CIDEC_HUMAN
ID CIDEC_HUMAN Reviewed; 238 AA.
AC Q96AQ7; C9JMN7; Q67DW9; Q9GZY9;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Cell death activator CIDE-3;
DE AltName: Full=Cell death-inducing DFFA-like effector protein C;
DE AltName: Full=Fat-specific protein FSP27 homolog;
GN Name=CIDEC; Synonyms=FSP27;
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] (ISOFORMS 1 AND 2), FUNCTION IN APOPTOSIS,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12429024; DOI=10.1042/bj20020656;
RA Liang L., Zhao M., Xu Z., Yokoyama K.K., Li T.;
RT "Molecular cloning and characterization of CIDE-3, a novel member of the
RT cell-death-inducing DNA-fragmentation-factor (DFF45)-like effector
RT family.";
RL Biochem. J. 370:195-203(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Liang L., Xu Z., Li T., Zhao M.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Adipose tissue;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Brain, and Colon;
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISEASE.
RX PubMed=18334488; DOI=10.1074/jbc.m708323200;
RA Keller P., Petrie J.T., De Rose P., Gerin I., Wright W.S., Chiang S.H.,
RA Nielsen A.R., Fischer C.P., Pedersen B.K., MacDougald O.A.;
RT "Fat-specific protein 27 regulates storage of triacylglycerol.";
RL J. Biol. Chem. 283:14355-14365(2008).
RN [7]
RP DISEASE.
RX PubMed=18509062; DOI=10.1073/pnas.0802063105;
RA Puri V., Ranjit S., Konda S., Nicoloro S.M., Straubhaar J., Chawla A.,
RA Chouinard M., Lin C., Burkart A., Corvera S., Perugini R.A., Czech M.P.;
RT "Cidea is associated with lipid droplets and insulin sensitivity in
RT humans.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7833-7838(2008).
RN [8]
RP FUNCTION, AND INTERACTION WITH CIDEA.
RX PubMed=19843876; DOI=10.1152/ajpendo.00188.2009;
RA Liu K., Zhou S., Kim J.Y., Tillison K., Majors D., Rearick D., Lee J.H.,
RA Fernandez-Boyanapalli R.F., Barricklow K., Houston M.S., Smas C.M.;
RT "Functional analysis of FSP27 protein regions for lipid droplet
RT localization, caspase-dependent apoptosis, and dimerization with CIDEA.";
RL Am. J. Physiol. 297:E1395-E1413(2009).
RN [9]
RP FUNCTION, AND INVOLVEMENT IN FPLD5.
RX PubMed=20049731; DOI=10.1002/emmm.200900037;
RG LD Screening Consortium;
RA Rubio-Cabezas O., Puri V., Murano I., Saudek V., Semple R.K., Dash S.,
RA Hyden C.S., Bottomley W., Vigouroux C., Magre J., Raymond-Barker P.,
RA Murgatroyd P.R., Chawla A., Skepper J.N., Chatterjee V.K., Suliman S.,
RA Patch A.M., Agarwal A.K., Garg A., Barroso I., Cinti S., Czech M.P.,
RA Argente J., O'Rahilly S., Savage D.B.;
RT "Partial lipodystrophy and insulin resistant diabetes in a patient with a
RT homozygous nonsense mutation in CIDEC.";
RL EMBO Mol. Med. 1:280-287(2009).
RN [10]
RP FUNCTION IN UNILOCULAR LIPID DROPLET FORMATION AND LIPOLYSIS, INTERACTION
RP WITH PLIN1, AND SUBCELLULAR LOCATION.
RX PubMed=23399566; DOI=10.1016/j.bbrc.2013.01.113;
RA Grahn T.H., Zhang Y., Lee M.J., Sommer A.G., Mostoslavsky G., Fried S.K.,
RA Greenberg A.S., Puri V.;
RT "FSP27 and PLIN1 interaction promotes the formation of large lipid droplets
RT in human adipocytes.";
RL Biochem. Biophys. Res. Commun. 432:296-301(2013).
CC -!- FUNCTION: Binds to lipid droplets and regulates their enlargement,
CC thereby restricting lipolysis and favoring storage. At focal contact
CC sites between lipid droplets, promotes directional net neutral lipid
CC transfer from the smaller to larger lipid droplets. The transfer
CC direction may be driven by the internal pressure difference between the
CC contacting lipid droplet pair. Its role in neutral lipid transfer and
CC lipid droplet enlargement is activated by the interaction with PLIN1.
CC May act as a CEBPB coactivator in the white adipose tissue to control
CC the expression of a subset of CEBPB downstream target genes, including
CC SOCS1, SOCS3, TGFB1, TGFBR1, ID2 and XDH. When overexpressed in
CC preadipocytes, induces apoptosis or increases cell susceptibility to
CC apoptosis induced by serum deprivation or TGFB treatment. As mature
CC adipocytes, that express high CIDEC levels, are quite resistant to
CC apoptotic stimuli, the physiological significance of its role in
CC apoptosis is unclear. May play a role in the modulation of the response
CC to osmotic stress by preventing NFAT5 to translocate into the nucleus
CC and activate its target genes expression. {ECO:0000269|PubMed:12429024,
CC ECO:0000269|PubMed:18334488, ECO:0000269|PubMed:19843876,
CC ECO:0000269|PubMed:20049731, ECO:0000269|PubMed:23399566}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacyl-sn-glycerol(in) = a triacyl-sn-glycerol(out);
CC Xref=Rhea:RHEA:39011, ChEBI:CHEBI:64615;
CC Evidence={ECO:0000250|UniProtKB:P56198};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with CEBPB. Interacts
CC with NFAT5; this interaction is direct and retains NFAT5 in the
CC cytoplasm (By similarity). Interacts with CIDEA. Interacts with PLIN1.
CC {ECO:0000250, ECO:0000269|PubMed:19843876,
CC ECO:0000269|PubMed:23399566}.
CC -!- INTERACTION:
CC Q96AQ7; Q9BS75: KLHL20; NbExp=3; IntAct=EBI-14151404, EBI-10693436;
CC Q96AQ7; A6NJ78-4: METTL15; NbExp=3; IntAct=EBI-14151404, EBI-10174029;
CC Q96AQ7; Q15466: NR0B2; NbExp=3; IntAct=EBI-14151404, EBI-3910729;
CC Q96AQ7; Q7Z6I5: SPATA12; NbExp=3; IntAct=EBI-14151404, EBI-10696971;
CC Q96AQ7; Q6NVU6: UFSP1; NbExp=3; IntAct=EBI-14151404, EBI-12068150;
CC Q96AQ7; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-14151404, EBI-12287587;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Endoplasmic reticulum.
CC Lipid droplet. Note=Diffuses quickly on lipid droplet surface, but
CC becomes trapped and clustered at lipid droplet contact sites, thereby
CC enabling its rapid enrichment at lipid droplet contact sites.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=CIDE-3;
CC IsoId=Q96AQ7-1; Sequence=Displayed;
CC Name=2; Synonyms=CIDE-3alpha;
CC IsoId=Q96AQ7-2; Sequence=VSP_012738;
CC Name=3; Synonyms=CIDE-3beta;
CC IsoId=Q96AQ7-3; Sequence=VSP_012739, VSP_012740;
CC Name=4;
CC IsoId=Q96AQ7-4; Sequence=VSP_045051;
CC -!- TISSUE SPECIFICITY: Expressed mainly in adipose tissue, small
CC intestine, heart, colon and stomach and, at lower levels, in brain,
CC kidney and liver. {ECO:0000269|PubMed:12429024,
CC ECO:0000269|PubMed:18334488}.
CC -!- DOMAIN: The CIDE-N domain is involved in homodimerization which is
CC crucial for its function in promoting lipid exchange and transfer.
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated and targeted to proteasomal degradation, resulting
CC in a short half-life. Protein stability depends on triaclyglycerol
CC synthesis, fatty acid availability and lipid droplet formation (By
CC similarity). {ECO:0000250}.
CC -!- DISEASE: Note=In omental adipose tissue of obese patients matched for
CC BMI, expression levels tend to correlate with insulin sensitivity.
CC Expression is increased 2-3 fold in the group of patients with high
CC insulin sensitivity, compared to the insulin-resistant group. This
CC observation is consistent with the idea that triglyceride storage in
CC adipocytes plays an important role in sequestering triglycerides and
CC fatty acids away from the circulation and peripheral tissues, thus
CC enhancing insulin sensitivity in liver and muscle. This effect is not
CC significant in subcutaneous adipose tissue (PubMed:18509062). In
CC subcutaneous adipose tissue of diabetic patients, tends to negatively
CC correlate with body mass index and total fat mass, independently of
CC insulin sensitivity (PubMed:18334488). {ECO:0000269|PubMed:18334488,
CC ECO:0000269|PubMed:18509062}.
CC -!- DISEASE: Lipodystrophy, familial partial, 5 (FPLD5) [MIM:615238]: A
CC form of lipodystrophy characterized by loss of subcutaneous adipose
CC tissue affecting limb, femorogluteal and subcutaneous abdominal fat,
CC preservation of visceral, neck and axilliary fat, hepatomegaly, hepatic
CC steatosis and insulin-resistant diabetes.
CC {ECO:0000269|PubMed:20049731}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; AF303893; AAN32612.1; -; mRNA.
DR EMBL; AY364640; AAQ65242.1; -; mRNA.
DR EMBL; AY364638; AAR23106.1; -; mRNA.
DR EMBL; AK024524; BAB14920.1; -; mRNA.
DR EMBL; AK024530; BAB14922.1; -; mRNA.
DR EMBL; AC018809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016851; AAH16851.1; -; mRNA.
DR EMBL; CD518729; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS2587.1; -. [Q96AQ7-1]
DR CCDS; CCDS56239.1; -. [Q96AQ7-4]
DR CCDS; CCDS82731.1; -. [Q96AQ7-2]
DR RefSeq; NP_001186480.1; NM_001199551.1. [Q96AQ7-4]
DR RefSeq; NP_001186481.1; NM_001199552.1. [Q96AQ7-1]
DR RefSeq; NP_001186552.1; NM_001199623.1.
DR RefSeq; NP_001308071.1; NM_001321142.1. [Q96AQ7-1]
DR RefSeq; NP_001308072.1; NM_001321143.1. [Q96AQ7-2]
DR RefSeq; NP_001308073.1; NM_001321144.1. [Q96AQ7-2]
DR RefSeq; NP_071377.2; NM_022094.3. [Q96AQ7-1]
DR AlphaFoldDB; Q96AQ7; -.
DR BioGRID; 121993; 20.
DR IntAct; Q96AQ7; 8.
DR STRING; 9606.ENSP00000373328; -.
DR iPTMnet; Q96AQ7; -.
DR PhosphoSitePlus; Q96AQ7; -.
DR BioMuta; CIDEC; -.
DR DMDM; 20138281; -.
DR jPOST; Q96AQ7; -.
DR MassIVE; Q96AQ7; -.
DR PaxDb; Q96AQ7; -.
DR PeptideAtlas; Q96AQ7; -.
DR PRIDE; Q96AQ7; -.
DR Antibodypedia; 10363; 316 antibodies from 33 providers.
DR DNASU; 63924; -.
DR Ensembl; ENST00000336832.7; ENSP00000338642.2; ENSG00000187288.12. [Q96AQ7-1]
DR Ensembl; ENST00000423850.5; ENSP00000400649.1; ENSG00000187288.12. [Q96AQ7-2]
DR Ensembl; ENST00000430427.6; ENSP00000408631.1; ENSG00000187288.12. [Q96AQ7-4]
DR Ensembl; ENST00000455015.6; ENSP00000392975.1; ENSG00000187288.12. [Q96AQ7-2]
DR Ensembl; ENST00000618572.4; ENSP00000483641.1; ENSG00000187288.12. [Q96AQ7-4]
DR Ensembl; ENST00000675828.1; ENSP00000502377.1; ENSG00000187288.12. [Q96AQ7-1]
DR Ensembl; ENST00000679265.1; ENSP00000504614.1; ENSG00000187288.12. [Q96AQ7-1]
DR GeneID; 63924; -.
DR KEGG; hsa:63924; -.
DR MANE-Select; ENST00000336832.7; ENSP00000338642.2; NM_001321142.2; NP_001308071.1.
DR UCSC; uc003btq.4; human. [Q96AQ7-1]
DR CTD; 63924; -.
DR DisGeNET; 63924; -.
DR GeneCards; CIDEC; -.
DR HGNC; HGNC:24229; CIDEC.
DR HPA; ENSG00000187288; Group enriched (adipose tissue, breast).
DR MalaCards; CIDEC; -.
DR MIM; 612120; gene.
DR MIM; 615238; phenotype.
DR neXtProt; NX_Q96AQ7; -.
DR OpenTargets; ENSG00000187288; -.
DR Orphanet; 435651; CIDEC-related familial partial lipodystrophy.
DR PharmGKB; PA134923736; -.
DR VEuPathDB; HostDB:ENSG00000187288; -.
DR eggNOG; ENOG502QU28; Eukaryota.
DR GeneTree; ENSGT00390000018596; -.
DR HOGENOM; CLU_090011_1_0_1; -.
DR InParanoid; Q96AQ7; -.
DR OMA; TSCYMQH; -.
DR OrthoDB; 1421916at2759; -.
DR PhylomeDB; Q96AQ7; -.
DR TreeFam; TF334321; -.
DR PathwayCommons; Q96AQ7; -.
DR Reactome; R-HSA-8963889; Assembly of active LPL and LIPC lipase complexes. [Q96AQ7-1]
DR Reactome; R-HSA-8964572; Lipid particle organization.
DR SignaLink; Q96AQ7; -.
DR BioGRID-ORCS; 63924; 17 hits in 1076 CRISPR screens.
DR ChiTaRS; CIDEC; human.
DR GenomeRNAi; 63924; -.
DR Pharos; Q96AQ7; Tbio.
DR PRO; PR:Q96AQ7; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q96AQ7; protein.
DR Bgee; ENSG00000187288; Expressed in subcutaneous adipose tissue and 127 other tissues.
DR ExpressionAtlas; Q96AQ7; baseline and differential.
DR Genevisible; Q96AQ7; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006915; P:apoptotic process; IDA:MGI.
DR GO; GO:0097194; P:execution phase of apoptosis; IDA:UniProtKB.
DR GO; GO:0034389; P:lipid droplet organization; IMP:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR InterPro; IPR003508; CIDE-N_dom.
DR Pfam; PF02017; CIDE-N; 1.
DR SMART; SM00266; CAD; 1.
DR PROSITE; PS51135; CIDE_N; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Apoptosis; Endoplasmic reticulum;
KW Lipid droplet; Lipid transport; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Transport; Ubl conjugation.
FT CHAIN 1..238
FT /note="Cell death activator CIDE-3"
FT /id="PRO_0000144722"
FT DOMAIN 41..118
FT /note="CIDE-N"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00447"
FT VAR_SEQ 1..74
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12429024,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_012738"
FT VAR_SEQ 69
FT /note="K -> KTRNPEARSQE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045051"
FT VAR_SEQ 70..129
FT /note="VRDTLMLADKPFFLVLEEDGTTVETEEYFQALAGDTVFMVLQKGQKWQPPSE
FT QGTRHPLS -> GSFPLGPLQHAGHRPRTAWHLLLPAAAPRCYGGRAAPQGQGLIPYPD
FT LSEDTAVKAQVLG (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_012739"
FT VAR_SEQ 130..238
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_012740"
FT CONFLICT 149
FT /note="K -> N (in Ref. 4; CD518729)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 238 AA; 26754 MW; 5CF774929E821DA5 CRC64;
MEYAMKSLSL LYPKSLSRHV SVRTSVVTQQ LLSEPSPKAP RARPCRVSTA DRSVRKGIMA
YSLEDLLLKV RDTLMLADKP FFLVLEEDGT TVETEEYFQA LAGDTVFMVL QKGQKWQPPS
EQGTRHPLSL SHKPAKKIDV ARVTFDLYKL NPQDFIGCLN VKATFYDTYS LSYDLHCCGA
KRIMKEAFRW ALFSMQATGH VLLGTSCYLQ QLLDATEEGQ PPKGKASSLI PTCLKILQ
