PORCN_MOUSE
ID PORCN_MOUSE Reviewed; 461 AA.
AC Q9JJJ7; A2AC30; A2AC32; A2AC33; Q9CWT0; Q9JJJ8; Q9JJJ9; Q9JJK0;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Protein-serine O-palmitoleoyltransferase porcupine {ECO:0000305};
DE Short=mPORC;
DE EC=2.3.1.250 {ECO:0000269|PubMed:17141155, ECO:0000269|PubMed:24798332};
GN Name=Porcn {ECO:0000312|MGI:MGI:1890212}; Synonyms=Porc, Ppn;
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] (ISOFORMS 1; 2; 3 AND 4), FUNCTION IN WNT
RP PROTEINS PROCESSING, INTERACTION WITH WNT1; WNT3; WNT3A; WNT4; WNT5A;
RP WNT5B; WNT6; WNT7A AND WNT7B, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10866835; DOI=10.1046/j.1432-1033.2000.01478.x;
RA Tanaka K., Okabayashi H., Asashima M., Perrimon N., Kadowaki T.;
RT "The evolutionarily conserved porcupine gene family is involved in the
RT processing of the Wnt family.";
RL Eur. J. Biochem. 267:4300-4311(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
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].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3 AND 4).
RX PubMed=12842094; DOI=10.1016/s1065-6995(03)00080-5;
RA Tanaka K., Kitagawa Y., Kadowaki T.;
RT "Misexpression of mouse porcupine isoforms modulates the differentiation of
RT P19 embryonic carcinoma cells.";
RL Cell Biol. Int. 27:549-557(2003).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17141155; DOI=10.1016/j.devcel.2006.10.003;
RA Takada R., Satomi Y., Kurata T., Ueno N., Norioka S., Kondoh H., Takao T.,
RA Takada S.;
RT "Monounsaturated fatty acid modification of Wnt protein: its role in Wnt
RT secretion.";
RL Dev. Cell 11:791-801(2006).
RN [7]
RP FUNCTION.
RX PubMed=22046319; DOI=10.1371/journal.pone.0026636;
RA Galli L.M., Burrus L.W.;
RT "Differential palmit(e)oylation of Wnt1 on C93 and S224 residues has
RT overlapping and distinct consequences.";
RL PLoS ONE 6:E26636-E26636(2011).
RN [8]
RP FUNCTION.
RX PubMed=24055053; DOI=10.1016/j.celrep.2013.08.027;
RA Rios-Esteves J., Resh M.D.;
RT "Stearoyl CoA desaturase is required to produce active, lipid-modified Wnt
RT proteins.";
RL Cell Rep. 4:1072-1081(2013).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH WNT3A,
RP ACTIVE SITE, AND MUTAGENESIS OF SER-136; SER-172; ARG-228; TRP-305;
RP ASN-306; TRP-312; TYR-316; LEU-331; TYR-334; SER-337; LEU-340; HIS-341 AND
RP ARG-365.
RX PubMed=24798332; DOI=10.1074/jbc.m114.561209;
RA Rios-Esteves J., Haugen B., Resh M.D.;
RT "Identification of key residues and regions important for porcupine-
RT mediated Wnt acylation.";
RL J. Biol. Chem. 289:17009-17019(2014).
CC -!- FUNCTION: Protein-serine O-palmitoleoyltransferase that acts as a key
CC regulator of the Wnt signaling pathway by mediating the attachment of
CC palmitoleate, a 16-carbon monounsaturated fatty acid (C16:1), to Wnt
CC proteins. Serine palmitoleylation of WNT proteins is required for
CC efficient binding to frizzled receptors. {ECO:0000269|PubMed:10866835,
CC ECO:0000269|PubMed:17141155, ECO:0000269|PubMed:22046319,
CC ECO:0000269|PubMed:24055053, ECO:0000269|PubMed:24798332}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + [Wnt protein]-L-serine = [Wnt
CC protein]-O-(9Z)-hexadecenoyl-L-serine + CoA; Xref=Rhea:RHEA:45336,
CC Rhea:RHEA-COMP:11170, Rhea:RHEA-COMP:11171, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:61540, ChEBI:CHEBI:85189;
CC EC=2.3.1.250; Evidence={ECO:0000269|PubMed:17141155,
CC ECO:0000269|PubMed:24798332};
CC -!- SUBUNIT: Interacts with WNT1, WNT3, WNT3A, WNT4, WNT5A, WNT5B, WNT6,
CC WNT7A and WNT7B. {ECO:0000269|PubMed:10866835,
CC ECO:0000269|PubMed:24798332}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10866835, ECO:0000269|PubMed:24798332}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:10866835}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=D;
CC IsoId=Q9JJJ7-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q9JJJ7-2; Sequence=VSP_015892;
CC Name=3; Synonyms=C;
CC IsoId=Q9JJJ7-3; Sequence=VSP_015891;
CC Name=4; Synonyms=A;
CC IsoId=Q9JJJ7-4; Sequence=VSP_015890;
CC Name=5;
CC IsoId=Q9JJJ7-5; Sequence=VSP_015889, VSP_015893;
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung,
CC muscle, spleen and testis. Isoform 4 is strongly expressed in kidney,
CC liver, lung, spleen and testis. Isoform 1 is strongly expressed in
CC brain, heart and muscle and poorly in kidney, liver, lung, spleen and
CC testis. {ECO:0000269|PubMed:10866835}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1, isoform 2, isoform 3 and isoform 4 are
CC expressed at different levels in embryo at 9.5, 10.5, 11.5, 12.5, 13.5
CC and 15.5 dpc. {ECO:0000269|PubMed:10866835}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC Porcupine subfamily. {ECO:0000305}.
CC -!- CAUTION: Was initially thought to mediate palmitoylation of Wnt
CC proteins. It was later shown that it instead acts as a serine O-
CC palmitoleoyltransferase that mediates the attachment of palmitoleate, a
CC 16-carbon monounsaturated fatty acid (C16:1), to Wnt proteins
CC (PubMed:17141155, PubMed:24798332). {ECO:0000269|PubMed:17141155,
CC ECO:0000269|PubMed:24798332}.
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DR EMBL; AB036746; BAA89467.1; -; mRNA.
DR EMBL; AB036747; BAA89468.1; -; mRNA.
DR EMBL; AB036748; BAA89469.1; -; mRNA.
DR EMBL; AB036749; BAA89470.1; -; mRNA.
DR EMBL; AK010405; BAB26914.1; -; mRNA.
DR EMBL; AL663032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032284; AAH32284.1; -; mRNA.
DR CCDS; CCDS29990.1; -. [Q9JJJ7-4]
DR CCDS; CCDS29991.1; -. [Q9JJJ7-1]
DR CCDS; CCDS29992.1; -. [Q9JJJ7-3]
DR CCDS; CCDS29993.1; -. [Q9JJJ7-2]
DR RefSeq; NP_001295403.1; NM_001308474.1. [Q9JJJ7-5]
DR RefSeq; NP_058609.1; NM_016913.4. [Q9JJJ7-4]
DR RefSeq; NP_076127.1; NM_023638.4. [Q9JJJ7-1]
DR RefSeq; NP_665914.1; NM_145907.4. [Q9JJJ7-3]
DR RefSeq; NP_665915.1; NM_145908.4. [Q9JJJ7-2]
DR AlphaFoldDB; Q9JJJ7; -.
DR BioGRID; 207344; 9.
DR IntAct; Q9JJJ7; 7.
DR STRING; 10090.ENSMUSP00000076790; -.
DR BindingDB; Q9JJJ7; -.
DR ChEMBL; CHEMBL1255164; -.
DR PhosphoSitePlus; Q9JJJ7; -.
DR MaxQB; Q9JJJ7; -.
DR PaxDb; Q9JJJ7; -.
DR PRIDE; Q9JJJ7; -.
DR ProteomicsDB; 291767; -. [Q9JJJ7-1]
DR ProteomicsDB; 291768; -. [Q9JJJ7-2]
DR ProteomicsDB; 291769; -. [Q9JJJ7-3]
DR ProteomicsDB; 291770; -. [Q9JJJ7-4]
DR ProteomicsDB; 291771; -. [Q9JJJ7-5]
DR Antibodypedia; 25667; 111 antibodies from 21 providers.
DR DNASU; 53627; -.
DR Ensembl; ENSMUST00000077595; ENSMUSP00000076790; ENSMUSG00000031169. [Q9JJJ7-1]
DR Ensembl; ENSMUST00000082320; ENSMUSP00000080937; ENSMUSG00000031169. [Q9JJJ7-2]
DR Ensembl; ENSMUST00000089402; ENSMUSP00000086824; ENSMUSG00000031169. [Q9JJJ7-4]
DR Ensembl; ENSMUST00000089403; ENSMUSP00000086825; ENSMUSG00000031169. [Q9JJJ7-3]
DR GeneID; 53627; -.
DR KEGG; mmu:53627; -.
DR UCSC; uc009soj.2; mouse. [Q9JJJ7-1]
DR UCSC; uc009sok.2; mouse. [Q9JJJ7-2]
DR UCSC; uc009sol.2; mouse. [Q9JJJ7-3]
DR UCSC; uc009som.2; mouse. [Q9JJJ7-4]
DR UCSC; uc012heo.1; mouse. [Q9JJJ7-5]
DR CTD; 64840; -.
DR MGI; MGI:1890212; Porcn.
DR VEuPathDB; HostDB:ENSMUSG00000031169; -.
DR eggNOG; KOG4312; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_048745_0_0_1; -.
DR InParanoid; Q9JJJ7; -.
DR OMA; YIYSPAT; -.
DR OrthoDB; 975725at2759; -.
DR PhylomeDB; Q9JJJ7; -.
DR TreeFam; TF313724; -.
DR BRENDA; 2.3.1.250; 3474.
DR BioGRID-ORCS; 53627; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q9JJJ7; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9JJJ7; protein.
DR Bgee; ENSMUSG00000031169; Expressed in primary visual cortex and 175 other tissues.
DR ExpressionAtlas; Q9JJJ7; baseline and differential.
DR Genevisible; Q9JJJ7; MM.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0008374; F:O-acyltransferase activity; TAS:Reactome.
DR GO; GO:1990698; F:palmitoleoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0017147; F:Wnt-protein binding; IPI:UniProtKB.
DR GO; GO:0009100; P:glycoprotein metabolic process; IDA:MGI.
DR GO; GO:0030258; P:lipid modification; IBA:GO_Central.
DR GO; GO:0006497; P:protein lipidation; IDA:UniProtKB.
DR GO; GO:0045234; P:protein palmitoleylation; IDA:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; IBA:GO_Central.
DR GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; IDA:SynGO.
DR GO; GO:0061355; P:Wnt protein secretion; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IDA:UniProtKB.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Wnt signaling pathway.
FT CHAIN 1..461
FT /note="Protein-serine O-palmitoleoyltransferase porcupine"
FT /id="PRO_0000213138"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..66
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..152
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..252
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..396
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 341
FT /evidence="ECO:0000269|PubMed:24798332"
FT VAR_SEQ 1..234
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015889"
FT VAR_SEQ 229..240
FT /note="NKKRKARGTMVR -> K (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10866835"
FT /id="VSP_015890"
FT VAR_SEQ 229..235
FT /note="NKKRKAR -> K (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10866835,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_015891"
FT VAR_SEQ 235..239
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10866835"
FT /id="VSP_015892"
FT VAR_SEQ 235..239
FT /note="RGTMV -> MAQDA (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015893"
FT MUTAGEN 136
FT /note="S->F: Impaired acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:24798332"
FT MUTAGEN 172
FT /note="S->A: Does not affect acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:24798332"
FT MUTAGEN 228
FT /note="R->C: Does not affect acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:24798332"
FT MUTAGEN 305
FT /note="W->A: Impaired acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:24798332"
FT MUTAGEN 306
FT /note="N->A: Does not affect acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:24798332"
FT MUTAGEN 312
FT /note="W->A: Does not affect acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:24798332"
FT MUTAGEN 316
FT /note="Y->A: Impaired acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:24798332"
FT MUTAGEN 331
FT /note="L->R: Impaired acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:24798332"
FT MUTAGEN 334
FT /note="Y->A: Impaired acyltransferase activity. Impaired
FT ability to interact with WNT3A."
FT /evidence="ECO:0000269|PubMed:24798332"
FT MUTAGEN 337
FT /note="S->A: Abolished acyltransferase activity. Impaired
FT ability to interact with WNT3A."
FT /evidence="ECO:0000269|PubMed:24798332"
FT MUTAGEN 340
FT /note="L->A: Abolished acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:24798332"
FT MUTAGEN 341
FT /note="H->A: Abolished acyltransferase activity. Impaired
FT ability to interact with WNT3A."
FT /evidence="ECO:0000269|PubMed:24798332"
FT MUTAGEN 365
FT /note="R->Q: Impaired acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:24798332"
SQ SEQUENCE 461 AA; 52508 MW; 25A52681C251A0A6 CRC64;
MATFSRQEFF QQLLQGCLLP TVQQGLDQIW LLLTICFACR LLWRLGLPSY LKHASTVAGG
FFSLYHFFQL HMVWVVLLSL LCYLVLFLCR HSSHRGVFLS VTILIYLLMG EMHMVDTVTW
HKMRGAQMIV AMKAVSLGFD LDRGEVGAVP SPVEFMGYLY FVGTIVFGPW ISFHSYLQAV
QGRPLSRRWL KKVARSLALA LLCLVLSTCV GPYLFPYFIP LDGDRLLRNK KRKARGTMVR
WLRAYESAVS FHFSNYFVGF LSEATATLAG AGFTEEKDHL EWDLTVSRPL NVELPRSMVE
VVTSWNLPMS YWLNNYVFKN ALRLGTFSAV LVTYAASALL HGFSFHLAAV LLSLAFITYV
EHVLRKRLAQ ILSACILSKR CLPDCSHRHR LGLGVRALNL LFGALAIFHL SYLGSLFDVD
VDDTTEEQGY GMAYTVHKWS ELSWASHWVT FGCWIFYRLI G
