.6.
DR   Ensembl; ENSBTAT00000073723.1; ENSBTAP00000066341.1; ENSBTAG00000017866.6.
DR   Ensembl; ENSBTAT00000080828.1; ENSBTAP00000061478.1; ENSBTAG00000017866.6.
DR   GeneID; 281052; -.
DR   KEGG; bta:281052; -.
DR   CTD; 948; -.
DR   VEuPathDB; HostDB:ENSBTAG00000017866; -.
DR   eggNOG; KOG3776; Eukaryota.
DR   GeneTree; ENSGT00940000153372; -.
DR   HOGENOM; CLU_019853_0_0_1; -.
DR   InParanoid; P26201; -.
DR   OMA; AFQNWLV; -.
DR   OrthoDB; 315994at2759; -.
DR   TreeFam; TF317925; -.
DR   Reactome; R-BTA-114608; Platelet degranulation.
DR   Reactome; R-BTA-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
DR   Reactome; R-BTA-3000471; Scavenging by Class B Receptors.
DR   Reactome; R-BTA-434313; Intracellular metabolism of fatty acids regulates insulin secretion.
DR   Reactome; R-BTA-5686938; Regulation of TLR by endogenous ligand.
DR   Reactome; R-BTA-6798695; Neutrophil degranulation.
DR   Proteomes; UP000009136; Chromosome 4.
DR   Bgee; ENSBTAG00000017866; Expressed in omental fat pad and 103 other cell types or tissues.
DR   ExpressionAtlas; P26201; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
DR   GO; GO:0005901; C:caveola; IBA:GO_Central.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0030169; F:low-density lipoprotein particle binding; IBA:GO_Central.
DR   GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IBA:GO_Central.
DR   GO; GO:0005044; F:scavenger receptor activity; IBA:GO_Central.
DR   GO; GO:1990000; P:amyloid fibril formation; ISS:UniProtKB.
DR   GO; GO:0150094; P:amyloid-beta clearance by cellular catabolic process; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0071726; P:cellular response to diacyl bacterial lipopeptide; ISS:UniProtKB.
DR   GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
DR   GO; GO:0070508; P:cholesterol import; ISS:UniProtKB.
DR   GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
DR   GO; GO:0050892; P:intestinal absorption; ISS:UniProtKB.
DR   GO; GO:0030299; P:intestinal cholesterol absorption; ISS:UniProtKB.
DR   GO; GO:0019915; P:lipid storage; IBA:GO_Central.
DR   GO; GO:0042953; P:lipoprotein transport; IBA:GO_Central.
DR   GO; GO:0044539; P:long-chain fatty acid import into cell; ISS:UniProtKB.
DR   GO; GO:0034383; P:low-density lipoprotein particle clearance; IBA:GO_Central.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR   GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISS:UniProtKB.
DR   GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; ISS:UniProtKB.
DR   GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR   GO; GO:0070542; P:response to fatty acid; ISS:UniProtKB.
DR   GO; GO:0070543; P:response to linoleic acid; ISS:UniProtKB.
DR   GO; GO:0033993; P:response to lipid; ISS:UniProtKB.
DR   GO; GO:0050909; P:sensory perception of taste; ISS:UniProtKB.
DR   GO; GO:0034197; P:triglyceride transport; ISS:UniProtKB.
DR   InterPro; IPR005428; CD36/SCARB1/SNMP1.
DR   InterPro; IPR002159; CD36_fam.
DR   PANTHER; PTHR11923:SF12; PLATELET GLYCOPROTEIN 4; 1.
DR   PANTHER; PTHR11923; SCAVENGER RECEPTOR CLASS B TYPE-1 SR-B1; 1.
DR   Pfam; PF01130; CD36; 1.
DR   PRINTS; PR01610; CD36ANTIGEN.
DR   PRINTS; PR01609; CD36FAMILY.
PE   1: Evidence at protein level;
KW   Cell adhesion; Cell membrane; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Golgi apparatus; Isopeptide bond; Lipid transport;
KW   Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1697855"
FT   CHAIN           2..472
FT                   /note="Platelet glycoprotein 4"
FT                   /id="PRO_0000144150"
FT   TOPO_DOM        2..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        8..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..439
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        440..461
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        462..472
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          93..120
FT                   /note="Required for interaction with thrombospondins, THBS1
FT                   and THBS2"
FT   REGION          460..472
FT                   /note="Interaction with PTK2, PXN and LYN"
FT                   /evidence="ECO:0000250|UniProtKB:P16671"
FT   SITE            463
FT                   /note="Critical for TLR4-TLR6 dimerization and signaling"
FT                   /evidence="ECO:0000250|UniProtKB:P16671"
FT   LIPID           3
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           7
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           464
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           466
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8950178"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8950178"
FT   CARBOHYD        172
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8950178"
FT   CARBOHYD        205
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8950178"
FT   CARBOHYD        235
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8950178"
FT   CARBOHYD        247
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8950178"
FT   CARBOHYD        321
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8950178"
FT   CARBOHYD        417
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8950178"
FT   DISULFID        243..311
FT                   /evidence="ECO:0000269|PubMed:9826197"
FT   DISULFID        272..333
FT                   /evidence="ECO:0000269|PubMed:9826197"
FT   DISULFID        313..322
FT                   /evidence="ECO:0000269|PubMed:9826197"
FT   CROSSLNK        469
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P16671"
FT   CONFLICT        39
FT                   /note="K -> N (in Ref. 2; CAA62803)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        110
FT                   /note="H -> N (in Ref. 1; BAA08224)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        125
FT                   /note="S -> L (in Ref. 1; BAA08224)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        134
FT                   /note="T -> K (in Ref. 1; BAA08224)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        257
FT                   /note="F -> L (in Ref. 1; BAA08224)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        294
FT                   /note="I -> V (in Ref. 1; BAA08224)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        305
FT                   /note="Q -> E (in Ref. 1; BAA08224)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        359
FT                   /note="S -> G (in Ref. 1; BAA08224)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        391..396
FT                   /note="MLVKPA -> TGQARQ (in Ref. 1; BAA08224)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        466
FT                   /note="C -> Y (in Ref. 1; BAA08224)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        470..472
FT                   /note="RVN -> TIK (in Ref. 1; BAA08224)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   472 AA;  52940 MW;  D864D6D3D6E8622F CRC64;
     MGCNRNCGLI AGAVIGAVLA VFGGILMPVG DMLIEKTIKK EVVLEEGTIA FKNWVKTGTD
     VYRQFWIFDV QNPDEVTVNS SKIKVKQRGP YTYRVRYLAK ENITQDPETH TVSFLQPNGA
     IFEPSLSVGT EDDTFTILNL AVAAAPQLYP NTFMQGILNS FIKKSKSSMF QNRTLKELLW
     GYTDPFLNLV PYPITTTIGV FYPYNNTADG IYKVFNGKDD ISKVAIIDTY KGRKNLSYWS
     SYCDLINGTD AASFPPFVEK TRVLQFFSSD ICRSIYAVFG AEINLKGIPV YRFILPSFAF
     ASPFQNPDNH CFCTEKIISK NCTLYGVLDI GKCKEGKPVY ISLPHFLHGS PELAEPIESL
     SPNEEEHSTY LDVEPITGFT LRFAKRLQVN MLVKPAKKIE ALKNLKHNYI VPILWLNETG
     TIGDEKAEMF RNQVTGKINL LGLVEIVLLS VGVVMFIAFM ISYCACRSKR VN
//