FITM2_HUMAN
ID FITM2_HUMAN Reviewed; 262 AA.
AC Q8N6M3; A1L492; B9EGQ4; Q5TE59; Q9H3Y1;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Acyl-coenzyme A diphosphatase FITM2 {ECO:0000255|HAMAP-Rule:MF_03230, ECO:0000303|PubMed:32915949};
DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_03230, ECO:0000269|PubMed:32915949};
DE AltName: Full=Fat storage-inducing transmembrane protein 2 {ECO:0000255|HAMAP-Rule:MF_03230};
DE AltName: Full=Fat-inducing protein 2 {ECO:0000255|HAMAP-Rule:MF_03230};
GN Name=FITM2 {ECO:0000255|HAMAP-Rule:MF_03230, ECO:0000312|HGNC:HGNC:16135};
GN Synonyms=C20orf142, FIT2 {ECO:0000255|HAMAP-Rule:MF_03230,
GN ECO:0000303|PubMed:18160536};
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [2]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, 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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18160536; DOI=10.1073/pnas.0708579105;
RA Kadereit B., Kumar P., Wang W.-J., Miranda D., Snapp E.L., Severina N.,
RA Torregroza I., Evans T., Silver D.L.;
RT "Evolutionarily conserved gene family important for fat storage.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:94-99(2008).
RN [5]
RP FUNCTION.
RX PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT "Identification and characterization of a set of conserved and new
RT regulators of cytoskeletal organisation, cell morphology and migration.";
RL BMC Biol. 9:54-54(2011).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVE SITE, AND MUTAGENESIS OF HIS-155 AND HIS-214.
RX PubMed=32915949; DOI=10.1083/jcb.202006111;
RA Becuwe M., Bond L.M., Pinto A.F.M., Boland S., Mejhert N., Elliott S.D.,
RA Cicconet M., Graham M.M., Liu X.N., Ilkayeva O., Saghatelian A.,
RA Walther T.C., Farese R.V.;
RT "FIT2 is an acyl-coenzyme A diphosphatase crucial for endoplasmic reticulum
RT homeostasis.";
RL J. Cell Biol. 219:0-0(2020).
RN [7]
RP INVOLVEMENT IN SIDDIS SYNDROME, AND VARIANT 2-GLU--LYS-262 DEL.
RX PubMed=28067622; DOI=10.1242/dmm.026476;
RA Zazo Seco C., Castells-Nobau A., Joo S.H., Schraders M., Foo J.N.,
RA van der Voet M., Velan S.S., Nijhof B., Oostrik J., de Vrieze E.,
RA Katana R., Mansoor A., Huynen M., Szklarczyk R., Oti M., Tranebjaerg L.,
RA van Wijk E., Scheffer-de Gooyert J.M., Siddique S., Baets J., de Jonghe P.,
RA Kazmi S.A., Sadananthan S.A., van de Warrenburg B.P., Khor C.C.,
RA Goepfert M.C., Qamar R., Schenck A., Kremer H., Siddiqi S.;
RT "A homozygous FITM2 mutation causes a deafness-dystonia syndrome with motor
RT regression and signs of ichthyosis and sensory neuropathy.";
RL Dis. Model. Mech. 10:105-118(2017).
RN [8]
RP VARIANT SIDDIS 218-GLN--LYS-262 DEL.
RX PubMed=30214770; DOI=10.1002/ccr3.1719;
RA Shakir A., Wadley A.F., Purcarin G., Wierenga K.J.;
RT "The first case of deafness-dystonia syndrome due to compound heterozygous
RT variants in FITM2.";
RL Clin. Case Rep. 6:1815-1817(2018).
RN [9]
RP VARIANT SIDDIS ARG-232.
RX PubMed=30288795; DOI=10.1002/mds.27481;
RA Riedhammer K.M., Leszinski G.S., Andres S., Strobl-Wildemann G., Wagner M.;
RT "First replication that biallelic variants in FITM2 cause a complex
RT deafness-dystonia syndrome.";
RL Mov. Disord. 33:1665-1666(2018).
CC -!- FUNCTION: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes
CC fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-
CC bisphosphate (PubMed:32915949) (By similarity). Preferentially
CC hydrolyzes unsaturated long-chain acyl-CoA substrates such as oleoyl-
CC CoA/(9Z)-octadecenoyl-CoA and arachidonoyl-CoA/(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-CoA in the endoplasmic reticulum (ER) lumen
CC (PubMed:32915949) (By similarity). This catalytic activity is required
CC for maintaining ER structure and for lipid droplets (LDs) biogenesis,
CC which are lipid storage organelles involved in maintaining lipid and
CC energy homeostasis (PubMed:18160536, PubMed:32915949) (By similarity).
CC Directly binds to diacylglycerol (DAGs) and triacylglycerol, which is
CC also important for LD biogenesis (By similarity). May support
CC directional budding of nacent LDs from the ER into the cytosol by
CC reducing DAG levels at sites of LD formation (By similarity). Plays a
CC role in the regulation of cell morphology and cytoskeletal organization
CC (PubMed:21834987) (By similarity). {ECO:0000255|HAMAP-Rule:MF_03230,
CC ECO:0000269|PubMed:18160536, ECO:0000269|PubMed:21834987,
CC ECO:0000269|PubMed:32915949}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + H2O = adenosine 3',5'-bisphosphate + an acyl-4'-
CC phosphopantetheine + 2 H(+); Xref=Rhea:RHEA:50044, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58342, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:132023; Evidence={ECO:0000255|HAMAP-Rule:MF_03230,
CC ECO:0000269|PubMed:32915949};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50045;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03230,
CC ECO:0000305|PubMed:32915949};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2
CC H(+) + S-(9Z-octadecenoyl)-4'-phosphopantetheine;
CC Xref=Rhea:RHEA:65564, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:58343, ChEBI:CHEBI:156553;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03230,
CC ECO:0000269|PubMed:32915949};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65565;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03230,
CC ECO:0000305|PubMed:32915949};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H2O = adenosine 3',5'-
CC bisphosphate + 2 H(+) + S-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-4'-
CC phosphopantetheine; Xref=Rhea:RHEA:65568, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57368, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:156554; Evidence={ECO:0000255|HAMAP-Rule:MF_03230,
CC ECO:0000269|PubMed:32915949};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65569;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03230,
CC ECO:0000305|PubMed:32915949};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+)
CC + S-hexadecanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50032,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132018; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03230, ECO:0000269|PubMed:32915949};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03230,
CC ECO:0000305|PubMed:32915949};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 uM for (9Z)-octadecenoyl-CoA {ECO:0000269|PubMed:32915949};
CC Vmax=6.5 umol/min/mg enzyme with (9Z)-octadecenoyl-CoA as substrate
CC {ECO:0000269|PubMed:32915949};
CC -!- INTERACTION:
CC Q8N6M3; Q9BUP3-3: HTATIP2; NbExp=3; IntAct=EBI-11722638, EBI-12937691;
CC Q8N6M3; Q53HI1: UNC50; NbExp=3; IntAct=EBI-11722638, EBI-7601760;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03230, ECO:0000269|PubMed:18160536}; Multi-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03230}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:18160536}.
CC -!- DISEASE: Siddiqi syndrome (SIDDIS) [MIM:618635]: An autosomal recessive
CC disorder characterized by early-onset progressive sensorineural hearing
CC impairment, global developmental delay, regression of motor skills,
CC dystonia, and low body mass index. Some patients have an ichthosis-like
CC appearance of the skin and signs of sensory neuropathy.
CC {ECO:0000269|PubMed:28067622, ECO:0000269|PubMed:30214770,
CC ECO:0000269|PubMed:30288795}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the FIT family. FIT2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03230}.
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; AL117382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75929.1; -; Genomic_DNA.
DR EMBL; BC130446; AAI30447.1; -; mRNA.
DR EMBL; BC136640; AAI36641.1; -; mRNA.
DR EMBL; BC029662; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS33473.1; -.
DR RefSeq; NP_001073941.1; NM_001080472.3.
DR AlphaFoldDB; Q8N6M3; -.
DR BioGRID; 126125; 68.
DR IntAct; Q8N6M3; 31.
DR MINT; Q8N6M3; -.
DR STRING; 9606.ENSP00000380037; -.
DR TCDB; 9.B.287.1.1; the fat storage-inducing transmembrane protein 2 (fit2) family.
DR iPTMnet; Q8N6M3; -.
DR PhosphoSitePlus; Q8N6M3; -.
DR BioMuta; FITM2; -.
DR DMDM; 28212210; -.
DR EPD; Q8N6M3; -.
DR jPOST; Q8N6M3; -.
DR MassIVE; Q8N6M3; -.
DR MaxQB; Q8N6M3; -.
DR PaxDb; Q8N6M3; -.
DR PeptideAtlas; Q8N6M3; -.
DR PRIDE; Q8N6M3; -.
DR ProteomicsDB; 72192; -.
DR Antibodypedia; 51829; 10 antibodies from 1 providers.
DR DNASU; 128486; -.
DR Ensembl; ENST00000396825.4; ENSP00000380037.3; ENSG00000197296.6.
DR GeneID; 128486; -.
DR KEGG; hsa:128486; -.
DR MANE-Select; ENST00000396825.4; ENSP00000380037.3; NM_001080472.4; NP_001073941.1.
DR UCSC; uc002xlr.2; human.
DR CTD; 128486; -.
DR DisGeNET; 128486; -.
DR GeneCards; FITM2; -.
DR HGNC; HGNC:16135; FITM2.
DR HPA; ENSG00000197296; Tissue enhanced (heart).
DR MalaCards; FITM2; -.
DR MIM; 612029; gene.
DR MIM; 618635; phenotype.
DR neXtProt; NX_Q8N6M3; -.
DR OpenTargets; ENSG00000197296; -.
DR PharmGKB; PA25685; -.
DR VEuPathDB; HostDB:ENSG00000197296; -.
DR eggNOG; KOG3750; Eukaryota.
DR GeneTree; ENSGT00530000063693; -.
DR HOGENOM; CLU_049499_1_1_1; -.
DR InParanoid; Q8N6M3; -.
DR OMA; ERCAWFL; -.
DR OrthoDB; 1621925at2759; -.
DR PhylomeDB; Q8N6M3; -.
DR PathwayCommons; Q8N6M3; -.
DR Reactome; R-HSA-8964572; Lipid particle organization.
DR SignaLink; Q8N6M3; -.
DR BioGRID-ORCS; 128486; 41 hits in 1080 CRISPR screens.
DR ChiTaRS; FITM2; human.
DR GenomeRNAi; 128486; -.
DR Pharos; Q8N6M3; Tdark.
DR PRO; PR:Q8N6M3; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q8N6M3; protein.
DR Bgee; ENSG00000197296; Expressed in cardiac muscle of right atrium and 182 other tissues.
DR Genevisible; Q8N6M3; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:BHF-UCL.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0010945; F:CoA pyrophosphatase activity; IMP:UniProtKB.
DR GO; GO:0019992; F:diacylglycerol binding; ISS:UniProtKB.
DR GO; GO:0017129; F:triglyceride binding; ISS:UniProtKB.
DR GO; GO:0035356; P:cellular triglyceride homeostasis; ISS:BHF-UCL.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0036115; P:fatty-acyl-CoA catabolic process; IMP:UniProtKB.
DR GO; GO:0140042; P:lipid droplet formation; IMP:UniProtKB.
DR GO; GO:0034389; P:lipid droplet organization; ISS:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; IMP:UniProtKB.
DR GO; GO:0019915; P:lipid storage; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0010890; P:positive regulation of sequestering of triglyceride; ISS:BHF-UCL.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IMP:UniProtKB.
DR GO; GO:0010866; P:regulation of triglyceride biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0030730; P:sequestering of triglyceride; IEA:Ensembl.
DR HAMAP; MF_03230; FITM2; 1.
DR InterPro; IPR019388; FIT.
DR InterPro; IPR046401; FITM1/2.
DR PANTHER; PTHR23129; PTHR23129; 1.
DR Pfam; PF10261; Scs3p; 1.
PE 1: Evidence at protein level;
KW Deafness; Disease variant; Dystonia; Endoplasmic reticulum; Hydrolase;
KW Intellectual disability; Lipid metabolism; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..262
FT /note="Acyl-coenzyme A diphosphatase FITM2"
FT /id="PRO_0000021035"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..57
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..145
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..218
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ACT_SITE 155
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03230,
FT ECO:0000269|PubMed:32915949"
FT ACT_SITE 214
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03230,
FT ECO:0000269|PubMed:32915949"
FT VARIANT 2..262
FT /note="Missing (in SIDDIS)"
FT /evidence="ECO:0000269|PubMed:28067622"
FT /id="VAR_081219"
FT VARIANT 218..262
FT /note="Missing (in SIDDIS)"
FT /evidence="ECO:0000269|PubMed:30214770"
FT /id="VAR_083498"
FT VARIANT 232
FT /note="G -> R (in SIDDIS; dbSNP:rs765281145)"
FT /evidence="ECO:0000269|PubMed:30288795"
FT /id="VAR_083499"
FT MUTAGEN 155
FT /note="H->A: Loss of oleoyl-CoA diphosphatase activity;
FT when associated with A-214. Impaired ER morphology. No
FT difference in the appearance of the Golgi apparatus,
FT lysosomes or peroxisomes."
FT /evidence="ECO:0000269|PubMed:32915949"
FT MUTAGEN 214
FT /note="H->A: Loss of oleoyl-CoA diphosphatase activity;
FT when associated with A-155. Impaired ER morphology, ER
FT homeostasis and lipid droplet biogenesis. No difference in
FT the appearance of the Golgi apparatus, lysosomes or
FT peroxisomes."
FT /evidence="ECO:0000269|PubMed:32915949"
SQ SEQUENCE 262 AA; 29855 MW; 3822E7CEFBB6CDEB CRC64;
MEHLERCEWL LRGTLVRAAV RRYLPWALVA SMLAGSLLKE LSPLPESYLS NKRNVLNVYF
VKVAWAWTFC LLLPFIALTN YHLTGKAGLV LRRLSTLLVG TAIWYICTSI FSNIEHYTGS
CYQSPALEGV RKEHQSKQQC HQEGGFWHGF DISGHSFLLT FCALMIVEEM SVLHEVKTDR
SHCLHTAITT LVVALGILTF IWVLMFLCTA VYFHNLSQKV FGTLFGLLSW YGTYGFWYPK
AFSPGLPPQS CSLNLKQDSY KK
