ID   VP35L_HUMAN             Reviewed;         963 AA.
AC   Q7Z3J2; A8K2M1; O43329; Q69YI1; Q6PDA0; Q7L371; Q86W66; Q8WXA5; Q9H0L7;
AC   Q9H7C8;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   27-MAR-2024, entry version 130.
DE   RecName: Full=VPS35 endosomal protein-sorting factor-like {ECO:0000305};
DE   AltName: Full=Esophageal cancer-associated protein;
GN   Name=VPS35L {ECO:0000312|HGNC:HGNC:24641};
GN   Synonyms=C16orf62 {ECO:0000312|HGNC:HGNC:24641}; ORFNames=101F10.2;
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] (ISOFORM 2).
RA   Lu J., Liu Z., Hu G., Wu M., Wang X.;
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tongue;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Heart;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS CYS-32 AND
RP   VAL-506.
RC   TISSUE=Pancreas, and Uterus;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 396-963 (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 758-963.
RX   PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA   Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA   Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA   Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA   Adams M.D.;
RT   "Genome duplications and other features in 12 Mb of DNA sequence from human
RT   chromosome 16p and 16q.";
RL   Genomics 60:295-308(1999).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [9]
RP   FUNCTION, IDENTIFICATION IN THE CCC COMPLEX, SUBCELLULAR LOCATION, AND
RP   SUBUNIT.
RX   PubMed=25355947; DOI=10.1091/mbc.e14-06-1073;
RA   Phillips-Krawczak C.A., Singla A., Starokadomskyy P., Deng Z.,
RA   Osborne D.G., Li H., Dick C.J., Gomez T.S., Koenecke M., Zhang J.S.,
RA   Dai H., Sifuentes-Dominguez L.F., Geng L.N., Kaufmann S.H., Hein M.Y.,
RA   Wallis M., McGaughran J., Gecz J., van de Sluis B., Billadeau D.D.,
RA   Burstein E.;
RT   "COMMD1 is linked to the WASH complex and regulates endosomal trafficking
RT   of the copper transporter ATP7A.";
RL   Mol. Biol. Cell 26:91-103(2015).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [11]
RP   FUNCTION, INTERACTION WITH CCDC22; SNX17 AND SNX31, IDENTIFICATION IN THE
RP   RETRIEVER COMPLEX, SUBCELLULAR LOCATION, AND FUNCTION (MICROBIAL
RP   INFECTION).
RX   PubMed=28892079; DOI=10.1038/ncb3610;
RA   McNally K.E., Faulkner R., Steinberg F., Gallon M., Ghai R., Pim D.,
RA   Langton P., Pearson N., Danson C.M., Naegele H., Morris L.L., Singla A.,
RA   Overlee B.L., Heesom K.J., Sessions R., Banks L., Collins B.M., Berger I.,
RA   Billadeau D.D., Burstein E., Cullen P.J.;
RT   "Retriever is a multiprotein complex for retromer-independent endosomal
RT   cargo recycling.";
RL   Nat. Cell Biol. 19:1214-1225(2017).
RN   [12]
RP   INTERACTION WITH VPS29, INVOLVEMENT IN RTSC3, VARIANT RTSC3 THR-830, AND
RP   CHARACTERIZATION OF VARIANT RTSC3 THR-830.
RX   PubMed=31712251; DOI=10.1136/jmedgenet-2019-106213;
RA   Kato K., Oka Y., Muramatsu H., Vasilev F.F., Otomo T., Oishi H., Kawano Y.,
RA   Kidokoro H., Nakazawa Y., Ogi T., Takahashi Y., Saitoh S.;
RT   "Biallelic VPS35L pathogenic variants cause 3C/Ritscher-Schinzel-like
RT   syndrome through dysfunction of retriever complex.";
RL   J. Med. Genet. 57:245-253(2020).
CC   -!- FUNCTION: Acts as a component of the retriever complex. The retriever
CC       complex is a heterotrimeric complex related to retromer cargo-selective
CC       complex (CSC) and essential for retromer-independent retrieval and
CC       recycling of numerous cargos such as integrin alpha-5/beta-1
CC       (ITGA5:ITGB1) (PubMed:28892079). The recruitment of the retriever
CC       complex to the endosomal membrane involves CCC and WASH complexes
CC       (PubMed:28892079). In the endosomes, drives the retrieval and recycling
CC       of NxxY-motif-containing cargo proteins by coupling to SNX17, a cargo
CC       essential for the homeostatic maintenance of numerous cell surface
CC       proteins associated with processes that include cell migration, cell
CC       adhesion, nutrient supply and cell signaling (PubMed:28892079).
CC       Involved in copper-dependent ATP7A trafficking between the trans-Golgi
CC       network and vesicles in the cell periphery; the function is proposed to
CC       depend on its association with the CCC complex and cooperation with the
CC       WASH complex on early endosomes. Seems not to be required for CCC
CC       complex stability (PubMed:25355947). {ECO:0000269|PubMed:25355947,
CC       ECO:0000269|PubMed:28892079}.
CC   -!- FUNCTION: (Microbial infection) The heterotrimeric retriever complex,
CC       in collaboration with the CCC complex, mediates the exit of human
CC       papillomavirus to the cell surface. {ECO:0000269|PubMed:28892079}.
CC   -!- SUBUNIT: Component of the heterotrimeric retriever complex formed by
CC       VPS26C, VPS29 and VPS35L (PubMed:28892079). Interacts with VPS29
CC       (PubMed:31712251). Interacts with COMMD1, CCDC93 and CCDC22; associates
CC       with the CCC (COMMD/CCDC22/CCDC93) complex which contains at least
CC       COMMD1 (and possibly other COMM domain-containing proteins), CCDC22 and
CC       CCDC93 (PubMed:25355947, PubMed:28892079). Interacts with WASHC1,
CC       WASHC2A and WASHC2C (PubMed:25355947). Interacts with SNX17 and SNX31
CC       (PubMed:28892079). {ECO:0000269|PubMed:25355947,
CC       ECO:0000269|PubMed:28892079, ECO:0000269|PubMed:31712251}.
CC   -!- INTERACTION:
CC       Q7Z3J2; O14972: VPS26C; NbExp=7; IntAct=EBI-11080070, EBI-7207091;
CC       Q7Z3J2; Q9UBQ0: VPS29; NbExp=12; IntAct=EBI-11080070, EBI-718596;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}. Endosome {ECO:0000269|PubMed:25355947,
CC       ECO:0000269|PubMed:28892079}. Note=Endosome location is dependent of
CC       the association with the CCC and WASH complexes.
CC       {ECO:0000269|PubMed:28892079}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7Z3J2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7Z3J2-2; Sequence=VSP_029536, VSP_029537, VSP_029538;
CC   -!- DISEASE: Ritscher-Schinzel syndrome 3 (RTSC3) [MIM:619135]: A form of
CC       Ritscher-Schinzel syndrome, a developmental malformation syndrome
CC       characterized by cerebellar brain malformations, congenital heart
CC       defects, and craniofacial abnormalities. RTSC3 is an autosomal
CC       recessive form. Affected individuals show cranio-cerebello-cardiac
CC       anomalies, coloboma, microphthalmia, chondrodysplasia punctata,
CC       complicated skeletal malformations, periventricular nodular heterotopia
CC       and proteinuria. {ECO:0000269|PubMed:31712251}. Note=The disease may be
CC       caused by variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the VPS35L family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH14900.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAD97869.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF461052; AAL67806.2; -; mRNA.
DR   EMBL; AK024693; BAB14965.1; -; mRNA.
DR   EMBL; AK290286; BAF82975.1; -; mRNA.
DR   EMBL; BX537867; CAD97869.1; ALT_INIT; mRNA.
DR   EMBL; AL833428; CAH10399.1; -; mRNA.
DR   EMBL; BC014900; AAH14900.2; ALT_INIT; mRNA.
DR   EMBL; BC050464; AAH50464.1; -; mRNA.
DR   EMBL; BC058845; AAH58845.1; -; mRNA.
DR   EMBL; AL136744; CAB66678.1; -; mRNA.
DR   EMBL; AC002550; AAC05806.1; -; Genomic_DNA.
DR   CCDS; CCDS32397.3; -. [Q7Z3J2-1]
DR   RefSeq; NP_064710.4; NM_020314.5. [Q7Z3J2-1]
DR   PDB; 8SYM; EM; 3.20 A; A=1-963.
DR   PDB; 8SYN; EM; 2.94 A; A=1-963.
DR   PDB; 8SYO; EM; 2.94 A; A=1-963.
DR   PDBsum; 8SYM; -.
DR   PDBsum; 8SYN; -.
DR   PDBsum; 8SYO; -.
DR   AlphaFoldDB; Q7Z3J2; -.
DR   EMDB; EMD-40884; -.
DR   EMDB; EMD-40885; -.
DR   EMDB; EMD-40886; -.
DR   SMR; Q7Z3J2; -.
DR   BioGRID; 121329; 43.
DR   ComplexPortal; CPX-2211; Commander complex.
DR   CORUM; Q7Z3J2; -.
DR   IntAct; Q7Z3J2; 23.
DR   MINT; Q7Z3J2; -.
DR   STRING; 9606.ENSP00000251143; -.
DR   iPTMnet; Q7Z3J2; -.
DR   PhosphoSitePlus; Q7Z3J2; -.
DR   BioMuta; C16orf62; -.
DR   EPD; Q7Z3J2; -.
DR   jPOST; Q7Z3J2; -.
DR   MassIVE; Q7Z3J2; -.
DR   MaxQB; Q7Z3J2; -.
DR   PaxDb; 9606-ENSP00000251143; -.
DR   PeptideAtlas; Q7Z3J2; -.
DR   ProteomicsDB; 69055; -. [Q7Z3J2-1]
DR   ProteomicsDB; 69056; -. [Q7Z3J2-2]
DR   Pumba; Q7Z3J2; -.
DR   Antibodypedia; 52453; 53 antibodies from 15 providers.
DR   DNASU; 57020; -.
DR   Ensembl; ENST00000417362.7; ENSP00000395973.3; ENSG00000103544.17. [Q7Z3J2-1]
DR   GeneID; 57020; -.
DR   KEGG; hsa:57020; -.
DR   MANE-Select; ENST00000417362.7; ENSP00000395973.3; NM_020314.7; NP_064710.5.
DR   UCSC; uc059rnn.1; human. [Q7Z3J2-1]
DR   AGR; HGNC:24641; -.
DR   CTD; 57020; -.
DR   DisGeNET; 57020; -.
DR   GeneCards; VPS35L; -.
DR   HGNC; HGNC:24641; VPS35L.
DR   HPA; ENSG00000103544; Low tissue specificity.
DR   MalaCards; VPS35L; -.
DR   MIM; 618981; gene.
DR   MIM; 619135; phenotype.
DR   neXtProt; NX_Q7Z3J2; -.
DR   OpenTargets; ENSG00000103544; -.
DR   Orphanet; 7; 3C syndrome.
DR   PharmGKB; PA162378300; -.
DR   VEuPathDB; HostDB:ENSG00000103544; -.
DR   eggNOG; KOG3682; Eukaryota.
DR   GeneTree; ENSGT00390000011343; -.
DR   InParanoid; Q7Z3J2; -.
DR   OrthoDB; 179316at2759; -.
DR   PhylomeDB; Q7Z3J2; -.
DR   PathwayCommons; Q7Z3J2; -.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   SignaLink; Q7Z3J2; -.
DR   BioGRID-ORCS; 57020; 28 hits in 1150 CRISPR screens.
DR   ChiTaRS; VPS35L; human.
DR   GenomeRNAi; 57020; -.
DR   Pharos; Q7Z3J2; Tdark.
DR   PRO; PR:Q7Z3J2; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q7Z3J2; Protein.
DR   Bgee; ENSG00000103544; Expressed in buccal mucosa cell and 195 other cell types or tissues.
DR   ExpressionAtlas; Q7Z3J2; baseline and differential.
DR   GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR   GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR   GO; GO:0006893; P:Golgi to plasma membrane transport; IMP:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR029705; VPS35L.
DR   PANTHER; PTHR13673; ESOPHAGEAL CANCER ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR13673:SF0; VPS35 ENDOSOMAL PROTEIN-SORTING FACTOR-LIKE; 1.
DR   Genevisible; Q7Z3J2; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Disease variant; Endosome; Membrane;
KW   Phosphoprotein; Protein transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..963
FT                   /note="VPS35 endosomal protein-sorting factor-like"
FT                   /id="PRO_0000311352"
FT   TRANSMEM        703..719
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          43..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         265
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..122
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_029536"
FT   VAR_SEQ         123..144
FT                   /note="EILARYTTTEKLSINLFMGSEK -> MPPLGVLVHEKSHLCDVNSFCL (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_029537"
FT   VAR_SEQ         214..243
FT                   /note="CSKLLSDTSVIQFYPSKFVLITDILDTFGK -> EE (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_029538"
FT   VARIANT         32
FT                   /note="Y -> C (in dbSNP:rs17854969)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_037230"
FT   VARIANT         186
FT                   /note="N -> I (in dbSNP:rs7206637)"
FT                   /id="VAR_037231"
FT   VARIANT         506
FT                   /note="A -> V (in dbSNP:rs17854970)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_037232"
FT   VARIANT         830
FT                   /note="A -> T (in RTSC3; does not interact with VPS29;
FT                   dbSNP:rs747119819)"
FT                   /evidence="ECO:0000269|PubMed:31712251"
FT                   /id="VAR_085197"
FT   CONFLICT        168
FT                   /note="F -> S (in Ref. 3; CAH10399)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        340
FT                   /note="C -> G (in Ref. 1; AAL67806)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        675
FT                   /note="I -> V (in Ref. 3; CAD97869)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   963 AA;  109563 MW;  5500471390F85683 CRC64;
     MAVFPWHSRN RNYKAEFASC RLEAVPLEFG DYHPLKPITV TESKTKKVNR KGSTSSTSSS
     SSSSVVDPLS SVLDGTDPLS MFAATADPAA LAAAMDSSRR KRDRDDNSVV GSDFEPWTNK
     RGEILARYTT TEKLSINLFM GSEKGKAGTA TLAMSEKVRT RLEELDDFEE GSQKELLNLT
     QQDYVNRIEE LNQSLKDAWA SDQKVKALKI VIQCSKLLSD TSVIQFYPSK FVLITDILDT
     FGKLVYERIF SMCVDSRSVL PDHFSPENAN DTAKETCLNW FFKIASIREL IPRFYVEASI
     LKCNKFLSKT GISECLPRLT CMIRGIGDPL VSVYARAYLC RVGMEVAPHL KETLNKNFFD
     FLLTFKQIHG DTVQNQLVVQ GVELPSYLPL YPPAMDWIFQ CISYHAPEAL LTEMMERCKK
     LGNNALLLNS VMSAFRAEFI ATRSMDFIGM IKECDESGFP KHLLFRSLGL NLALADPPES
     DRLQILNEAW KVITKLKNPQ DYINCAEVWV EYTCKHFTKR EVNTVLADVI KHMTPDRAFE
     DSYPQLQLII KKVIAHFHDF SVLFSVEKFL PFLDMFQKES VRVEVCKCIM DAFIKHQQEP
     TKDPVILNAL LHVCKTMHDS VNALTLEDEK RMLSYLINGF IKMVSFGRDF EQQLSFYVES
     RSMFCNLEPV LVQLIHSVNR LAMETRKVMK GNHSRKTAAF VRACVAYCFI TIPSLAGIFT
     RLNLYLHSGQ VALANQCLSQ ADAFFKAAIS LVPEVPKMIN IDGKMRPSES FLLEFLCNFF
     STLLIVPDHP EHGVLFLVRE LLNVIQDYTW EDNSDEKIRI YTCVLHLLSA MSQETYLYHI
     DKVDSNDSLY GGDSKFLAEN NKLCETVMAQ ILEHLKTLAK DEALKRQSSL GLSFFNSILA
     HGDLRNNKLN QLSVNLWHLA QRHGCADTRT MVKTLEYIKK QSKQPDMTHL TELALRLPLQ
     TRT
//