SNX33_HUMAN
ID SNX33_HUMAN Reviewed; 574 AA.
AC Q8WV41; B1NM17;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Sorting nexin-33;
DE AltName: Full=SH3 and PX domain-containing protein 3;
GN Name=SNX33; Synonyms=SH3PX3, SH3PXD3C, SNX30;
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], AND INTERACTION WITH ADAM15.
RX PubMed=16374509; DOI=10.1038/sj.embor.7400596;
RA Kaerkkaeinen S., Hiipakka M., Wang J.-H., Kleino I., Vaehae-Jaakkola M.,
RA Renkema G.H., Liss M., Wagner R., Saksela K.;
RT "Identification of preferred protein interactions by phage-display of the
RT human Src homology-3 proteome.";
RL EMBO Rep. 7:186-191(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH DNM1 AND DNM2,
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=18353773; DOI=10.1074/jbc.m801531200;
RA Schobel S., Neumann S., Hertweck M., Dislich B., Kuhn P.H., Kremmer E.,
RA Seed B., Baumeister R., Haass C., Lichtenthaler S.F.;
RT "A novel sorting nexin modulates endocytic trafficking and alpha-secretase
RT cleavage of the amyloid precursor protein.";
RL J. Biol. Chem. 283:14257-14268(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Stomach;
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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP FUNCTION.
RX PubMed=18419754; DOI=10.1111/j.1600-0854.2008.00750.x;
RA Heiseke A., Schobel S., Lichtenthaler S.F., Vorberg I., Groschup M.H.,
RA Kretzschmar H., Schatzl H.M., Nunziante M.;
RT "The novel sorting nexin SNX33 interferes with cellular PrP formation by
RT modulation of PrP shedding.";
RL Traffic 9:1116-1129(2008).
RN [8]
RP INTERACTION WITH FASLG.
RX PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA Voss M., Lettau M., Janssen O.;
RT "Identification of SH3 domain interaction partners of human FasL (CD178) by
RT phage display screening.";
RL BMC Immunol. 10:53-53(2009).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH WASL.
RX PubMed=19487689; DOI=10.1074/jbc.m109.007278;
RA Zhang J., Zhang X., Guo Y., Xu L., Pei D.;
RT "Sorting nexin 33 induces mammalian cell micronucleated phenotype and actin
RT polymerization by interacting with Wiskott-Aldrich syndrome protein.";
RL J. Biol. Chem. 284:21659-21669(2009).
RN [10]
RP INTERACTION WITH ADAM15.
RX PubMed=19718658; DOI=10.1002/jcb.22317;
RA Kleino I., Ortiz R.M., Yritys M., Huovila A.P., Saksela K.;
RT "Alternative splicing of ADAM15 regulates its interactions with cellular
RT SH3 proteins.";
RL J. Cell. Biochem. 108:877-885(2009).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21048941; DOI=10.1371/journal.pone.0013763;
RA Wang J.T., Kerr M.C., Karunaratne S., Jeanes A., Yap A.S., Teasdale R.D.;
RT "The SNX-PX-BAR family in macropinocytosis: the regulation of macropinosome
RT formation by SNX-PX-BAR proteins.";
RL PLoS ONE 5:E13763-E13763(2010).
RN [12]
RP FUNCTION, DOMAIN, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=20964629; DOI=10.1042/bj20100709;
RA Dislich B., Than M.E., Lichtenthaler S.F.;
RT "Specific amino acids in the BAR domain allow homodimerization and prevent
RT heterodimerization of sorting nexin 33.";
RL Biochem. J. 433:75-83(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22718350; DOI=10.1242/jcs.105981;
RA Ma M.P., Chircop M.;
RT "SNX9, SNX18 and SNX33 are required for progression through and completion
RT of mitosis.";
RL J. Cell Sci. 125:4372-4382(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-92, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [16]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 212-574.
RG Structural genomics consortium (SGC);
RT "Structure of human sorting nexin 33.";
RL Submitted (DEC-2012) to the PDB data bank.
CC -!- FUNCTION: Plays a role in the reorganization of the cytoskeleton,
CC endocytosis and cellular vesicle trafficking via its interactions with
CC membranes, WASL, DNM1 and DNM2. Acts both during interphase and at the
CC end of mitotic cell divisions. Required for efficient progress through
CC mitosis and cytokinesis. Required for normal formation of the cleavage
CC furrow at the end of mitosis. Modulates endocytosis of cell-surface
CC proteins, such as APP and PRNP; this then modulates the secretion of
CC APP and PRNP peptides. Promotes membrane tubulation (in vitro). May
CC promote the formation of macropinosomes. {ECO:0000269|PubMed:18353773,
CC ECO:0000269|PubMed:18419754, ECO:0000269|PubMed:19487689,
CC ECO:0000269|PubMed:20964629, ECO:0000269|PubMed:21048941,
CC ECO:0000269|PubMed:22718350}.
CC -!- SUBUNIT: Homodimer (via BAR domain). Interacts with ADAM15. Interacts
CC with FASLG. Interacts (via SH3 domain) with DNM1 and DNM2. Interacts
CC with WASL. Interacts with FCHSD1 (via the F-BAR domain) (By
CC similarity). {ECO:0000250|UniProtKB:Q4VAA7,
CC ECO:0000269|PubMed:16374509, ECO:0000269|PubMed:18353773,
CC ECO:0000269|PubMed:19487689, ECO:0000269|PubMed:19718658,
CC ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:20964629}.
CC -!- INTERACTION:
CC Q8WV41; Q13444: ADAM15; NbExp=4; IntAct=EBI-2481535, EBI-77818;
CC Q8WV41; Q13444-2: ADAM15; NbExp=3; IntAct=EBI-2481535, EBI-12137265;
CC Q8WV41; P05067: APP; NbExp=3; IntAct=EBI-2481535, EBI-77613;
CC Q8WV41; Q05193: DNM1; NbExp=2; IntAct=EBI-2481535, EBI-713135;
CC Q8WV41; P50570-2: DNM2; NbExp=3; IntAct=EBI-2481535, EBI-10968534;
CC Q8WV41; Q7L190: DPPA4; NbExp=5; IntAct=EBI-2481535, EBI-710457;
CC Q8WV41; P48023: FASLG; NbExp=3; IntAct=EBI-2481535, EBI-495538;
CC Q8WV41; P42858: HTT; NbExp=6; IntAct=EBI-2481535, EBI-466029;
CC Q8WV41; Q92993: KAT5; NbExp=3; IntAct=EBI-2481535, EBI-399080;
CC Q8WV41; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-2481535, EBI-11742507;
CC Q8WV41; P41227: NAA10; NbExp=3; IntAct=EBI-2481535, EBI-747693;
CC Q8WV41; Q96HR8: NAF1; NbExp=4; IntAct=EBI-2481535, EBI-2515597;
CC Q8WV41; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-2481535, EBI-9090795;
CC Q8WV41; Q8WV41: SNX33; NbExp=2; IntAct=EBI-2481535, EBI-2481535;
CC Q8WV41; Q9Y5X1: SNX9; NbExp=2; IntAct=EBI-2481535, EBI-77848;
CC Q8WV41; P42768: WAS; NbExp=3; IntAct=EBI-2481535, EBI-346375;
CC Q8WV41; P61981: YWHAG; NbExp=3; IntAct=EBI-2481535, EBI-359832;
CC Q8WV41; Q86XF7: ZNF575; NbExp=3; IntAct=EBI-2481535, EBI-14069183;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Membrane; Peripheral membrane
CC protein; Cytoplasmic side. Cytoplasmic vesicle membrane; Peripheral
CC membrane protein; Cytoplasmic side. Note=Primarily cytosolic, but a
CC minor proportion is membrane-bound (PubMed:18353773). Not associated
CC with membranes (PubMed:21048941). {ECO:0000269|PubMed:18353773,
CC ECO:0000269|PubMed:21048941}.
CC -!- TISSUE SPECIFICITY: Detected in heart and pancreas.
CC {ECO:0000269|PubMed:18353773}.
CC -!- DOMAIN: The PX and BAR domains mediate association with membranes and
CC are required for membrane tubulation. {ECO:0000269|PubMed:20964629}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:18353773}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; EF219141; ABN09670.1; -; mRNA.
DR EMBL; EF653821; ABV26009.1; -; mRNA.
DR EMBL; AL833039; CAH56299.1; -; mRNA.
DR EMBL; CH471136; EAW99243.1; -; Genomic_DNA.
DR EMBL; BC018775; AAH18775.1; -; mRNA.
DR CCDS; CCDS10283.1; -.
DR RefSeq; NP_001305075.1; NM_001318146.1.
DR RefSeq; NP_695003.1; NM_153271.1.
DR PDB; 4AKV; X-ray; 2.65 A; A/B=212-574.
DR PDBsum; 4AKV; -.
DR AlphaFoldDB; Q8WV41; -.
DR SMR; Q8WV41; -.
DR BioGRID; 129214; 59.
DR IntAct; Q8WV41; 46.
DR MINT; Q8WV41; -.
DR STRING; 9606.ENSP00000311427; -.
DR iPTMnet; Q8WV41; -.
DR PhosphoSitePlus; Q8WV41; -.
DR BioMuta; SNX33; -.
DR DMDM; 74751538; -.
DR EPD; Q8WV41; -.
DR jPOST; Q8WV41; -.
DR MassIVE; Q8WV41; -.
DR MaxQB; Q8WV41; -.
DR PaxDb; Q8WV41; -.
DR PeptideAtlas; Q8WV41; -.
DR PRIDE; Q8WV41; -.
DR ProteomicsDB; 74746; -.
DR Antibodypedia; 27355; 136 antibodies from 23 providers.
DR DNASU; 257364; -.
DR Ensembl; ENST00000308527.6; ENSP00000311427.6; ENSG00000173548.9.
DR GeneID; 257364; -.
DR KEGG; hsa:257364; -.
DR MANE-Select; ENST00000308527.6; ENSP00000311427.6; NM_153271.2; NP_695003.1.
DR UCSC; uc002bau.4; human.
DR CTD; 257364; -.
DR GeneCards; SNX33; -.
DR HGNC; HGNC:28468; SNX33.
DR HPA; ENSG00000173548; Low tissue specificity.
DR MIM; 619107; gene.
DR neXtProt; NX_Q8WV41; -.
DR OpenTargets; ENSG00000173548; -.
DR PharmGKB; PA162404345; -.
DR VEuPathDB; HostDB:ENSG00000173548; -.
DR eggNOG; KOG2528; Eukaryota.
DR GeneTree; ENSGT00940000160162; -.
DR HOGENOM; CLU_021494_3_0_1; -.
DR InParanoid; Q8WV41; -.
DR OMA; KHMMQSY; -.
DR OrthoDB; 811995at2759; -.
DR PhylomeDB; Q8WV41; -.
DR TreeFam; TF314082; -.
DR PathwayCommons; Q8WV41; -.
DR SignaLink; Q8WV41; -.
DR BioGRID-ORCS; 257364; 18 hits in 1076 CRISPR screens.
DR ChiTaRS; SNX33; human.
DR GenomeRNAi; 257364; -.
DR Pharos; Q8WV41; Tbio.
DR PRO; PR:Q8WV41; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q8WV41; protein.
DR Bgee; ENSG00000173548; Expressed in pancreatic ductal cell and 174 other tissues.
DR ExpressionAtlas; Q8WV41; baseline and differential.
DR Genevisible; Q8WV41; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0036089; P:cleavage furrow formation; IMP:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; IMP:UniProtKB.
DR GO; GO:0007032; P:endosome organization; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0044351; P:macropinocytosis; IMP:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
DR GO; GO:0045806; P:negative regulation of endocytosis; IDA:UniProtKB.
DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; IDA:UniProtKB.
DR GO; GO:0097320; P:plasma membrane tubulation; IDA:UniProtKB.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IDA:UniProtKB.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IDA:UniProtKB.
DR GO; GO:0017038; P:protein import; IDA:UniProtKB.
DR CDD; cd07669; BAR_SNX33; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR028642; SNX33.
DR InterPro; IPR037427; SNX33_BAR.
DR InterPro; IPR014536; Snx9_fam.
DR InterPro; IPR019497; Sorting_nexin_WASP-bd-dom.
DR PANTHER; PTHR45827:SF3; PTHR45827:SF3; 1.
DR Pfam; PF10456; BAR_3_WASP_bdg; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PIRSF; PIRSF027744; Snx9; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; Cytoplasmic vesicle;
KW Endocytosis; Membrane; Mitosis; Phosphoprotein; Protein transport;
KW Reference proteome; SH3 domain; Transport.
FT CHAIN 1..574
FT /note="Sorting nexin-33"
FT /id="PRO_0000311948"
FT DOMAIN 1..61
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 230..340
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 371..574
FT /note="BAR"
FT REGION 68..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:4AKV"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:4AKV"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:4AKV"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:4AKV"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:4AKV"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:4AKV"
FT HELIX 267..280
FT /evidence="ECO:0007829|PDB:4AKV"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:4AKV"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:4AKV"
FT HELIX 305..318
FT /evidence="ECO:0007829|PDB:4AKV"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:4AKV"
FT HELIX 327..333
FT /evidence="ECO:0007829|PDB:4AKV"
FT HELIX 339..349
FT /evidence="ECO:0007829|PDB:4AKV"
FT HELIX 355..360
FT /evidence="ECO:0007829|PDB:4AKV"
FT HELIX 371..407
FT /evidence="ECO:0007829|PDB:4AKV"
FT HELIX 409..427
FT /evidence="ECO:0007829|PDB:4AKV"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:4AKV"
FT HELIX 437..459
FT /evidence="ECO:0007829|PDB:4AKV"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:4AKV"
FT HELIX 465..504
FT /evidence="ECO:0007829|PDB:4AKV"
FT HELIX 510..568
FT /evidence="ECO:0007829|PDB:4AKV"
FT HELIX 569..571
FT /evidence="ECO:0007829|PDB:4AKV"
SQ SEQUENCE 574 AA; 65265 MW; 7CE51C0F35DDBC3C CRC64;
MALKGRALYD FHSENKEEIS IQQDEDLVIF SETSLDGWLQ GQNSRGETGL FPASYVEIVR
SGISTNHADY SSSPAGSPGA QVSLYNSPSV ASPARSGGGS GFLSNQGSFE EDDDDDWDDW
DDGCTVVEEP RAGGLGTNGH PPLNLSYPGA YPSQHMAFRP KPPLERQDSL ASAKRGSVVG
RNLNRFSCFV RSGVEAFILG DVPMMAKIAE TYSIEMGPRG PQWKANPHPF ACSVEDPTKQ
TKFKGIKSYI SYKLTPTHAA SPVYRRYKHF DWLYNRLLHK FTVISVPHLP EKQATGRFEE
DFIEKRKRRL ILWMDHMTSH PVLSQYEGFQ HFLSCLDDKQ WKMGKRRAEK DEMVGASFLL
TFQIPTEHQD LQDVEDRVDT FKAFSKKMDD SVLQLSTVAS ELVRKHVGGF RKEFQKLGSA
FQAISHSFQM DPPFCSEALN SAISHTGRTY EAIGEMFAEQ PKNDLFQMLD TLSLYQGLLS
NFPDIIHLQK GAFAKVKESQ RMSDEGRMVQ DEADGIRRRC RVVGFALQAE MNHFHQRREL
DFKHMMQNYL RQQILFYQRV GQQLEKTLRM YDNL
