AL2CL_HUMAN
ID AL2CL_HUMAN Reviewed; 953 AA.
AC Q60I27; Q32MA1; Q6AI56; Q6ZNC5; Q6ZNC7; Q6ZTL4; Q86YD2; Q8N9U1; Q8NAL7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=ALS2 C-terminal-like protein;
GN Name=ALS2CL;
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 1), FUNCTION, INTERACTION WITH RAB5A,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=15388334; DOI=10.1016/j.febslet.2004.07.092;
RA Hadano S., Otomo A., Suzuki-Utsunomiya K., Kunita R., Yanagisawa Y.,
RA Showguchi-Miyata J., Mizumura H., Ikeda J.-E.;
RT "ALS2CL, the novel protein highly homologous to the carboxy-terminal half
RT of ALS2, binds to Rab5 and modulates endosome dynamics.";
RL FEBS Lett. 575:64-70(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 6).
RC TISSUE=Placenta, Tongue, Trachea, and Uterus;
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 GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 293-953 (ISOFORM 1).
RC TISSUE=Prostate;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-392 (ISOFORM 1), AND VARIANT
RP GLN-45.
RC TISSUE=Cervix;
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 [7]
RP FUNCTION.
RX PubMed=16473597; DOI=10.1016/s0076-6879(05)03026-0;
RA Hadano S., Ikeda J.-E.;
RT "Purification and functional analyses of ALS2 and its homologue.";
RL Methods Enzymol. 403:310-321(2005).
RN [8]
RP FUNCTION, HOMODIMERIZATION, INTERACTION WITH ALS2, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17239822; DOI=10.1016/j.bbrc.2006.12.229;
RA Suzuki-Utsunomiya K., Hadano S., Otomo A., Kunita R., Mizumura H.,
RA Osuga H., Ikeda J.-E.;
RT "ALS2CL, a novel ALS2-interactor, modulates ALS2-mediated endosome
RT dynamics.";
RL Biochem. Biophys. Res. Commun. 354:491-497(2007).
RN [9]
RP VARIANTS [LARGE SCALE ANALYSIS] GLU-280 AND PHE-576.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Acts as a guanine nucleotide exchange factor (GEF) for Rab5
CC GTPase. Regulates the ALS2-mediated endosome dynamics.
CC {ECO:0000269|PubMed:15388334, ECO:0000269|PubMed:16473597,
CC ECO:0000269|PubMed:17239822}.
CC -!- SUBUNIT: Homodimer. Forms a heteromeric complex with ALS2 (By
CC similarity). Interacts with ALS2 and RAB5A. {ECO:0000250,
CC ECO:0000269|PubMed:15388334, ECO:0000269|PubMed:17239822}.
CC -!- INTERACTION:
CC Q60I27; Q96AZ1: EEF1AKMT3; NbExp=3; IntAct=EBI-12078276, EBI-12108304;
CC Q60I27; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-12078276, EBI-12000762;
CC Q60I27; Q9UL26: RAB22A; NbExp=3; IntAct=EBI-12078276, EBI-399456;
CC Q60I27; Q13636: RAB31; NbExp=3; IntAct=EBI-12078276, EBI-725987;
CC Q60I27; P51148: RAB5C; NbExp=3; IntAct=EBI-12078276, EBI-1054923;
CC Q60I27; Q9UHP6: RSPH14; NbExp=3; IntAct=EBI-12078276, EBI-748350;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15388334,
CC ECO:0000269|PubMed:17239822}. Note=Distributed onto the vesicular
CC compartments in the cytoplasm with strong punctated staining.
CC Colocalizes with RAB5A onto the vesicular/membranous compartments in
CC the cytoplasm, particularly to the leading edges of the cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q60I27-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q60I27-2; Sequence=VSP_030170;
CC Name=3;
CC IsoId=Q60I27-3; Sequence=VSP_030169;
CC Name=4;
CC IsoId=Q60I27-4; Sequence=VSP_030168, VSP_030171;
CC Name=5;
CC IsoId=Q60I27-5; Sequence=VSP_030168;
CC Name=6;
CC IsoId=Q60I27-6; Sequence=VSP_043859;
CC -!- TISSUE SPECIFICITY: Expressed in heart and kidney.
CC {ECO:0000269|PubMed:15388334}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD18450.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB107015; BAD51817.1; -; mRNA.
DR EMBL; AK092455; BAC03895.1; -; mRNA.
DR EMBL; AK093844; BAC04237.1; -; mRNA.
DR EMBL; AK131273; BAD18450.1; ALT_FRAME; mRNA.
DR EMBL; AK131270; BAD18448.1; -; mRNA.
DR EMBL; AK126505; BAC86572.1; -; mRNA.
DR EMBL; AC104304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC134504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW64777.1; -; Genomic_DNA.
DR EMBL; BC042906; AAH42906.1; -; mRNA.
DR EMBL; BC061883; AAH61883.1; -; mRNA.
DR EMBL; BC075825; AAH75825.1; -; mRNA.
DR EMBL; BC109233; AAI09234.1; -; mRNA.
DR EMBL; CR627258; CAH10367.1; -; mRNA.
DR CCDS; CCDS2743.1; -. [Q60I27-1]
DR RefSeq; NP_001177636.1; NM_001190707.1. [Q60I27-1]
DR RefSeq; NP_667340.2; NM_147129.4. [Q60I27-1]
DR RefSeq; XP_005265082.1; XM_005265025.1. [Q60I27-3]
DR AlphaFoldDB; Q60I27; -.
DR SMR; Q60I27; -.
DR BioGRID; 129223; 14.
DR IntAct; Q60I27; 7.
DR STRING; 9606.ENSP00000313670; -.
DR iPTMnet; Q60I27; -.
DR PhosphoSitePlus; Q60I27; -.
DR BioMuta; ALS2CL; -.
DR DMDM; 74708351; -.
DR EPD; Q60I27; -.
DR jPOST; Q60I27; -.
DR MassIVE; Q60I27; -.
DR MaxQB; Q60I27; -.
DR PaxDb; Q60I27; -.
DR PeptideAtlas; Q60I27; -.
DR PRIDE; Q60I27; -.
DR ProteomicsDB; 65869; -. [Q60I27-1]
DR ProteomicsDB; 65870; -. [Q60I27-2]
DR ProteomicsDB; 65871; -. [Q60I27-3]
DR ProteomicsDB; 65874; -. [Q60I27-6]
DR Antibodypedia; 29738; 85 antibodies from 14 providers.
DR DNASU; 259173; -.
DR Ensembl; ENST00000318962.9; ENSP00000313670.4; ENSG00000178038.17. [Q60I27-1]
DR Ensembl; ENST00000415953.5; ENSP00000413223.1; ENSG00000178038.17. [Q60I27-1]
DR GeneID; 259173; -.
DR KEGG; hsa:259173; -.
DR MANE-Select; ENST00000318962.9; ENSP00000313670.4; NM_147129.5; NP_667340.2.
DR UCSC; uc003cpx.3; human. [Q60I27-1]
DR CTD; 259173; -.
DR DisGeNET; 259173; -.
DR GeneCards; ALS2CL; -.
DR HGNC; HGNC:20605; ALS2CL.
DR HPA; ENSG00000178038; Tissue enhanced (esophagus, kidney, skin).
DR MIM; 612402; gene.
DR neXtProt; NX_Q60I27; -.
DR OpenTargets; ENSG00000178038; -.
DR PharmGKB; PA134949717; -.
DR VEuPathDB; HostDB:ENSG00000178038; -.
DR eggNOG; KOG0231; Eukaryota.
DR GeneTree; ENSGT00940000161305; -.
DR HOGENOM; CLU_013321_0_0_1; -.
DR InParanoid; Q60I27; -.
DR OMA; CYKCHWQ; -.
DR PhylomeDB; Q60I27; -.
DR TreeFam; TF331793; -.
DR PathwayCommons; Q60I27; -.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q60I27; -.
DR BioGRID-ORCS; 259173; 17 hits in 1065 CRISPR screens.
DR ChiTaRS; ALS2CL; human.
DR GenomeRNAi; 259173; -.
DR Pharos; Q60I27; Tbio.
DR PRO; PR:Q60I27; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q60I27; protein.
DR Bgee; ENSG00000178038; Expressed in lower esophagus mucosa and 191 other tissues.
DR ExpressionAtlas; Q60I27; baseline and differential.
DR Genevisible; Q60I27; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:0007032; P:endosome organization; IGI:MGI.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR Gene3D; 1.20.1050.80; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR003409; MORN.
DR InterPro; IPR003123; VPS9.
DR InterPro; IPR037191; VPS9_dom_sf.
DR Pfam; PF02493; MORN; 7.
DR Pfam; PF02204; VPS9; 1.
DR SMART; SM00698; MORN; 7.
DR SUPFAM; SSF109993; SSF109993; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR PROSITE; PS51205; VPS9; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; GTPase activation; Reference proteome;
KW Repeat.
FT CHAIN 1..953
FT /note="ALS2 C-terminal-like protein"
FT /id="PRO_0000313849"
FT REPEAT 358..380
FT /note="MORN 1"
FT REPEAT 381..403
FT /note="MORN 2"
FT REPEAT 409..431
FT /note="MORN 3"
FT REPEAT 432..452
FT /note="MORN 4"
FT REPEAT 459..479
FT /note="MORN 5"
FT REPEAT 483..505
FT /note="MORN 6"
FT REPEAT 506..528
FT /note="MORN 7"
FT REPEAT 529..552
FT /note="MORN 8"
FT DOMAIN 796..942
FT /note="VPS9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00550"
FT VAR_SEQ 1..763
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_030168"
FT VAR_SEQ 1..653
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043859"
FT VAR_SEQ 1..485
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030169"
FT VAR_SEQ 1..199
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030170"
FT VAR_SEQ 896..953
FT /note="IQHLGAEIHLIRDMMDPNHTGGLYDFLLTALESCYEHIQKEDMRLHRLPGHW
FT HSRELW -> WGSQGPEKGGSQPGCWGARGRVRTTPQVSSHPGQRSFPSCLSATGLFSL
FT SPSLSWWGGVLQNSAPGSRDPPDP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030171"
FT VARIANT 29
FT /note="Q -> R (in dbSNP:rs59661801)"
FT /id="VAR_061554"
FT VARIANT 45
FT /note="E -> Q (in dbSNP:rs7642448)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_037791"
FT VARIANT 280
FT /note="Q -> E (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_037792"
FT VARIANT 576
FT /note="L -> F (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_037793"
FT CONFLICT 172
FT /note="L -> P (in Ref. 2; BAD18448)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="E -> G (in Ref. 2; BAD18448)"
FT /evidence="ECO:0000305"
FT CONFLICT 711
FT /note="E -> G (in Ref. 2; BAD18450)"
FT /evidence="ECO:0000305"
FT CONFLICT 893
FT /note="R -> H (in Ref. 2; BAD18448)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 953 AA; 107748 MW; 1BBC38A16E6A1168 CRC64;
MCNPEEAALL RLEEVFSATL AHVNSLVLQP LLPAAPDPSD PWGRECLRLL QQLHKSSQQL
WEVTEESLHS LQERLRYPDS TGLESLLLLR GADRVLQAHI EYIESYTSCM VVQAFQKAAK
RRSEYWRGQR KALRQLLSGV SSEGSVGASL GQALHQPLAH HVQQYVLLLL SLGDTIGEHH
PTRELVVNAV TLFGNLQSFM KQELDQAVAT QALWHTLRGR LRDVLCTPAH RLLQDSQDVP
VTVAPLRAER VLLFDDALVL LQGHNVHTFD LKLVWVDPGQ DGCTFHLLTP EEEFSFCAKD
SQGQAVWQWK VTWAVHQALH GKKDFPVLGA GLEPSQPPDC RCAEYTFQAE GRLCQATYEG
EWCRGRPHGK GTLKWPDGRN HVGNFCQGLE HGFGIRLLPQ ASEDKFDCYK CHWREGSMCG
YGICEYSTDE VYKGYFQEGL RHGFGVLESG PQAPQPFRYT GHWERGQRSG YGIEEDGDRG
ERYIGMWQAG QRHGPGVMVT QAGVCYQGTF QADKTVGPGI LLSEDDSLYE GTFTRDLTLM
GKGKVTFPNG FTLEGSFGSG AGRGLHTQGV LDTAALPPDP SSTCKRQLGV GAFPVESRWQ
GVYSPFRDFV CAGCPRDLQE ALLGFDVQSS RELRRSQDYL SCERTHPEDS VGSMEDILEE
LLQHREPKAL QLYLRKALSN SLHPLGKLLR TLMLTFQATY AGVGANKHLQ ELAQEEVKQH
AQELWAAYRG LLRVALERKG QALEEDEDTE TRDLQVHGLV LPLMLPSFYS ELFTLYLLLH
EREDSFYSQG IANLSLFPDT QLLEFLDVQK HLWPLKDLTL TSNQRYSLVR DKCFLSATEC
LQKIMTTVDP REKLEVLERT YGEIEGTVSR VLGREYKLPM DDLLPLLIYV VSRARIQHLG
AEIHLIRDMM DPNHTGGLYD FLLTALESCY EHIQKEDMRL HRLPGHWHSR ELW
