ZDHC7_MOUSE
ID ZDHC7_MOUSE Reviewed; 308 AA.
AC Q91WU6; Q3TC41; Q6EMK2; Q8K1H6;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Palmitoyltransferase ZDHHC7 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000269|PubMed:15603741, ECO:0000269|PubMed:18596047, ECO:0000269|PubMed:19001095, ECO:0000269|PubMed:23687301, ECO:0000269|PubMed:25253725, ECO:0000269|PubMed:28057756};
DE AltName: Full=Acyltransferase ZDHHC7 {ECO:0000305|PubMed:28167757};
DE EC=2.3.1.- {ECO:0000305|PubMed:28167757};
DE AltName: Full=GABA-A receptor-associated membrane protein 2 {ECO:0000312|EMBL:AAO27360.1};
DE AltName: Full=SERZ-beta {ECO:0000303|PubMed:27875292};
DE AltName: Full=Zinc finger DHHC domain-containing protein 7 {ECO:0000312|MGI:MGI:2142662};
DE Short=DHHC-7 {ECO:0000303|PubMed:15603741};
GN Name=Zdhhc7 {ECO:0000312|MGI:MGI:2142662};
GN Synonyms=Gramp2 {ECO:0000312|EMBL:AAO27360.1};
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 STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15229235; DOI=10.1523/jneurosci.1037-04.2004;
RA Keller C.A., Yuan X., Panzanelli P., Martin M.L., Alldred M.,
RA Sassoe-Pognetto M., Luescher B.;
RT "The gamma2 subunit of GABA(A) receptors is a substrate for palmitoylation
RT by GODZ.";
RL J. Neurosci. 24:5881-5891(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Colon, Inner ear, Spleen, and Thymus;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Colon, Eye, and Retina;
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, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 157-ASP-HIS-158.
RX PubMed=15603741; DOI=10.1016/j.neuron.2004.12.005;
RA Fukata M., Fukata Y., Adesnik H., Nicoll R.A., Bredt D.S.;
RT "Identification of PSD-95 palmitoylating enzymes.";
RL Neuron 44:987-996(2004).
RN [5]
RP SUBUNIT.
RX PubMed=17151279; DOI=10.1523/jneurosci.4214-06.2006;
RA Fang C., Deng L., Keller C.A., Fukata M., Fukata Y., Chen G., Luescher B.;
RT "GODZ-mediated palmitoylation of GABA(A) receptors is required for normal
RT assembly and function of GABAergic inhibitory synapses.";
RL J. Neurosci. 26:12758-12768(2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ACTIVE SITE, AND
RP MUTAGENESIS OF CYS-160.
RX PubMed=18596047; DOI=10.1074/jbc.m802140200;
RA Greaves J., Salaun C., Fukata Y., Fukata M., Chamberlain L.H.;
RT "Palmitoylation and membrane interactions of the neuroprotective chaperone
RT cysteine-string protein.";
RL J. Biol. Chem. 283:25014-25026(2008).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19001095; DOI=10.1128/mcb.01144-08;
RA Tsutsumi R., Fukata Y., Noritake J., Iwanaga T., Perez F., Fukata M.;
RT "Identification of G protein alpha subunit-palmitoylating enzyme.";
RL Mol. Cell. Biol. 29:435-447(2009).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23687301; DOI=10.1074/jbc.m112.431676;
RA Oku S., Takahashi N., Fukata Y., Fukata M.;
RT "In silico screening for palmitoyl substrates reveals a role for DHHC1/3/10
RT (zDHHC1/3/11)-mediated neurochondrin palmitoylation in its targeting to
RT Rab5-positive endosomes.";
RL J. Biol. Chem. 288:19816-19829(2013).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND AUTOPALMITOYLATION.
RX PubMed=25253725; DOI=10.1091/mbc.e14-06-1169;
RA Lemonidis K., Gorleku O.A., Sanchez-Perez M.C., Grefen C.,
RA Chamberlain L.H.;
RT "The Golgi S-acylation machinery comprises zDHHC enzymes with major
RT differences in substrate affinity and S-acylation activity.";
RL Mol. Biol. Cell 25:3870-3883(2014).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=25301068; DOI=10.1038/cdd.2014.153;
RA Rossin A., Durivault J., Chakhtoura-Feghali T., Lounnas N.,
RA Gagnoux-Palacios L., Hueber A.O.;
RT "Fas palmitoylation by the palmitoyl acyltransferase DHHC7 regulates Fas
RT stability.";
RL Cell Death Differ. 22:643-653(2015).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=27875292; DOI=10.1074/jbc.m116.732768;
RA Kilpatrick C.L., Murakami S., Feng M., Wu X., Lal R., Chen G., Du K.,
RA Luscher B.;
RT "Dissociation of Golgi-associated DHHC-type Zinc Finger Protein (GODZ)- and
RT Sertoli Cell Gene with a Zinc Finger Domain-beta (SERZ-beta)-mediated
RT Palmitoylation by Loss of Function Analyses in Knock-out Mice.";
RL J. Biol. Chem. 291:27371-27386(2016).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, PALMITOYLATION, AND DISRUPTION PHENOTYPE.
RX PubMed=28057756; DOI=10.1074/jbc.m116.747139;
RA Du K., Murakami S., Sun Y., Kilpatrick C.L., Luscher B.;
RT "DHHC7 Palmitoylates Glucose Transporter 4 (Glut4) and Regulates Glut4
RT Membrane Translocation.";
RL J. Biol. Chem. 292:2979-2991(2017).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=28167757; DOI=10.1073/pnas.1612254114;
RA Greaves J., Munro K.R., Davidson S.C., Riviere M., Wojno J., Smith T.K.,
RA Tomkinson N.C., Chamberlain L.H.;
RT "Molecular basis of fatty acid selectivity in the zDHHC family of S-
RT acyltransferases revealed by click chemistry.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E1365-E1374(2017).
CC -!- FUNCTION: Golgi-localized palmitoyltransferase that catalyzes the
CC addition of palmitate onto various protein substrates and therefore
CC functions in several unrelated biological processes (PubMed:15603741,
CC PubMed:19001095, PubMed:23687301, PubMed:25253725). Has no stringent
CC fatty acid selectivity and in addition to palmitate can also transfer
CC onto target proteins myristate from tetradecanoyl-CoA and stearate from
CC octadecanoyl-CoA (Probable). Palmitoylates sex steroid hormone
CC receptors, including ESR1, PGR and AR, thereby regulating their
CC targeting to the plasma membrane and their function in rapid
CC intracellular signaling upon binding of sex hormones. Palmitoylates
CC GNAQ, a heterotrimeric G protein, regulating its dynamic localization
CC at the plasma membrane and is thereby involved in GNAQ-dependent G
CC protein-coupled receptor signaling pathways (PubMed:19001095).
CC Functions also in ligand-induced cell death by regulating the FAS
CC signaling pathway through the palmitoylation and stabilization of the
CC receptor at the plasma membrane. In epithelial cells, palmitoylates
CC SCRIB and regulates its localization to the plasma membrane, regulating
CC indirectly cell polarity and differentiation. Also palmitoylates JAM3
CC and promotes its expression at tight junctions and regulates its
CC function in cell migration (By similarity). Palmitoylates the glucose
CC transporter GLUT4/SLC2A4 and controls the insulin-dependent
CC translocation of GLUT4 to the plasma membrane (PubMed:28057756). In
CC brain, could also palmitoylate SNAP25 and DLG4/PSD95 (PubMed:15603741,
CC PubMed:25253725). Could also palmitoylate DNAJC5 and regulate its
CC localization to the Golgi membrane (PubMed:18596047). Could also
CC palmitoylate NCDN (PubMed:23687301). May play a role in follicle
CC stimulation hormone (FSH) activation of testicular Sertoli cells (By
CC similarity). {ECO:0000250|UniProtKB:Q923G5,
CC ECO:0000250|UniProtKB:Q9NXF8, ECO:0000269|PubMed:15603741,
CC ECO:0000269|PubMed:18596047, ECO:0000269|PubMed:19001095,
CC ECO:0000269|PubMed:23687301, ECO:0000269|PubMed:25253725,
CC ECO:0000269|PubMed:28057756, ECO:0000305|PubMed:28167757}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-
CC hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151;
CC EC=2.3.1.225; Evidence={ECO:0000269|PubMed:15603741,
CC ECO:0000269|PubMed:18596047, ECO:0000269|PubMed:19001095,
CC ECO:0000269|PubMed:23687301, ECO:0000269|PubMed:25253725,
CC ECO:0000269|PubMed:28057756};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000269|PubMed:28057756};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + tetradecanoyl-CoA = CoA + S-
CC tetradecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59736, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:15433, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:143199;
CC Evidence={ECO:0000305|PubMed:28167757};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737;
CC Evidence={ECO:0000305|PubMed:28167757};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + octadecanoyl-CoA = CoA + S-
CC octadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59740, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:15434, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:143200;
CC Evidence={ECO:0000305|PubMed:28167757};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741;
CC Evidence={ECO:0000305|PubMed:28167757};
CC -!- SUBUNIT: Homooligomers (PubMed:17151279). Heterooligomers with ZDHHC3
CC (PubMed:17151279). {ECO:0000269|PubMed:17151279}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:18596047, ECO:0000269|PubMed:25301068}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC liver, kidney and brain. Expressed in all brain regions.
CC {ECO:0000269|PubMed:15603741}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- PTM: Autopalmitoylated. {ECO:0000269|PubMed:25253725,
CC ECO:0000269|PubMed:28057756}.
CC -!- DISRUPTION PHENOTYPE: Homozygous knockout mice are viable, fertile and
CC do not display overt phenotype (PubMed:27875292). Knockout mice are
CC hyperglycemic, glucose intolerant and develop a type II diabetic
CC syndrome (PubMed:28057756). Zdhhc3 and Zdhhc7 double knockout mice show
CC a perinatally lethal phenotype (PubMed:27875292).
CC {ECO:0000269|PubMed:27875292, ECO:0000269|PubMed:28057756}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AY166673; AAO27360.1; -; mRNA.
DR EMBL; AK041905; BAC31093.1; -; mRNA.
DR EMBL; AK157968; BAE34289.1; -; mRNA.
DR EMBL; AK170639; BAE41929.1; -; mRNA.
DR EMBL; AK170923; BAE42116.1; -; mRNA.
DR EMBL; AK172462; BAE43018.1; -; mRNA.
DR EMBL; BC013467; AAH13467.1; -; mRNA.
DR EMBL; BC029666; AAH29666.1; -; mRNA.
DR EMBL; BC075666; AAH75666.1; -; mRNA.
DR CCDS; CCDS22715.1; -.
DR RefSeq; NP_598728.1; NM_133967.3.
DR RefSeq; XP_011246559.1; XM_011248257.2.
DR AlphaFoldDB; Q91WU6; -.
DR SMR; Q91WU6; -.
DR STRING; 10090.ENSMUSP00000034280; -.
DR iPTMnet; Q91WU6; -.
DR PhosphoSitePlus; Q91WU6; -.
DR SwissPalm; Q91WU6; -.
DR MaxQB; Q91WU6; -.
DR PaxDb; Q91WU6; -.
DR PRIDE; Q91WU6; -.
DR ProteomicsDB; 275142; -.
DR Antibodypedia; 30621; 147 antibodies from 26 providers.
DR DNASU; 102193; -.
DR Ensembl; ENSMUST00000034280; ENSMUSP00000034280; ENSMUSG00000031823.
DR GeneID; 102193; -.
DR KEGG; mmu:102193; -.
DR UCSC; uc009nqr.1; mouse.
DR CTD; 55625; -.
DR MGI; MGI:2142662; Zdhhc7.
DR VEuPathDB; HostDB:ENSMUSG00000031823; -.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000156519; -.
DR HOGENOM; CLU_048061_1_1_1; -.
DR InParanoid; Q91WU6; -.
DR OMA; WYSMING; -.
DR OrthoDB; 1491968at2759; -.
DR PhylomeDB; Q91WU6; -.
DR TreeFam; TF319798; -.
DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling.
DR BioGRID-ORCS; 102193; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q91WU6; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q91WU6; protein.
DR Bgee; ENSMUSG00000031823; Expressed in interventricular septum and 248 other tissues.
DR Genevisible; Q91WU6; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0016409; F:palmitoyltransferase activity; IDA:MGI.
DR GO; GO:0019705; F:protein-cysteine S-myristoyltransferase activity; IC:UniProtKB.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0140439; F:protein-cysteine S-stearoyltransferase activity; IC:UniProtKB.
DR GO; GO:0044381; P:glucose import in response to insulin stimulus; IMP:UniProtKB.
DR GO; GO:0009895; P:negative regulation of catabolic process; ISS:UniProtKB.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IDA:UniProtKB.
DR GO; GO:0030859; P:polarized epithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR GO; GO:1902044; P:regulation of Fas signaling pathway; ISS:UniProtKB.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0150106; P:regulation of protein localization to cell-cell junction; ISS:UniProtKB.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; IMP:UniProtKB.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Golgi apparatus; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..308
FT /note="Palmitoyltransferase ZDHHC7"
FT /id="PRO_0000212875"
FT TOPO_DOM 1..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..75
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..217
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 130..180
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 160
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067,
FT ECO:0000305|PubMed:18596047"
FT MUTAGEN 157..158
FT /note="DH->AA: Fails to enhance DLG4 palmitoylation."
FT /evidence="ECO:0000269|PubMed:15603741"
FT MUTAGEN 160
FT /note="C->S: Loss of protein-cysteine S-
FT palmitoyltransferase activity."
FT /evidence="ECO:0000305|PubMed:18596047"
FT CONFLICT 56
FT /note="L -> F (in Ref. 2; BAE42116)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 35213 MW; 03BD4CB85245DF28 CRC64;
MQPSGHRLRD IEHHPLLTDN DNYDSASSSS SETDMADRVW FIRDGCGMVC AVMTWLLVVY
ADFVVTFVML LPSKDFWYSV VNGVLFNCLA VLALSSHLRT MLTDPGAVPK GNATKEYMES
LQLKPGEVIY KCPKCCCIKP ERAHHCSICK RCIRKMDHHC PWVNNCVGEK NQRFFVLFTM
YIALSSVHAL ILCGLQFISC VRGQWTECSD FSPPITVILL VFLCLEGLLF FTFTAVMFGT
QIHSICNDET EIERLKSEKP TWERRLRWEG MKSVFGGPPS LLWMNPFVGF RLRRLQMRTR
KGGPEFSV
