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 29-MAY-2024, entry version 143. 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; 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 Q60I27; Q7Z5V6-2: SAXO4; NbExp=3; IntAct=EBI-12078276, EBI-12000762; 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}; 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; 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. DR AlphaFoldDB; Q60I27; -. DR SMR; Q60I27; -. DR BioGRID; 129223; 15. 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; 9606-ENSP00000313670; -. DR PeptideAtlas; Q60I27; -. DR ProteomicsDB; 65869; -. [Q60I27-1] DR ProteomicsDB; 65870; -. [Q60I27-2] DR ProteomicsDB; 65871; -. [Q60I27-3] DR ProteomicsDB; 65872; -. [Q60I27-4] DR ProteomicsDB; 65873; -. [Q60I27-5] DR ProteomicsDB; 65874; -. [Q60I27-6] DR Pumba; Q60I27; -. DR Antibodypedia; 29738; 93 antibodies from 15 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 AGR; HGNC:20605; -. 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; YEGEWCQ; -. DR OrthoDB; 3740287at2759; -. 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; 22 hits in 1141 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 192 other cell types or tissues. DR ExpressionAtlas; Q60I27; baseline and differential. 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:0005096; F:GTPase activator activity; IEA:UniProtKB-KW. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central. DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central. DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central. DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1. DR Gene3D; 2.20.110.10; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 3. DR Gene3D; 1.20.1050.80; VPS9 domain; 1. DR InterPro; IPR035899; DBL_dom_sf. DR InterPro; IPR003409; MORN. DR InterPro; IPR003123; VPS9. DR InterPro; IPR037191; VPS9_dom_sf. DR PANTHER; PTHR46089:SF1; ALS2 C-TERMINAL-LIKE PROTEIN; 1. DR PANTHER; PTHR46089; ALSIN HOMOLOG; 1. DR Pfam; PF02493; MORN; 7. DR Pfam; PF02204; VPS9; 1. DR SMART; SM00698; MORN; 7. DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1. DR SUPFAM; SSF82185; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 2. DR SUPFAM; SSF109993; VPS9 domain; 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 //