ID   CLN5_MOUSE              Reviewed;         341 AA.
AC   Q3UMW8; Q8C054; Q8R152;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   RecName: Full=Bis(monoacylglycero)phosphate synthase CLN5 {ECO:0000250|UniProtKB:O75503};
DE            Short=BMP synthase CLN5;
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:O75503};
DE   AltName: Full=Ceroid-lipofuscinosis neuronal protein 5;
DE            Short=Protein CLN5;
DE   AltName: Full=Palmitoyl protein thioesterase CLN5;
DE            EC=3.1.2.22 {ECO:0000269|PubMed:35427157};
DE   AltName: Full=S-depalmitoylase CLN5;
DE   Contains:
DE     RecName: Full=Bis(monoacylglycero)phosphate synthase CLN5, secreted form;
GN   Name=Cln5; Synonyms=Bmps {ECO:0000250|UniProtKB:O75503};
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Lung, and Olfactory bulb;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-341.
RC   STRAIN=FVB/N; 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   [3]
RP   INTERACTION WITH PPT1; TPP1; CLN3; CLN6; CLN8; ATP5F1A AND ATP5F1B.
RX   PubMed=19941651; DOI=10.1186/1471-2121-10-83;
RA   Lyly A., von Schantz C., Heine C., Schmiedt M.L., Sipilae T., Jalanko A.,
RA   Kyttaelae A.;
RT   "Novel interactions of CLN5 support molecular networking between neuronal
RT   ceroid lipofuscinosis proteins.";
RL   BMC Cell Biol. 10:83-83(2009).
RN   [4]
RP   SUBCELLULAR LOCATION (SECRETED FORM).
RX   PubMed=20052765; DOI=10.1002/humu.21195;
RA   Schmiedt M.L., Bessa C., Heine C., Ribeiro M.G., Jalanko A., Kyttaelae A.;
RT   "The neuronal ceroid lipofuscinosis protein CLN5: new insights into
RT   cellular maturation, transport, and consequences of mutations.";
RL   Hum. Mutat. 31:356-365(2010).
RN   [5]
RP   PROTEOLYTIC CLEAVAGE AT C-TERMINUS, AND TISSUE SPECIFICITY.
RX   PubMed=26342652; DOI=10.1016/j.yexcr.2015.08.021;
RA   De Silva B., Adams J., Lee S.Y.;
RT   "Proteolytic processing of the neuronal ceroid lipofuscinosis related
RT   lysosomal protein CLN5.";
RL   Exp. Cell Res. 338:45-53(2015).
RN   [6]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=35427157; DOI=10.1126/sciadv.abj8633;
RA   Luebben A.V., Bender D., Becker S., Crowther L.M., Erven I., Hofmann K.,
RA   Soeding J., Klemp H., Bellotti C., Staeuble A., Qiu T., Kathayat R.S.,
RA   Dickinson B.C., Gaertner J., Sheldrick G.M., Kraetzner R., Steinfeld R.;
RT   "Cln5 represents a new type of cysteine-based S-depalmitoylase linked to
RT   neurodegeneration.";
RL   Sci. Adv. 8:eabj8633-eabj8633(2022).
CC   -!- FUNCTION: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]:
CC       Catalyzes the synthesis of bis(monoacylglycero)phosphate (BMP) via
CC       transacylation of 2 molecules of lysophosphatidylglycerol (LPG). BMP
CC       also known as lysobisphosphatidic acid plays a key role in the
CC       formation of intraluminal vesicles and in maintaining intracellular
CC       cholesterol homeostasis. Can use only LPG as the exclusive
CC       lysophospholipid acyl donor for base exchange and displays BMP synthase
CC       activity towards various LPGs (LPG 14:0, LPG 16:0, LPG 18:0, LPG 18:1)
CC       with a higher preference for longer chain lengths. Plays a role in
CC       influencing the retrograde trafficking of lysosomal sorting receptors
CC       SORT1 and IGF2R from the endosomes to the trans-Golgi network by
CC       controlling the recruitment of retromer complex to the endosomal
CC       membrane. Regulates the localization and activation of RAB7A which is
CC       required to recruit the retromer complex to the endosomal membrane.
CC       {ECO:0000250|UniProtKB:O75503}.
CC   -!- FUNCTION: Exhibits palmitoyl protein thioesterase (S-depalmitoylation)
CC       activity in vitro and most likely plays a role in protein S-
CC       depalmitoylation. {ECO:0000269|PubMed:35427157}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) +
CC         hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233,
CC         Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:74151; EC=3.1.2.22;
CC         Evidence={ECO:0000269|PubMed:35427157};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19234;
CC         Evidence={ECO:0000305|PubMed:35427157};
CC   -!- CATALYTIC ACTIVITY: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]:
CC       Reaction=2 a 3-acyl-sn-glycero-1-phospho-(1'-sn-glycerol) = a 3-acyl-
CC         sn-glycero-1-phospho-(3'-acyl-1'-sn-glycerol) + sn-glycero-1-phospho-
CC         (1'-sn-glycerol); Xref=Rhea:RHEA:77619, ChEBI:CHEBI:77717,
CC         ChEBI:CHEBI:197411, ChEBI:CHEBI:197425;
CC         Evidence={ECO:0000250|UniProtKB:O75503};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77620;
CC         Evidence={ECO:0000250|UniProtKB:O75503};
CC   -!- CATALYTIC ACTIVITY: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]:
CC       Reaction=2 3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(1'-sn-glycerol) =
CC         3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(3'-(9Z-octadecenoyl)-1'-sn-
CC         glycerol) + sn-glycero-1-phospho-(1'-sn-glycerol);
CC         Xref=Rhea:RHEA:77599, ChEBI:CHEBI:139150, ChEBI:CHEBI:139152,
CC         ChEBI:CHEBI:197411; Evidence={ECO:0000250|UniProtKB:O75503};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77600;
CC         Evidence={ECO:0000250|UniProtKB:O75503};
CC   -!- CATALYTIC ACTIVITY: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]:
CC       Reaction=2 3-octadecanoyl-sn-glycero-1-phospho-(1'-sn-glycerol) = 3-
CC         octadecanoyl-sn-glycero-1-phospho-(3'-octadecanoyl-1'-sn-glycerol) +
CC         sn-glycero-1-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:77603,
CC         ChEBI:CHEBI:197411, ChEBI:CHEBI:197412, ChEBI:CHEBI:197414;
CC         Evidence={ECO:0000250|UniProtKB:O75503};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77604;
CC         Evidence={ECO:0000250|UniProtKB:O75503};
CC   -!- CATALYTIC ACTIVITY: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]:
CC       Reaction=2 3-hexadecanoyl-sn-glycero-1-phospho-(1'-sn-glycerol) = 3-
CC         hexadecanoyl-sn-glycero-1-phospho-(3'-hexadecanoyl-1'-sn-glycerol) +
CC         sn-glycero-1-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:77607,
CC         ChEBI:CHEBI:44859, ChEBI:CHEBI:197411, ChEBI:CHEBI:197415;
CC         Evidence={ECO:0000250|UniProtKB:O75503};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77608;
CC         Evidence={ECO:0000250|UniProtKB:O75503};
CC   -!- CATALYTIC ACTIVITY: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]:
CC       Reaction=2 3-tetradecanoyl-sn-glycero-1-phospho-(1'-sn-glycerol) = 3-
CC         tetradecanoyl-sn-glycero-1-phospho-(3'-tetradecanoyl-1'-sn-glycerol)
CC         + sn-glycero-1-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:77611,
CC         ChEBI:CHEBI:197411, ChEBI:CHEBI:197413, ChEBI:CHEBI:197416;
CC         Evidence={ECO:0000250|UniProtKB:O75503};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77612;
CC         Evidence={ECO:0000250|UniProtKB:O75503};
CC   -!- SUBUNIT: Multimer (By similarity). Interacts with PPT1, TPP1, CLN3,
CC       CLN6, CLN8, ATP5F1A and ATP5F1B (PubMed:19941651). Interacts with
CC       SORT1, RAB5A and RAB7A (By similarity). {ECO:0000250|UniProtKB:O75503,
CC       ECO:0000269|PubMed:19941651}.
CC   -!- SUBCELLULAR LOCATION: [Bis(monoacylglycero)phosphate synthase CLN5,
CC       secreted form]: Lysosome {ECO:0000269|PubMed:20052765}.
CC   -!- SUBCELLULAR LOCATION: [Bis(monoacylglycero)phosphate synthase CLN5]:
CC       Membrane {ECO:0000250|UniProtKB:O75503}; Single-pass type II membrane
CC       protein {ECO:0000250|UniProtKB:O75503}. Note=An amphipathic anchor
CC       region facilitates its association with the membrane.
CC       {ECO:0000250|UniProtKB:O75503}.
CC   -!- TISSUE SPECIFICITY: Heart, kidney, liver, spleen, muscle and rectum (at
CC       protein level). {ECO:0000269|PubMed:26342652}.
CC   -!- PTM: N-glycosylated with both high mannose and complex type sugars.
CC       Glycosylation is important for proper folding and trafficking to the
CC       lysosomes. {ECO:0000250|UniProtKB:O75503}.
CC   -!- PTM: [Bis(monoacylglycero)phosphate synthase CLN5]: The type II
CC       membrane signal anchor is proteolytically cleaved to produce a mature
CC       form that is transported to the lysosomes
CC       (Bis(monoacylglycero)phosphate synthase CLN5, secreted form).
CC       {ECO:0000250|UniProtKB:O75503}.
CC   -!- PTM: Can undergo proteolytic cleavage at the C-terminus, probably by a
CC       cysteine protease and may involve the removal of approximately 10-15
CC       residues from the C-terminal end (PubMed:26342652).
CC       {ECO:0000269|PubMed:26342652}.
CC   -!- SIMILARITY: Belongs to the CLN5 family. {ECO:0000305}.
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; AK032293; BAC27797.1; -; mRNA.
DR   EMBL; AK144635; BAE25980.1; -; mRNA.
DR   EMBL; BC025487; AAH25487.1; -; mRNA.
DR   CCDS; CCDS27314.1; -.
DR   RefSeq; NP_001028414.1; NM_001033242.1.
DR   AlphaFoldDB; Q3UMW8; -.
DR   SMR; Q3UMW8; -.
DR   STRING; 10090.ENSMUSP00000022721; -.
DR   GlyConnect; 2208; 1 N-Linked glycan (1 site).
DR   GlyCosmos; Q3UMW8; 7 sites, 1 glycan.
DR   GlyGen; Q3UMW8; 7 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; Q3UMW8; -.
DR   PhosphoSitePlus; Q3UMW8; -.
DR   SwissPalm; Q3UMW8; -.
DR   EPD; Q3UMW8; -.
DR   MaxQB; Q3UMW8; -.
DR   PaxDb; 10090-ENSMUSP00000022721; -.
DR   ProteomicsDB; 281645; -.
DR   Pumba; Q3UMW8; -.
DR   Ensembl; ENSMUST00000022721.8; ENSMUSP00000022721.7; ENSMUSG00000022125.8.
DR   GeneID; 211286; -.
DR   KEGG; mmu:211286; -.
DR   UCSC; uc007uwg.1; mouse.
DR   AGR; MGI:2442253; -.
DR   CTD; 1203; -.
DR   MGI; MGI:2442253; Cln5.
DR   VEuPathDB; HostDB:ENSMUSG00000022125; -.
DR   eggNOG; ENOG502QPQ5; Eukaryota.
DR   GeneTree; ENSGT00390000010065; -.
DR   HOGENOM; CLU_050387_0_0_1; -.
DR   InParanoid; Q3UMW8; -.
DR   OMA; FRPHQSF; -.
DR   OrthoDB; 2938611at2759; -.
DR   PhylomeDB; Q3UMW8; -.
DR   TreeFam; TF330864; -.
DR   BioGRID-ORCS; 211286; 1 hit in 78 CRISPR screens.
DR   ChiTaRS; Cln5; mouse.
DR   PRO; PR:Q3UMW8; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q3UMW8; Protein.
DR   Bgee; ENSMUSG00000022125; Expressed in placenta labyrinth and 254 other cell types or tissues.
DR   ExpressionAtlas; Q3UMW8; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR   GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005775; C:vacuolar lumen; IDA:MGI.
DR   GO; GO:0160121; F:bis(monoacylglycero)phosphate synthase activity; ISS:UniProtKB.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IBA:GO_Central.
DR   GO; GO:0005537; F:mannose binding; ISS:UniProtKB.
DR   GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR   GO; GO:0070085; P:glycosylation; ISS:UniProtKB.
DR   GO; GO:0007042; P:lysosomal lumen acidification; ISS:UniProtKB.
DR   GO; GO:0007040; P:lysosome organization; IMP:MGI.
DR   GO; GO:0022008; P:neurogenesis; ISS:UniProtKB.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
DR   GO; GO:0006465; P:signal peptide processing; ISS:UniProtKB.
DR   GO; GO:0007601; P:visual perception; IMP:MGI.
DR   InterPro; IPR026138; CLN5.
DR   PANTHER; PTHR15380:SF2; CEROID-LIPOFUSCINOSIS NEURONAL PROTEIN 5; 1.
DR   PANTHER; PTHR15380; CEROID-LIPOFUSCINOSIS, NEURONAL 5; 1.
DR   Pfam; PF15014; CLN5; 1.
DR   Genevisible; Q3UMW8; MM.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Membrane;
KW   Neurodegeneration; Neuronal ceroid lipofuscinosis; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..341
FT                   /note="Bis(monoacylglycero)phosphate synthase CLN5"
FT                   /id="PRO_0000330471"
FT   CHAIN           27..341
FT                   /note="Bis(monoacylglycero)phosphate synthase CLN5,
FT                   secreted form"
FT                   /id="PRO_0000438010"
FT   TOPO_DOM        1..13
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:O75503"
FT   TRANSMEM        14..30
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..341
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:O75503"
FT   REGION          287..326
FT                   /note="Membrane-anchoring"
FT                   /evidence="ECO:0000250|UniProtKB:O75503"
FT   ACT_SITE        100
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O75503"
FT   ACT_SITE        214
FT                   /note="Nucleophile; Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:O75503"
FT   SITE            26..27
FT                   /note="Cleavage; by SPPL3"
FT                   /evidence="ECO:0000250|UniProtKB:O75503"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        186
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        238
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        254
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        53..142
FT                   /evidence="ECO:0000250|UniProtKB:O75503"
FT   DISULFID        60..148
FT                   /evidence="ECO:0000250|UniProtKB:O75503"
FT   CONFLICT        6..8
FT                   /note="PCG -> TRP (in Ref. 2; AAH25487)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        42
FT                   /note="R -> H (in Ref. 1; BAC27797)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   341 AA;  39329 MW;  1969A4003CAF0E4D CRC64;
     MLRGGPCGAH WRPALALALL GLATILGASP TSGQRWPVPY KRFSFRPKTD PYCQAKYTFC
     PTGSPIPVMK DNDVIEVLRL QAPIWEFKYG DLLGHFKLMH DAVGFRSTLT GKNYTIEWYE
     LFQLGNCTFP HLRPDKSAPF WCNQGAACFF EGIDDKHWKE NGTLSVVATI SGNTFNKVAE
     WVKQDNETGI YYETWTVRAG PGQGAQTWFE SYDCSNFVLR TYKKLAEFGT EFKKIETNYT
     KIFLYSGEPI YLGNETSIFG PKGNKTLALA IKKFYGPFRP YLSTKDFLMN FLKIFDTVII
     HRQFYLFYNF EYWFLPMKPP FVKITYEETP LPTRHTTFTD L
//