E41L5_HUMAN
ID E41L5_HUMAN Reviewed; 733 AA.
AC Q9HCM4; Q7Z5S1; Q8IZ12; Q9H975;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Band 4.1-like protein 5;
DE AltName: Full=Erythrocyte membrane protein band 4.1-like 5 {ECO:0000312|HGNC:HGNC:19819};
GN Name=EPB41L5; Synonyms=KIAA1548;
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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), AND VARIANT
RP THR-462.
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Retinoblastoma, and Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 188-732 (ISOFORM 3), AND VARIANT
RP THR-462.
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [5]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH CRB1 AND PALS1, AND INTERACTION
RP WITH PALS1; CRB1; CRB2 AND CRB3.
RX PubMed=17920587; DOI=10.1016/j.yexcr.2007.08.025;
RA Gosens I., Sessa A., den Hollander A.I., Letteboer S.J.F., Belloni V.,
RA Arends M.L., Le Bivic A., Cremers F.P.M., Broccoli V., Roepman R.;
RT "FERM protein EPB41L5 is a novel member of the mammalian CRB-MPP5 polarity
RT complex.";
RL Exp. Cell Res. 313:3959-3970(2007).
RN [6]
RP IDENTIFICATION BY 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Plays a role in the formation and organization of tight
CC junctions during the establishment of polarity in epithelial cells.
CC {ECO:0000269|PubMed:17920587}.
CC -!- SUBUNIT: Component of a complex composed of PALS1, CRB1 and EPB41L5
CC (PubMed:17920587). Within the complex, interacts (via FERM domain) with
CC PALS1 (via HOOK domain) and with CRB1 (via intracellular domain)
CC (PubMed:17920587). Interacts with CRB2 (via intracellular domain)
CC (PubMed:17920587). Interacts with CRB3 (via intracellular domain)
CC (PubMed:17920587). {ECO:0000269|PubMed:17920587}.
CC -!- INTERACTION:
CC Q9HCM4; P82279: CRB1; NbExp=4; IntAct=EBI-1047162, EBI-1048648;
CC Q9HCM4; Q9BUF7: CRB3; NbExp=3; IntAct=EBI-1047162, EBI-9844372;
CC Q9HCM4; Q8N3R9: PALS1; NbExp=4; IntAct=EBI-1047162, EBI-2513978;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8BGS1}. Cell
CC junction, adherens junction {ECO:0000250|UniProtKB:Q8BGS1}. Cell
CC membrane {ECO:0000250|UniProtKB:Q8BGS1}; Peripheral membrane protein
CC {ECO:0000305}. Photoreceptor inner segment
CC {ECO:0000250|UniProtKB:Q5FVG2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9HCM4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HCM4-2; Sequence=VSP_033034, VSP_033035;
CC Name=3;
CC IsoId=Q9HCM4-3; Sequence=VSP_033036;
CC Name=4;
CC IsoId=Q9HCM4-4; Sequence=VSP_033037, VSP_033038;
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DR EMBL; AK023019; BAB14360.1; -; mRNA.
DR EMBL; AK290895; BAF83584.1; -; mRNA.
DR EMBL; CH471103; EAW95234.1; -; Genomic_DNA.
DR EMBL; BC032822; AAH32822.1; -; mRNA.
DR EMBL; BC054508; AAH54508.1; -; mRNA.
DR EMBL; AB046768; BAB13374.1; -; mRNA.
DR CCDS; CCDS2130.1; -. [Q9HCM4-1]
DR CCDS; CCDS54392.1; -. [Q9HCM4-2]
DR CCDS; CCDS54393.1; -. [Q9HCM4-4]
DR CCDS; CCDS82506.1; -. [Q9HCM4-3]
DR RefSeq; NP_001171866.1; NM_001184937.1. [Q9HCM4-4]
DR RefSeq; NP_001171867.1; NM_001184938.3. [Q9HCM4-2]
DR RefSeq; NP_001171868.1; NM_001184939.2. [Q9HCM4-2]
DR RefSeq; NP_001317239.1; NM_001330310.1. [Q9HCM4-3]
DR RefSeq; NP_065960.2; NM_020909.3. [Q9HCM4-1]
DR AlphaFoldDB; Q9HCM4; -.
DR SMR; Q9HCM4; -.
DR BioGRID; 121701; 344.
DR IntAct; Q9HCM4; 72.
DR MINT; Q9HCM4; -.
DR STRING; 9606.ENSP00000263713; -.
DR iPTMnet; Q9HCM4; -.
DR PhosphoSitePlus; Q9HCM4; -.
DR BioMuta; EPB41L5; -.
DR DMDM; 187608883; -.
DR EPD; Q9HCM4; -.
DR jPOST; Q9HCM4; -.
DR MassIVE; Q9HCM4; -.
DR MaxQB; Q9HCM4; -.
DR PaxDb; Q9HCM4; -.
DR PeptideAtlas; Q9HCM4; -.
DR PRIDE; Q9HCM4; -.
DR ProteomicsDB; 81763; -. [Q9HCM4-1]
DR ProteomicsDB; 81764; -. [Q9HCM4-2]
DR ProteomicsDB; 81765; -. [Q9HCM4-3]
DR ProteomicsDB; 81766; -. [Q9HCM4-4]
DR Antibodypedia; 33383; 136 antibodies from 27 providers.
DR DNASU; 57669; -.
DR Ensembl; ENST00000263713.10; ENSP00000263713.5; ENSG00000115109.14. [Q9HCM4-1]
DR Ensembl; ENST00000331393.8; ENSP00000329687.4; ENSG00000115109.14. [Q9HCM4-2]
DR Ensembl; ENST00000443124.5; ENSP00000393722.1; ENSG00000115109.14. [Q9HCM4-2]
DR Ensembl; ENST00000443902.6; ENSP00000393856.2; ENSG00000115109.14. [Q9HCM4-4]
DR Ensembl; ENST00000452780.1; ENSP00000390439.1; ENSG00000115109.14. [Q9HCM4-3]
DR GeneID; 57669; -.
DR KEGG; hsa:57669; -.
DR MANE-Select; ENST00000263713.10; ENSP00000263713.5; NM_020909.4; NP_065960.2.
DR UCSC; uc002tmg.4; human. [Q9HCM4-1]
DR CTD; 57669; -.
DR DisGeNET; 57669; -.
DR GeneCards; EPB41L5; -.
DR HGNC; HGNC:19819; EPB41L5.
DR HPA; ENSG00000115109; Low tissue specificity.
DR MIM; 611730; gene.
DR neXtProt; NX_Q9HCM4; -.
DR OpenTargets; ENSG00000115109; -.
DR PharmGKB; PA134862834; -.
DR VEuPathDB; HostDB:ENSG00000115109; -.
DR eggNOG; KOG3530; Eukaryota.
DR GeneTree; ENSGT00940000156332; -.
DR HOGENOM; CLU_003623_5_1_1; -.
DR InParanoid; Q9HCM4; -.
DR OMA; ATSDCCQ; -.
DR OrthoDB; 241659at2759; -.
DR PhylomeDB; Q9HCM4; -.
DR TreeFam; TF319780; -.
DR PathwayCommons; Q9HCM4; -.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR SignaLink; Q9HCM4; -.
DR BioGRID-ORCS; 57669; 17 hits in 1082 CRISPR screens.
DR ChiTaRS; EPB41L5; human.
DR GeneWiki; EPB41L5; -.
DR GenomeRNAi; 57669; -.
DR Pharos; Q9HCM4; Tbio.
DR PRO; PR:Q9HCM4; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9HCM4; protein.
DR Bgee; ENSG00000115109; Expressed in oocyte and 165 other tissues.
DR Genevisible; Q9HCM4; HS.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR GO; GO:0003383; P:apical constriction; IEA:Ensembl.
DR GO; GO:0048319; P:axial mesoderm morphogenesis; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0007398; P:ectoderm development; IEA:Ensembl.
DR GO; GO:0048617; P:embryonic foregut morphogenesis; IEA:Ensembl.
DR GO; GO:0007492; P:endoderm development; IEA:Ensembl.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0070986; P:left/right axis specification; IEA:Ensembl.
DR GO; GO:0007509; P:mesoderm migration involved in gastrulation; IEA:Ensembl.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl.
DR GO; GO:0001839; P:neural plate morphogenesis; IEA:Ensembl.
DR GO; GO:0048339; P:paraxial mesoderm development; IEA:Ensembl.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IEA:Ensembl.
DR GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IEA:Ensembl.
DR GO; GO:0070201; P:regulation of establishment of protein localization; IEA:Ensembl.
DR GO; GO:0032525; P:somite rostral/caudal axis specification; IEA:Ensembl.
DR GO; GO:0006931; P:substrate-dependent cell migration, cell attachment to substrate; IEA:Ensembl.
DR GO; GO:0009826; P:unidimensional cell growth; IEA:Ensembl.
DR CDD; cd14473; FERM_B-lobe; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR030694; Band4.1-like5.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR014847; FERM-adjacent.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23280:SF15; PTHR23280:SF15; 2.
DR Pfam; PF08736; FA; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SMART; SM01195; FA; 1.
DR SMART; SM01196; FERM_C; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Cytoplasm; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..733
FT /note="Band 4.1-like protein 5"
FT /id="PRO_0000219406"
FT DOMAIN 43..327
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 29..119
FT /note="Required for interaction with CRB1"
FT /evidence="ECO:0000269|PubMed:17920587"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 446..505
FT /note="CIPLNIDLLNSPDLLEATIGDVIGASDTMETSQALNDVNVATRLPGLGEPEV
FT EYETLKDT -> WLSAASDCCQRGGNQWNTRALPPPQTAHRNYTDFVHEHNVKNAGIRH
FT DVHFPGHTAMTEI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_033034"
FT VAR_SEQ 506..733
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_033035"
FT VAR_SEQ 668..669
FT /note="PQ -> P (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10997877"
FT /id="VSP_033036"
FT VAR_SEQ 669..687
FT /note="QSGAMSNGLAGCEMLLTGK -> LWSHFGRRSCPEAEVFTDH (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033037"
FT VAR_SEQ 688..733
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033038"
FT VARIANT 334
FT /note="H -> Y (in dbSNP:rs28930677)"
FT /id="VAR_048357"
FT VARIANT 462
FT /note="A -> T (in dbSNP:rs1034489)"
FT /evidence="ECO:0000269|PubMed:10997877,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_042699"
SQ SEQUENCE 733 AA; 81856 MW; A3712B5927C9C199 CRC64;
MLSFFRRTLG RRSMRKHAEK ERLREAQRAA THIPAAGDSK SIITCRVSLL DGTDVSVDLP
KKAKGQELFD QIMYHLDLIE SDYFGLRFMD SAQVAHWLDG TKSIKKQVKI GSPYCLHLRV
KFYSSEPNNL REELTRYLFV LQLKQDILSG KLDCPFDTAV QLAAYNLQAE LGDYDLAEHS
PELVSEFRFV PIQTEEMELA IFEKWKEYRG QTPAQAETNY LNKAKWLEMY GVDMHVVKAR
DGNDYSLGLT PTGVLVFEGD TKIGLFFWPK ITRLDFKKNK LTLVVVEDDD QGKEQEHTFV
FRLDHPKACK HLWKCAVEHH AFFRLRGPVQ KSSHRSGFIR LGSRFRYSGK TEYQTTKTNK
ARRSTSFERR PSKRYSRRTL QMKACATKPE ELSVHNNVST QSNGSQQAWG MRSALPVSPS
ISSAPVPVEI ENLPQSPGTD QHDRKCIPLN IDLLNSPDLL EATIGDVIGA SDTMETSQAL
NDVNVATRLP GLGEPEVEYE TLKDTSEKLK QLEMENSPLL SPRSNIDVNI NSQEEVVKLT
EKCLNNVIES PGLNVMRVPP DFKSNILKAQ VEAVHKVTKE DSLLSHKNAN VQDAATNSAV
LNENNVPLPK ESLETLMLIT PADSGSVLKE ATDELDALLA SLTENLIDHT VAPQVSSTSM
ITPRWIVPQS GAMSNGLAGC EMLLTGKEGH GNKDGISLIS PPAPFLVDAV TSSGPILAEE
AVLKQKCLLT TEL
