ID   CCKAR_HUMAN             Reviewed;         428 AA.
AC   P32238; B2R9Z5;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   27-MAR-2024, entry version 214.
DE   RecName: Full=Cholecystokinin receptor type A;
DE            Short=CCK-A receptor;
DE            Short=CCK-AR;
DE   AltName: Full=Cholecystokinin-1 receptor;
DE            Short=CCK1-R;
GN   Name=CCKAR; Synonyms=CCKRA;
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=Gall bladder;
RX   PubMed=8503909; DOI=10.1006/bbrc.1993.1610;
RA   Ulrich C.D., Ferber I., Holicky E., Hadac E., Buell G., Miller L.J.;
RT   "Molecular cloning and functional expression of the human gallbladder
RT   cholecystokinin A receptor.";
RL   Biochem. Biophys. Res. Commun. 193:204-211(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8343165; DOI=10.1006/bbrc.1993.1894;
RA   Wank S.A., de Weerth A., Pisegna J.R., Huppi K.;
RT   "Molecular cloning, functional expression and chromosomal localization of
RT   the human cholecystokinin type A receptor.";
RL   Biochem. Biophys. Res. Commun. 194:811-818(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7557108; DOI=10.1016/0016-5085(95)90601-0;
RA   Miller L.J., Holicky E.L., Ulrich C.D., Wieben E.D.;
RT   "Abnormal processing of the human cholecystokinin receptor gene in
RT   association with gallstones and obesity.";
RL   Gastroenterology 109:1375-1380(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Peripheral blood leukocyte;
RX   PubMed=10682840; DOI=10.1016/s0014-5793(00)01080-2;
RA   Funakoshi A., Miyasaka K., Matsumoto H., Yamamori S., Takiguchi S.,
RA   Kataoka K., Takata Y., Matsusue K., Kono A., Shimokata H.;
RT   "Gene structure of human cholecystokinin (CCK) type-A receptor: body fat
RT   content is related to CCK type-A receptor gene promoter polymorphism.";
RL   FEBS Lett. 466:264-266(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Stomach;
RA   Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT   "cDNA clones of human proteins involved in signal transduction sequenced by
RT   the Guthrie cDNA resource center (www.cdna.org).";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thalamus;
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 GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   STRUCTURE BY NMR OF 1-47 IN COMPLEX WITH CCK.
RX   PubMed=10555959; DOI=10.1021/bi991272l;
RA   Pellegrini M., Mierke D.F.;
RT   "Molecular complex of cholecystokinin-8 and N-terminus of the
RT   cholecystokinin A receptor by NMR spectroscopy.";
RL   Biochemistry 38:14775-14783(1999).
RN   [10]
RP   STRUCTURE BY NMR OF 329-357 IN COMPLEX WITH CCK.
RX   PubMed=11300760; DOI=10.1021/bi002659n;
RA   Giragossian C., Mierke D.F.;
RT   "Intermolecular interactions between cholecystokinin-8 and the third
RT   extracellular loop of the cholecystokinin A receptor.";
RL   Biochemistry 40:3804-3809(2001).
CC   -!- FUNCTION: Receptor for cholecystokinin. Mediates pancreatic growth and
CC       enzyme secretion, smooth muscle contraction of the gall bladder and
CC       stomach. Has a 1000-fold higher affinity for CCK rather than for
CC       gastrin. It modulates feeding and dopamine-induced behavior in the
CC       central and peripheral nervous system. This receptor mediates its
CC       action by association with G proteins that activate a
CC       phosphatidylinositol-calcium second messenger system.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Cholecystokinin receptor entry;
CC       URL="https://en.wikipedia.org/wiki/Cholecystokinin_receptor";
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DR   EMBL; L13605; AAA35659.1; -; mRNA.
DR   EMBL; L19315; AAA02819.1; -; mRNA.
DR   EMBL; U23430; AAA91123.1; -; Genomic_DNA.
DR   EMBL; U23427; AAA91123.1; JOINED; Genomic_DNA.
DR   EMBL; U23428; AAA91123.1; JOINED; Genomic_DNA.
DR   EMBL; U23429; AAA91123.1; JOINED; Genomic_DNA.
DR   EMBL; D85606; BAA90879.1; -; Genomic_DNA.
DR   EMBL; AY322549; AAP84362.1; -; mRNA.
DR   EMBL; AK313978; BAG36692.1; -; mRNA.
DR   EMBL; CH471069; EAW92850.1; -; Genomic_DNA.
DR   EMBL; BC074987; AAH74987.1; -; mRNA.
DR   CCDS; CCDS3438.1; -.
DR   PIR; JN0692; JN0692.
DR   RefSeq; NP_000721.1; NM_000730.2.
DR   PDB; 1D6G; NMR; -; A=1-47.
DR   PDB; 1HZN; NMR; -; A=329-357.
DR   PDB; 7EZH; EM; 3.20 A; D=1-428.
DR   PDB; 7EZK; EM; 3.10 A; D=1-428.
DR   PDB; 7EZM; EM; 2.90 A; D=1-428.
DR   PDB; 7F8U; X-ray; 2.80 A; A=37-240, A=302-375.
DR   PDB; 7F8X; X-ray; 3.00 A; A=2-240, A=302-406.
DR   PDB; 7F8Y; X-ray; 2.50 A; A=37-240, A=302-406.
DR   PDB; 7MBX; EM; 1.95 A; R=2-428.
DR   PDB; 7MBY; EM; 2.44 A; R=2-428.
DR   PDB; 7XOU; EM; 3.20 A; R=1-428.
DR   PDB; 7XOV; EM; 3.00 A; R=1-428.
DR   PDBsum; 1D6G; -.
DR   PDBsum; 1HZN; -.
DR   PDBsum; 7EZH; -.
DR   PDBsum; 7EZK; -.
DR   PDBsum; 7EZM; -.
DR   PDBsum; 7F8U; -.
DR   PDBsum; 7F8X; -.
DR   PDBsum; 7F8Y; -.
DR   PDBsum; 7MBX; -.
DR   PDBsum; 7MBY; -.
DR   PDBsum; 7XOU; -.
DR   PDBsum; 7XOV; -.
DR   AlphaFoldDB; P32238; -.
DR   EMDB; EMD-23749; -.
DR   EMDB; EMD-23750; -.
DR   EMDB; EMD-31387; -.
DR   EMDB; EMD-31388; -.
DR   EMDB; EMD-31389; -.
DR   EMDB; EMD-33359; -.
DR   EMDB; EMD-33360; -.
DR   SMR; P32238; -.
DR   BioGRID; 107328; 1.
DR   IntAct; P32238; 1.
DR   MINT; P32238; -.
DR   STRING; 9606.ENSP00000295589; -.
DR   BindingDB; P32238; -.
DR   ChEMBL; CHEMBL1901; -.
DR   DrugBank; DB00403; Ceruletide.
DR   DrugBank; DB08862; Cholecystokinin.
DR   DrugBank; DB04856; Dexloxiglumide.
DR   DrugBank; DB04867; Lintitript.
DR   DrugCentral; P32238; -.
DR   GuidetoPHARMACOLOGY; 76; -.
DR   GlyCosmos; P32238; 3 sites, No reported glycans.
DR   GlyGen; P32238; 3 sites.
DR   iPTMnet; P32238; -.
DR   PhosphoSitePlus; P32238; -.
DR   BioMuta; CCKAR; -.
DR   DMDM; 416772; -.
DR   MassIVE; P32238; -.
DR   MaxQB; P32238; -.
DR   PaxDb; 9606-ENSP00000295589; -.
DR   PeptideAtlas; P32238; -.
DR   ProteomicsDB; 54844; -.
DR   Antibodypedia; 3359; 486 antibodies from 37 providers.
DR   DNASU; 886; -.
DR   Ensembl; ENST00000295589.4; ENSP00000295589.3; ENSG00000163394.6.
DR   GeneID; 886; -.
DR   KEGG; hsa:886; -.
DR   MANE-Select; ENST00000295589.4; ENSP00000295589.3; NM_000730.3; NP_000721.1.
DR   UCSC; uc003gse.2; human.
DR   AGR; HGNC:1570; -.
DR   CTD; 886; -.
DR   DisGeNET; 886; -.
DR   GeneCards; CCKAR; -.
DR   HGNC; HGNC:1570; CCKAR.
DR   HPA; ENSG00000163394; Group enriched (gallbladder, stomach).
DR   MIM; 118444; gene.
DR   neXtProt; NX_P32238; -.
DR   OpenTargets; ENSG00000163394; -.
DR   PharmGKB; PA26142; -.
DR   VEuPathDB; HostDB:ENSG00000163394; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01100000263563; -.
DR   HOGENOM; CLU_009579_6_3_1; -.
DR   InParanoid; P32238; -.
DR   OMA; SNISPPC; -.
DR   OrthoDB; 3686620at2759; -.
DR   PhylomeDB; P32238; -.
DR   TreeFam; TF315303; -.
DR   PathwayCommons; P32238; -.
DR   Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR   Reactome; R-HSA-416476; G alpha (q) signalling events.
DR   SignaLink; P32238; -.
DR   SIGNOR; P32238; -.
DR   BioGRID-ORCS; 886; 9 hits in 1152 CRISPR screens.
DR   EvolutionaryTrace; P32238; -.
DR   GeneWiki; Cholecystokinin_A_receptor; -.
DR   GenomeRNAi; 886; -.
DR   Pharos; P32238; Tclin.
DR   PRO; PR:P32238; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; P32238; Protein.
DR   Bgee; ENSG00000163394; Expressed in gall bladder and 44 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0016020; C:membrane; IDA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0004951; F:cholecystokinin receptor activity; IDA:GO_Central.
DR   GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR   GO; GO:0017046; F:peptide hormone binding; IPI:GO_Central.
DR   GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR   GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
DR   GO; GO:0038188; P:cholecystokinin signaling pathway; IDA:GO_Central.
DR   GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR   GO; GO:0046883; P:regulation of hormone secretion; IBA:GO_Central.
DR   Gene3D; 4.10.670.10; Cholecystokinin A receptor, N-terminal domain; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 2.
DR   InterPro; IPR009126; Cholcskin_rcpt.
DR   InterPro; IPR000596; Cholcy_rcpt_A.
DR   InterPro; IPR015276; CholecystokininA_recpt_N.
DR   InterPro; IPR036472; CholecystokininA_recpt_N_sf.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24238:SF77; CHOLECYSTOKININ RECEPTOR TYPE A; 1.
DR   PANTHER; PTHR24238; G-PROTEIN COUPLED RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   Pfam; PF09193; CholecysA-Rec_N; 1.
DR   PRINTS; PR01822; CCYSTOKININR.
DR   PRINTS; PR00524; CCYSTOKNINAR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; P32238; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Lipoprotein; Membrane; Palmitate; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..428
FT                   /note="Cholecystokinin receptor type A"
FT                   /id="PRO_0000069223"
FT   TOPO_DOM        1..41
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..67
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        68..77
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..104
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        105..115
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..137
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..157
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        179..210
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        211..234
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        235..313
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        314..334
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        335..349
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        350..373
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        374..428
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          248..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           387
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        10
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        24
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        190
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        18..29
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   DISULFID        114..196
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   TURN            5..11
FT                   /evidence="ECO:0007829|PDB:1D6G"
FT   STRAND          13..15
FT                   /evidence="ECO:0007829|PDB:1D6G"
FT   STRAND          21..25
FT                   /evidence="ECO:0007829|PDB:1D6G"
FT   HELIX           40..68
FT                   /evidence="ECO:0007829|PDB:7MBX"
FT   HELIX           70..72
FT                   /evidence="ECO:0007829|PDB:7MBX"
FT   HELIX           75..104
FT                   /evidence="ECO:0007829|PDB:7MBX"
FT   HELIX           111..144
FT                   /evidence="ECO:0007829|PDB:7MBX"
FT   HELIX           146..152
FT                   /evidence="ECO:0007829|PDB:7MBX"
FT   HELIX           155..172
FT                   /evidence="ECO:0007829|PDB:7MBX"
FT   HELIX           175..179
FT                   /evidence="ECO:0007829|PDB:7MBX"
FT   STRAND          180..186
FT                   /evidence="ECO:0007829|PDB:7MBX"
FT   HELIX           188..190
FT                   /evidence="ECO:0007829|PDB:7F8U"
FT   STRAND          192..198
FT                   /evidence="ECO:0007829|PDB:7MBX"
FT   HELIX           203..217
FT                   /evidence="ECO:0007829|PDB:7MBX"
FT   HELIX           219..242
FT                   /evidence="ECO:0007829|PDB:7MBX"
FT   HELIX           304..338
FT                   /evidence="ECO:0007829|PDB:7MBX"
FT   HELIX           340..347
FT                   /evidence="ECO:0007829|PDB:7MBX"
FT   HELIX           350..360
FT                   /evidence="ECO:0007829|PDB:7MBX"
FT   HELIX           362..370
FT                   /evidence="ECO:0007829|PDB:7MBX"
FT   TURN            371..373
FT                   /evidence="ECO:0007829|PDB:7MBX"
FT   HELIX           375..381
FT                   /evidence="ECO:0007829|PDB:7MBX"
FT   TURN            382..384
FT                   /evidence="ECO:0007829|PDB:7MBX"
SQ   SEQUENCE   428 AA;  47841 MW;  A6E8FABDA805E610 CRC64;
     MDVVDSLLVN GSNITPPCEL GLENETLFCL DQPRPSKEWQ PAVQILLYSL IFLLSVLGNT
     LVITVLIRNK RMRTVTNIFL LSLAVSDLML CLFCMPFNLI PNLLKDFIFG SAVCKTTTYF
     MGTSVSVSTF NLVAISLERY GAICKPLQSR VWQTKSHALK VIAATWCLSF TIMTPYPIYS
     NLVPFTKNNN QTANMCRFLL PNDVMQQSWH TFLLLILFLI PGIVMMVAYG LISLELYQGI
     KFEASQKKSA KERKPSTTSS GKYEDSDGCY LQKTRPPRKL ELRQLSTGSS SRANRIRSNS
     SAANLMAKKR VIRMLIVIVV LFFLCWMPIF SANAWRAYDT ASAERRLSGT PISFILLLSY
     TSSCVNPIIY CFMNKRFRLG FMATFPCCPN PGPPGARGEV GEEEEGGTTG ASLSRFSYSH
     MSASVPPQ
//