VP35L_HUMAN
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 03-AUG-2022, entry version 122.
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 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 -!- 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; CCDS32397.2; -. [Q7Z3J2-1]
DR RefSeq; NP_064710.4; NM_020314.5. [Q7Z3J2-1]
DR AlphaFoldDB; Q7Z3J2; -.
DR BioGRID; 121329; 32.
DR CORUM; Q7Z3J2; -.
DR IntAct; Q7Z3J2; 18.
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; Q7Z3J2; -.
DR PeptideAtlas; Q7Z3J2; -.
DR PRIDE; Q7Z3J2; -.
DR ProteomicsDB; 69055; -. [Q7Z3J2-1]
DR ProteomicsDB; 69056; -. [Q7Z3J2-2]
DR Antibodypedia; 52453; 51 antibodies from 14 providers.
DR DNASU; 57020; -.
DR Ensembl; ENST00000417362.7; ENSP00000395973.3; ENSG00000103544.16. [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 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 PharmGKB; PA162378300; -.
DR VEuPathDB; HostDB:ENSG00000103544; -.
DR eggNOG; KOG3682; Eukaryota.
DR GeneTree; ENSGT00390000011343; -.
DR InParanoid; Q7Z3J2; -.
DR OrthoDB; 247677at2759; -.
DR PhylomeDB; Q7Z3J2; -.
DR PathwayCommons; Q7Z3J2; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q7Z3J2; -.
DR BioGRID-ORCS; 57020; 20 hits in 1069 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 193 other tissues.
DR ExpressionAtlas; Q7Z3J2; baseline and differential.
DR Genevisible; Q7Z3J2; HS.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; PTHR13673; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Endosome; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW 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
