ID   SCD2_MOUSE              Reviewed;         358 AA.
AC   P13011; Q8BH96;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=Stearoyl-CoA desaturase 2 {ECO:0000303|PubMed:16118274};
DE            EC=1.14.19.1 {ECO:0000269|PubMed:16443825, ECO:0000305|PubMed:16118274};
DE   AltName: Full=Acyl-CoA desaturase 2;
DE   AltName: Full=Delta(9)-desaturase 2;
DE            Short=Delta-9 desaturase 2 {ECO:0000303|PubMed:16443825};
DE   AltName: Full=Fatty acid desaturase 2;
GN   Name=Scd2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adipocyte;
RX   PubMed=2570068; DOI=10.1016/s0021-9258(18)63763-9;
RA   Kaestner K.H., Ntambi J.M., Kelly T.J. Jr., Lane M.D.;
RT   "Differentiation-induced gene expression in 3T3-L1 preadipocytes. A second
RT   differentially expressed gene encoding stearoyl-CoA desaturase.";
RL   J. Biol. Chem. 264:14755-14761(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=129; TISSUE=Mammary tumor;
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   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=10545940; DOI=10.1038/15446;
RA   Zheng Y., Eilertsen K.J., Ge L., Zhang L., Sundberg J.P., Prouty S.M.,
RA   Stenn K.S., Parimoo S.;
RT   "Scd1 is expressed in sebaceous glands and is disrupted in the asebia
RT   mouse.";
RL   Nat. Genet. 23:268-270(1999).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=11161812; DOI=10.1006/geno.2000.6429;
RA   Zheng Y., Prouty S.M., Harmon A., Sundberg J.P., Stenn K.S., Parimoo S.;
RT   "Scd3--a novel gene of the stearoyl-CoA desaturase family with restricted
RT   expression in skin.";
RL   Genomics 71:182-191(2001).
RN   [7]
RP   INDUCTION BY UNSATURATED FATTY ACIDS AND NR1H3, AND TISSUE SPECIFICITY.
RX   PubMed=12815040; DOI=10.1074/jbc.m304724200;
RA   Miyazaki M., Jacobson M.J., Man W.C., Cohen P., Asilmaz E., Friedman J.M.,
RA   Ntambi J.M.;
RT   "Identification and characterization of murine SCD4, a novel heart-specific
RT   stearoyl-CoA desaturase isoform regulated by leptin and dietary factors.";
RL   J. Biol. Chem. 278:33904-33911(2003).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=16118274; DOI=10.1073/pnas.0503132102;
RA   Miyazaki M., Dobrzyn A., Elias P.M., Ntambi J.M.;
RT   "Stearoyl-CoA desaturase-2 gene expression is required for lipid synthesis
RT   during early skin and liver development.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12501-12506(2005).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX   PubMed=16443825; DOI=10.1194/jlr.c500025-jlr200;
RA   Miyazaki M., Bruggink S.M., Ntambi J.M.;
RT   "Identification of mouse palmitoyl-coenzyme A Delta9-desaturase.";
RL   J. Lipid Res. 47:700-704(2006).
CC   -!- FUNCTION: Stearoyl-CoA desaturase that utilizes O(2) and electrons from
CC       reduced cytochrome b5 to introduce the first double bond into saturated
CC       fatty acyl-CoA substrates (PubMed:16443825). Catalyzes the insertion of
CC       a cis double bond at the delta-9 position into fatty acyl-CoA
CC       substrates including palmitoyl-CoA and stearoyl-CoA (PubMed:16443825).
CC       Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids
CC       (PubMed:16443825). Contributes to the biosynthesis of membrane
CC       phospholipids, cholesterol esters and triglycerides, especially during
CC       embryonic development and in neonates (PubMed:16118274). Important for
CC       normal permeability barrier function of the skin in neonates
CC       (PubMed:16118274). {ECO:0000269|PubMed:16118274,
CC       ECO:0000269|PubMed:16443825}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA =
CC         (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC         Xref=Rhea:RHEA:19721, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57387,
CC         ChEBI:CHEBI:57394; EC=1.14.19.1;
CC         Evidence={ECO:0000269|PubMed:16443825, ECO:0000305|PubMed:16118274};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19722;
CC         Evidence={ECO:0000305|PubMed:16118274, ECO:0000305|PubMed:16443825};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + hexadecanoyl-CoA + O2 =
CC         (9Z)-hexadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC         Xref=Rhea:RHEA:36931, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57379,
CC         ChEBI:CHEBI:61540; Evidence={ECO:0000269|PubMed:16443825};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36932;
CC         Evidence={ECO:0000305|PubMed:16443825};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:P13516};
CC       Note=Expected to bind 2 Fe(2+) ions per subunit.
CC       {ECO:0000250|UniProtKB:P13516};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000305|PubMed:16443825}; Multi-pass membrane protein
CC       {ECO:0000305|PubMed:16443825}. Microsome membrane
CC       {ECO:0000269|PubMed:16443825}.
CC   -!- TISSUE SPECIFICITY: Detected in brain and skin (PubMed:10545940,
CC       PubMed:11161812, PubMed:16118274). Highly expressed in brain, and
CC       detected at low levels in heart, stomach, lung and testis
CC       (PubMed:11161812, PubMed:12815040). Detected both in dermis and
CC       epidermis (PubMed:16118274). {ECO:0000269|PubMed:10545940,
CC       ECO:0000269|PubMed:12815040, ECO:0000269|PubMed:16118274}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed during embryonic development and
CC       during the first three weeks after birth. Expression is low in adults.
CC       {ECO:0000269|PubMed:16118274}.
CC   -!- INDUCTION: Up-regulated by agonists that activate NR1H3
CC       (PubMed:12815040). Slightly down-regulated by a high-carbohydrate diet
CC       enriched in unsaturated fatty acids (PubMed:12815040).
CC       {ECO:0000269|PubMed:12815040}.
CC   -!- DOMAIN: The histidine box domains are involved in binding the catalytic
CC       metal ions. {ECO:0000250|UniProtKB:O00767}.
CC   -!- DISRUPTION PHENOTYPE: Mutant mice are born at the expected Mendelian
CC       rate. Neonates are smaller than wild-type and present high mortality,
CC       ranging from 70 to 100%, depending on the genetic background. Neonates
CC       display a shiny skin, but after a few hours their skin appears dry and
CC       cracked. The permeability barrier function of their skin is impaired,
CC       leading to rapid weight loss due to dehydration. Their epidermis has
CC       decreased levels of cholesterol esters, triglycerides, acylceramide,
CC       and glucosylacylceramide containing unsaturated fatty acids. In mutant
CC       neonates, triglyceride levels in liver and blood plasma are reduced by
CC       half, due to strongly reduced levels of stearoyl-CoA desaturase
CC       activity in the liver and strongly reduced levels of triglyceride
CC       biosynthesis. In contrast, the levels of stearoyl-CoA desaturase
CC       activity are normal in adult mice deficient for Scd2. Adult mice
CC       display kinked tails. {ECO:0000269|PubMed:16118274}.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; M26270; AAA40094.1; -; mRNA.
DR   EMBL; AK083922; BAC39066.1; -; mRNA.
DR   EMBL; AK147406; BAE27893.1; -; mRNA.
DR   EMBL; CH466534; EDL41928.1; -; Genomic_DNA.
DR   EMBL; BC040384; AAH40384.1; -; mRNA.
DR   CCDS; CCDS29848.1; -.
DR   PIR; A36507; A36507.
DR   RefSeq; NP_033154.2; NM_009128.2.
DR   AlphaFoldDB; P13011; -.
DR   SMR; P13011; -.
DR   BioGRID; 203089; 5.
DR   IntAct; P13011; 1.
DR   MINT; P13011; -.
DR   STRING; 10090.ENSMUSP00000026221; -.
DR   iPTMnet; P13011; -.
DR   PhosphoSitePlus; P13011; -.
DR   SwissPalm; P13011; -.
DR   EPD; P13011; -.
DR   MaxQB; P13011; -.
DR   PaxDb; 10090-ENSMUSP00000026221; -.
DR   PeptideAtlas; P13011; -.
DR   ProteomicsDB; 285646; -.
DR   Pumba; P13011; -.
DR   DNASU; 20250; -.
DR   Ensembl; ENSMUST00000026221.7; ENSMUSP00000026221.6; ENSMUSG00000025203.7.
DR   GeneID; 20250; -.
DR   KEGG; mmu:20250; -.
DR   UCSC; uc008hpp.2; mouse.
DR   AGR; MGI:98240; -.
DR   CTD; 20250; -.
DR   MGI; MGI:98240; Scd2.
DR   VEuPathDB; HostDB:ENSMUSG00000025203; -.
DR   eggNOG; KOG1600; Eukaryota.
DR   GeneTree; ENSGT00940000154908; -.
DR   HOGENOM; CLU_027359_0_0_1; -.
DR   InParanoid; P13011; -.
DR   OMA; WWARLHR; -.
DR   OrthoDB; 637961at2759; -.
DR   PhylomeDB; P13011; -.
DR   TreeFam; TF313251; -.
DR   BRENDA; 1.14.19.1; 3474.
DR   BioGRID-ORCS; 20250; 12 hits in 81 CRISPR screens.
DR   ChiTaRS; Scd2; mouse.
DR   PRO; PR:P13011; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; P13011; Protein.
DR   Bgee; ENSMUSG00000025203; Expressed in migratory enteric neural crest cell and 271 other cell types or tissues.
DR   ExpressionAtlas; P13011; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005506; F:iron ion binding; ISO:MGI.
DR   GO; GO:0016491; F:oxidoreductase activity; ISO:MGI.
DR   GO; GO:0032896; F:palmitoyl-CoA 9-desaturase activity; IDA:MGI.
DR   GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IDA:MGI.
DR   GO; GO:1903966; P:monounsaturated fatty acid biosynthetic process; IDA:MGI.
DR   GO; GO:0070542; P:response to fatty acid; ISO:MGI.
DR   GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; ISO:MGI.
DR   CDD; cd03505; Delta9-FADS-like; 1.
DR   InterPro; IPR015876; Acyl-CoA_DS.
DR   InterPro; IPR005804; FA_desaturase_dom.
DR   InterPro; IPR001522; FADS-1_CS.
DR   PANTHER; PTHR11351; ACYL-COA DESATURASE; 1.
DR   PANTHER; PTHR11351:SF102; STEAROYL-COA DESATURASE; 1.
DR   Pfam; PF00487; FA_desaturase; 1.
DR   PRINTS; PR00075; FACDDSATRASE.
DR   PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1.
DR   Genevisible; P13011; MM.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW   Microsome; Oxidoreductase; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..358
FT                   /note="Stearoyl-CoA desaturase 2"
FT                   /id="PRO_0000185398"
FT   TOPO_DOM        1..71
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P13516"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:O00767"
FT   TOPO_DOM        93..96
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P13516"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:O00767"
FT   TOPO_DOM        118..216
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P13516"
FT   TRANSMEM        217..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:O00767"
FT   TOPO_DOM        237..240
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P13516"
FT   TRANSMEM        241..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:O00767"
FT   TOPO_DOM        263..358
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P13516"
FT   REGION          16..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           119..124
FT                   /note="Histidine box-1"
FT                   /evidence="ECO:0000305"
FT   MOTIF           156..160
FT                   /note="Histidine box-2"
FT                   /evidence="ECO:0000305"
FT   MOTIF           297..301
FT                   /note="Histidine box-3"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        16..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O00767"
FT   BINDING         119
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P13516"
FT   BINDING         124
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P13516"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O00767"
FT   BINDING         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O00767"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O00767"
FT   BINDING         156
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P13516"
FT   BINDING         159
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P13516"
FT   BINDING         160
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P13516"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O00767"
FT   BINDING         188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O00767"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O00767"
FT   BINDING         268
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P13516"
FT   BINDING         297
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P13516"
FT   BINDING         300
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P13516"
FT   BINDING         301
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P13516"
FT   CONFLICT        220
FT                   /note="G -> D (in Ref. 1; AAA40094)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        295
FT                   /note="G -> R (in Ref. 1; AAA40094)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   358 AA;  40916 MW;  3E04893F12E92A9A CRC64;
     MPAHILQEIS GAYSATTTIT APPSGGQQNG GEKFEKSSHH WGADVRPELK DDLYDPTYQD
     DEGPPPKLEY VWRNIILMAL LHLGALYGIT LVPSCKLYTC LFAYLYYVIS ALGITAGAHR
     LWSHRTYKAR LPLRLFLIIA NTMAFQNDVY EWARDHRAHH KFSETHADPH NSRRGFFFSH
     VGWLLVRKHP AVKEKGGKLD MSDLKAEKLV MFQRRYYKPG LLLMCFVLPT LVPWYCWGET
     FVNSLCVSTF LRYAVVLNAT WLVNSAAHLY GYRPYDKNIS SRENILVSMG AVGEGFHNYH
     HAFPYDYSAS EYRWHINFTT FFIDCMALLG LAYDRKRVSR AAVLARIKRT GDGSCKSG
//