HMMR_HUMAN
ID HMMR_HUMAN Reviewed; 724 AA.
AC O75330; A8K3G2; B4E114; D3DQK9; D3DQL0; E9PCS0; Q32N02; Q92767;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Hyaluronan mediated motility receptor;
DE AltName: Full=Intracellular hyaluronic acid-binding protein;
DE AltName: Full=Receptor for hyaluronan-mediated motility;
DE AltName: CD_antigen=CD168;
GN Name=HMMR; Synonyms=IHABP, RHAMM;
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 3), AND TISSUE SPECIFICITY.
RC TISSUE=Mammary gland;
RX PubMed=8890751; DOI=10.1016/0378-1119(96)00080-7;
RA Wang C., Entwistle J., Hou G., Li Q., Turley E.A.;
RT "The characterization of a human RHAMM cDNA: conservation of the
RT hyaluronan-binding domains.";
RL Gene 174:299-306(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 2),
RP AND CHARACTERIZATION.
RC TISSUE=Mammary carcinoma;
RX PubMed=9601098; DOI=10.1242/jcs.111.12.1685;
RA Assmann V., Marshall J.F., Fieber C., Hofmann M., Hart I.R.;
RT "The human hyaluronan receptor RHAMM is expressed as an intracellular
RT protein in breast cancer cells.";
RL J. Cell Sci. 111:1685-1694(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), AND VARIANTS
RP ALA-368 AND VAL-484.
RC TISSUE=Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS CYS-92;
RP ALA-368 AND VAL-484.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, 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 [8]
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 [9]
RP INTERACTION WITH DYNLL1 AND FAM83D, AND TISSUE SPECIFICITY.
RX PubMed=22965910; DOI=10.1083/jcb.201202112;
RA Dunsch A.K., Hammond D., Lloyd J., Schermelleh L., Gruneberg U., Barr F.A.;
RT "Dynein light chain 1 and a spindle-associated adaptor promote dynein
RT asymmetry and spindle orientation.";
RL J. Cell Biol. 198:1039-1054(2012).
RN [10]
RP INTERACTION WITH ANKRD26.
RX PubMed=22666460; DOI=10.1371/journal.pone.0038130;
RA Liu X.F., Bera T.K., Kahue C., Escobar T., Fei Z., Raciti G.A., Pastan I.;
RT "ANKRD26 and its interacting partners TRIO, GPS2, HMMR and DIPA regulate
RT adipogenesis in 3T3-L1 cells.";
RL PLoS ONE 7:E38130-E38130(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-703, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Receptor for hyaluronic acid (HA) (By similarity). Involved
CC in cell motility (By similarity). When hyaluronan binds to HMMR, the
CC phosphorylation of a number of proteins, including PTK2/FAK1 occurs.
CC May also be involved in cellular transformation and metastasis
CC formation, and in regulating extracellular-regulated kinase (ERK)
CC activity. May act as a regulator of adipogenisis (By similarity).
CC {ECO:0000250|UniProtKB:Q00547}.
CC -!- SUBUNIT: Interacts with ANKRD26 (PubMed:22666460). Interacts with
CC DYNLL1 (PubMed:22965910). Interacts with FAM83D/CHICA
CC (PubMed:22965910). {ECO:0000269|PubMed:22666460,
CC ECO:0000269|PubMed:22965910}.
CC -!- INTERACTION:
CC O75330; P38398: BRCA1; NbExp=4; IntAct=EBI-2556203, EBI-349905;
CC O75330; Q8NDC4: MORN4; NbExp=4; IntAct=EBI-2556203, EBI-10269566;
CC O75330; Q9ULW0: TPX2; NbExp=5; IntAct=EBI-2556203, EBI-1037322;
CC O75330-3; P54252: ATXN3; NbExp=3; IntAct=EBI-12098658, EBI-946046;
CC O75330-3; Q8NDC4: MORN4; NbExp=3; IntAct=EBI-12098658, EBI-10269566;
CC O75330-3; O76024: WFS1; NbExp=3; IntAct=EBI-12098658, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250|UniProtKB:Q00547}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q00547}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250|UniProtKB:Q00547}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=A;
CC IsoId=O75330-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=O75330-2; Sequence=VSP_004286;
CC Name=3;
CC IsoId=O75330-3; Sequence=VSP_038378;
CC Name=4;
CC IsoId=O75330-4; Sequence=VSP_041266;
CC -!- TISSUE SPECIFICITY: Expressed in testis (PubMed:22965910). Expressed in
CC the breast (PubMed:8890751). {ECO:0000269|PubMed:22965910,
CC ECO:0000269|PubMed:8890751}.
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DR EMBL; U29343; AAC52049.1; -; mRNA.
DR EMBL; AF032862; AAC32548.1; -; mRNA.
DR EMBL; AK290577; BAF83266.1; -; mRNA.
DR EMBL; AK303616; BAG64626.1; -; mRNA.
DR EMBL; AC112205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61522.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61523.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61524.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61525.1; -; Genomic_DNA.
DR EMBL; BC108904; AAI08905.1; -; mRNA.
DR CCDS; CCDS4362.1; -. [O75330-1]
DR CCDS; CCDS4363.1; -. [O75330-2]
DR CCDS; CCDS47334.1; -. [O75330-3]
DR CCDS; CCDS47335.1; -. [O75330-4]
DR PIR; JC5016; JC5016.
DR RefSeq; NP_001136028.1; NM_001142556.1. [O75330-3]
DR RefSeq; NP_001136029.1; NM_001142557.1. [O75330-4]
DR RefSeq; NP_036616.2; NM_012484.2. [O75330-1]
DR RefSeq; NP_036617.2; NM_012485.2. [O75330-2]
DR AlphaFoldDB; O75330; -.
DR SMR; O75330; -.
DR BioGRID; 109404; 91.
DR CORUM; O75330; -.
DR DIP; DIP-56496N; -.
DR IntAct; O75330; 62.
DR MINT; O75330; -.
DR STRING; 9606.ENSP00000377492; -.
DR BindingDB; O75330; -.
DR ChEMBL; CHEMBL4295676; -.
DR DrugBank; DB08818; Hyaluronic acid.
DR MoonDB; O75330; Curated.
DR GlyGen; O75330; 5 sites, 1 O-linked glycan (1 site).
DR iPTMnet; O75330; -.
DR PhosphoSitePlus; O75330; -.
DR BioMuta; HMMR; -.
DR REPRODUCTION-2DPAGE; O75330; -.
DR EPD; O75330; -.
DR jPOST; O75330; -.
DR MassIVE; O75330; -.
DR MaxQB; O75330; -.
DR PaxDb; O75330; -.
DR PeptideAtlas; O75330; -.
DR PRIDE; O75330; -.
DR ProteomicsDB; 49897; -. [O75330-1]
DR ProteomicsDB; 49898; -. [O75330-2]
DR ProteomicsDB; 49899; -. [O75330-3]
DR ProteomicsDB; 49900; -. [O75330-4]
DR Antibodypedia; 39622; 472 antibodies from 41 providers.
DR DNASU; 3161; -.
DR Ensembl; ENST00000353866.7; ENSP00000185942.6; ENSG00000072571.20. [O75330-2]
DR Ensembl; ENST00000358715.3; ENSP00000351554.3; ENSG00000072571.20. [O75330-1]
DR Ensembl; ENST00000393915.9; ENSP00000377492.4; ENSG00000072571.20. [O75330-3]
DR Ensembl; ENST00000432118.6; ENSP00000402673.2; ENSG00000072571.20. [O75330-4]
DR GeneID; 3161; -.
DR KEGG; hsa:3161; -.
DR MANE-Select; ENST00000393915.9; ENSP00000377492.4; NM_001142556.2; NP_001136028.1. [O75330-3]
DR UCSC; uc003lzf.5; human. [O75330-1]
DR CTD; 3161; -.
DR DisGeNET; 3161; -.
DR GeneCards; HMMR; -.
DR HGNC; HGNC:5012; HMMR.
DR HPA; ENSG00000072571; Tissue enhanced (bone marrow, lymphoid tissue, testis).
DR MalaCards; HMMR; -.
DR MIM; 600936; gene.
DR neXtProt; NX_O75330; -.
DR OpenTargets; ENSG00000072571; -.
DR PharmGKB; PA29340; -.
DR VEuPathDB; HostDB:ENSG00000072571; -.
DR eggNOG; ENOG502QQJM; Eukaryota.
DR GeneTree; ENSGT00390000007135; -.
DR HOGENOM; CLU_009698_0_0_1; -.
DR InParanoid; O75330; -.
DR OMA; MKSMMAK; -.
DR OrthoDB; 604725at2759; -.
DR PhylomeDB; O75330; -.
DR TreeFam; TF333963; -.
DR PathwayCommons; O75330; -.
DR Reactome; R-HSA-2160916; Hyaluronan uptake and degradation.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR SignaLink; O75330; -.
DR BioGRID-ORCS; 3161; 25 hits in 1085 CRISPR screens.
DR ChiTaRS; HMMR; human.
DR GeneWiki; Hyaluronan-mediated_motility_receptor; -.
DR GenomeRNAi; 3161; -.
DR Pharos; O75330; Tchem.
DR PRO; PR:O75330; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O75330; protein.
DR Bgee; ENSG00000072571; Expressed in sperm and 135 other tissues.
DR ExpressionAtlas; O75330; baseline and differential.
DR Genevisible; O75330; HS.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:UniProtKB-KW.
DR InterPro; IPR031794; HMMR_C.
DR InterPro; IPR026203; IHABP.
DR PANTHER; PTHR18956; PTHR18956; 2.
DR Pfam; PF15908; HMMR_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Glycoprotein;
KW Hyaluronic acid; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..724
FT /note="Hyaluronan mediated motility receptor"
FT /id="PRO_0000084007"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..546
FT /note="Required for interaction with FAM83D"
FT /evidence="ECO:0000269|PubMed:22965910"
FT REGION 635..645
FT /note="Hyaluronic acid-binding"
FT /evidence="ECO:0000255"
FT REGION 657..666
FT /note="Hyaluronic acid-binding"
FT /evidence="ECO:0000255"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 703
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 567
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..90
FT /note="MSFPKAPLKRFNDPSGCAPSPGAYDVKTLEVLKGPVSFQKSQRFKQQKESKQ
FT NLNVDKDTTLPASARKVKSSESKESQKNDKDLKILEKE -> MTLL (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041266"
FT VAR_SEQ 75
FT /note="K -> KK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8890751"
FT /id="VSP_038378"
FT VAR_SEQ 76..90
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_004286"
FT VARIANT 92
FT /note="R -> C (in dbSNP:rs299284)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_024155"
FT VARIANT 305
FT /note="N -> K (in dbSNP:rs2303077)"
FT /id="VAR_031661"
FT VARIANT 320
FT /note="N -> K (in dbSNP:rs2303077)"
FT /id="VAR_056917"
FT VARIANT 332
FT /note="R -> H (in dbSNP:rs2303078)"
FT /id="VAR_024156"
FT VARIANT 368
FT /note="V -> A (in dbSNP:rs299290)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_020044"
FT VARIANT 484
FT /note="A -> V (in dbSNP:rs299295)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_024157"
FT VARIANT 557
FT /note="D -> H (in dbSNP:rs2230362)"
FT /id="VAR_056918"
FT VARIANT 595
FT /note="L -> I (in dbSNP:rs2230363)"
FT /id="VAR_056919"
FT CONFLICT 103
FT /note="R -> S (in Ref. 2; AAC32548)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="E -> D (in Ref. 1; AAC52049)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="K -> T (in Ref. 1; AAC52049)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="K -> E (in Ref. 1; AAC52049)"
FT /evidence="ECO:0000305"
FT CONFLICT 330..332
FT /note="QER -> REH (in Ref. 1; AAC52049)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="Q -> R (in Ref. 3; BAF83266)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 724 AA; 84100 MW; F2C3C0DBA863955F CRC64;
MSFPKAPLKR FNDPSGCAPS PGAYDVKTLE VLKGPVSFQK SQRFKQQKES KQNLNVDKDT
TLPASARKVK SSESKESQKN DKDLKILEKE IRVLLQERGA QDRRIQDLET ELEKMEARLN
AALREKTSLS ANNATLEKQL IELTRTNELL KSKFSENGNQ KNLRILSLEL MKLRNKRETK
MRGMMAKQEG MEMKLQVTQR SLEESQGKIA QLEGKLVSIE KEKIDEKSET EKLLEYIEEI
SCASDQVEKY KLDIAQLEEN LKEKNDEILS LKQSLEENIV ILSKQVEDLN VKCQLLEKEK
EDHVNRNREH NENLNAEMQN LKQKFILEQQ EREKLQQKEL QIDSLLQQEK ELSSSLHQKL
CSFQEEMVKE KNLFEEELKQ TLDELDKLQQ KEEQAERLVK QLEEEAKSRA EELKLLEEKL
KGKEAELEKS SAAHTQATLL LQEKYDSMVQ SLEDVTAQFE SYKALTASEI EDLKLENSSL
QEKAAKAGKN AEDVQHQILA TESSNQEYVR MLLDLQTKSA LKETEIKEIT VSFLQKITDL
QNQLKQQEED FRKQLEDEEG RKAEKENTTA ELTEEINKWR LLYEELYNKT KPFQLQLDAF
EVEKQALLNE HGAAQEQLNK IRDSYAKLLG HQNLKQKIKH VVKLKDENSQ LKSEVSKLRC
QLAKKKQSET KLQEELNKVL GIKHFDPSKA FHHESKENFA LKTPLKEGNT NCYRAPMECQ
ESWK
