XIRP1_HUMAN
ID XIRP1_HUMAN Reviewed; 1843 AA.
AC Q702N8; A0JP25; A4QPE2; Q68DF2; Q6ZTR3; Q702N9; Q8IVN7; Q8N1N3; Q8N904;
AC Q8TCG7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Xin actin-binding repeat-containing protein 1;
DE AltName: Full=Cardiomyopathy-associated protein 1;
GN Name=XIRP1; Synonyms=CMYA1, XIN;
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 B), FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH F-ACTIN.
RC TISSUE=Skeletal muscle;
RX PubMed=15454575; DOI=10.1242/jcs.01406;
RA Pacholsky D., Vakeel P., Himmel M., Loewe T., Stradal T., Rottner K.,
RA Fuerst D.O., van der Ven P.F.M.;
RT "Xin repeats define a novel actin-binding motif.";
RL J. Cell Sci. 117:5257-5268(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), ALTERNATIVE SPLICING (ISOFORMS B
RP AND C), TISSUE SPECIFICITY, AND INTERACTION WITH FLNC AND VASP.
RC TISSUE=Skeletal muscle;
RX PubMed=16631741; DOI=10.1016/j.yexcr.2006.03.015;
RA van der Ven P.F.M., Ehler E., Vakeel P., Eulitz S., Schenk J.A.,
RA Milting H., Micheel B., Fuerst D.O.;
RT "Unusual splicing events result in distinct Xin isoforms that associate
RT differentially with filamin c and Mena/VASP.";
RL Exp. Cell Res. 312:2154-2167(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RA Luo J., Liu M., Wu X.;
RT "A novel human gene, hXin, specifically expressed in human heart and
RT skeletal muscle.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 444-1843 (ISOFORM A).
RC TISSUE=Heart, Tongue, and Trachea;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 570-1623 (ISOFORM A), AND VARIANT ARG-346.
RC TISSUE=Liver, and Skeletal muscle;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C), AND VARIANT ARG-1604.
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1554-1843.
RA Trevisan S., Lanfranchi G.;
RT "Study of a muscle specific transcript.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, 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 [9]
RP VARIANTS [LARGE SCALE ANALYSIS] HIS-929 AND LYS-1634.
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: Protects actin filaments from depolymerization.
CC {ECO:0000269|PubMed:15454575}.
CC -!- SUBUNIT: Interacts with CTNNB1 (By similarity). Interacts with F-actin,
CC FLNC and VASP. {ECO:0000250, ECO:0000269|PubMed:15454575,
CC ECO:0000269|PubMed:16631741}.
CC -!- INTERACTION:
CC Q702N8; Q14315: FLNC; NbExp=4; IntAct=EBI-7851194, EBI-489954;
CC Q702N8; P50552: VASP; NbExp=5; IntAct=EBI-7851194, EBI-748201;
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:15454575}.
CC Note=Colocalizes with actin stress fibers.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A;
CC IsoId=Q702N8-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q702N8-2; Sequence=VSP_030844, VSP_030845;
CC Name=C;
CC IsoId=Q702N8-3; Sequence=VSP_030843;
CC -!- TISSUE SPECIFICITY: Isoform A, isoform B and isoform C are expressed in
CC heart. {ECO:0000269|PubMed:16631741}.
CC -!- DOMAIN: Xin repeats bind F-actin.
CC -!- MISCELLANEOUS: 'Xin' means 'heart' in Chinese.
CC -!- SIMILARITY: Belongs to the Xin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00721}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC86519.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAC81057.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAD28459.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ626899; CAF25191.1; -; mRNA.
DR EMBL; AJ626900; CAF25192.1; -; mRNA.
DR EMBL; AY375160; AAQ64003.1; -; mRNA.
DR EMBL; AK095941; BAC04655.1; -; mRNA.
DR EMBL; AK096421; BAC04783.1; -; mRNA.
DR EMBL; AK126299; BAC86519.1; ALT_INIT; mRNA.
DR EMBL; AL713648; CAD28459.1; ALT_INIT; mRNA.
DR EMBL; CR749430; CAH18268.1; -; mRNA.
DR EMBL; BC127119; AAI27120.1; -; mRNA.
DR EMBL; BC139782; AAI39783.1; -; mRNA.
DR EMBL; AJ271461; CAC81057.1; ALT_FRAME; mRNA.
DR CCDS; CCDS2683.1; -. [Q702N8-1]
DR CCDS; CCDS56245.1; -. [Q702N8-2]
DR CCDS; CCDS87065.1; -. [Q702N8-3]
DR RefSeq; NP_001185550.1; NM_001198621.2. [Q702N8-2]
DR RefSeq; NP_919269.2; NM_194293.2. [Q702N8-1]
DR RefSeq; XP_005264966.1; XM_005264909.3. [Q702N8-1]
DR AlphaFoldDB; Q702N8; -.
DR SMR; Q702N8; -.
DR BioGRID; 127921; 18.
DR ELM; Q702N8; -.
DR IntAct; Q702N8; 6.
DR MINT; Q702N8; -.
DR STRING; 9606.ENSP00000343140; -.
DR GlyGen; Q702N8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q702N8; -.
DR PhosphoSitePlus; Q702N8; -.
DR BioMuta; XIRP1; -.
DR DMDM; 74712579; -.
DR EPD; Q702N8; -.
DR jPOST; Q702N8; -.
DR MassIVE; Q702N8; -.
DR PaxDb; Q702N8; -.
DR PeptideAtlas; Q702N8; -.
DR PRIDE; Q702N8; -.
DR ProteomicsDB; 68504; -. [Q702N8-1]
DR ProteomicsDB; 68505; -. [Q702N8-2]
DR ProteomicsDB; 68506; -. [Q702N8-3]
DR Antibodypedia; 12167; 80 antibodies from 21 providers.
DR DNASU; 165904; -.
DR Ensembl; ENST00000340369.4; ENSP00000343140.3; ENSG00000168334.9. [Q702N8-1]
DR Ensembl; ENST00000396251.1; ENSP00000379550.1; ENSG00000168334.9. [Q702N8-2]
DR Ensembl; ENST00000421646.1; ENSP00000391645.1; ENSG00000168334.9. [Q702N8-3]
DR GeneID; 165904; -.
DR KEGG; hsa:165904; -.
DR MANE-Select; ENST00000340369.4; ENSP00000343140.3; NM_194293.4; NP_919269.2.
DR UCSC; uc003cji.4; human. [Q702N8-1]
DR CTD; 165904; -.
DR DisGeNET; 165904; -.
DR GeneCards; XIRP1; -.
DR HGNC; HGNC:14301; XIRP1.
DR HPA; ENSG00000168334; Group enriched (heart muscle, skeletal muscle).
DR MIM; 609777; gene.
DR neXtProt; NX_Q702N8; -.
DR OpenTargets; ENSG00000168334; -.
DR PharmGKB; PA162409336; -.
DR VEuPathDB; HostDB:ENSG00000168334; -.
DR eggNOG; ENOG502QTAC; Eukaryota.
DR GeneTree; ENSGT00530000063779; -.
DR HOGENOM; CLU_280589_0_0_1; -.
DR InParanoid; Q702N8; -.
DR OMA; DGIYTAH; -.
DR OrthoDB; 34408at2759; -.
DR PhylomeDB; Q702N8; -.
DR TreeFam; TF330745; -.
DR PathwayCommons; Q702N8; -.
DR SignaLink; Q702N8; -.
DR BioGRID-ORCS; 165904; 5 hits in 1065 CRISPR screens.
DR ChiTaRS; XIRP1; human.
DR GenomeRNAi; 165904; -.
DR Pharos; Q702N8; Tbio.
DR PRO; PR:Q702N8; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q702N8; protein.
DR Bgee; ENSG00000168334; Expressed in left ventricle myocardium and 119 other tissues.
DR Genevisible; Q702N8; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IMP:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IMP:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; IMP:UniProtKB.
DR InterPro; IPR012510; Actin-binding_Xin_repeat.
DR InterPro; IPR030072; XIRP1/XIRP2.
DR PANTHER; PTHR22591; PTHR22591; 2.
DR Pfam; PF08043; Xin; 9.
DR PROSITE; PS51389; XIN; 17.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell junction; Coiled coil;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1843
FT /note="Xin actin-binding repeat-containing protein 1"
FT /id="PRO_0000316983"
FT REPEAT 89..104
FT /note="Xin 1"
FT REPEAT 121..136
FT /note="Xin 2"
FT REPEAT 151..166
FT /note="Xin 3"
FT REPEAT 186..201
FT /note="Xin 4"
FT REPEAT 226..241
FT /note="Xin 5"
FT REPEAT 264..279
FT /note="Xin 6"
FT REPEAT 302..317
FT /note="Xin 7"
FT REPEAT 340..355
FT /note="Xin 8"
FT REPEAT 376..391
FT /note="Xin 9"
FT REPEAT 436..451
FT /note="Xin 10"
FT REPEAT 507..522
FT /note="Xin 11"
FT REPEAT 545..560
FT /note="Xin 12"
FT REPEAT 589..604
FT /note="Xin 13"
FT REPEAT 621..636
FT /note="Xin 14"
FT REPEAT 654..669
FT /note="Xin 15"
FT REPEAT 691..706
FT /note="Xin 16"
FT REPEAT 723..738
FT /note="Xin 17"
FT REGION 1..54
FT /note="Interaction with VASP"
FT /evidence="ECO:0000269|PubMed:16631741"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..632
FT /note="Interaction with CTNNB1"
FT /evidence="ECO:0000250"
FT REGION 564..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1238..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1561..1696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1685..1843
FT /note="Interaction with FLNC"
FT /evidence="ECO:0000269|PubMed:16631741"
FT COILED 1462..1490
FT /evidence="ECO:0000255"
FT COMPBIAS 21..35
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1250..1264
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1296..1314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1346
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1393..1443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1585..1620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1634..1650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1662..1684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70373"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70373"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70373"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70373"
FT VAR_SEQ 1..1317
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_030843"
FT VAR_SEQ 1120..1121
FT /note="VS -> LL (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15454575,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_030844"
FT VAR_SEQ 1122..1843
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15454575,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_030845"
FT VARIANT 3
FT /note="D -> N (in dbSNP:rs2271488)"
FT /id="VAR_038439"
FT VARIANT 346
FT /note="Q -> R (in dbSNP:rs6805248)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_038440"
FT VARIANT 551
FT /note="R -> Q (in dbSNP:rs34121641)"
FT /id="VAR_038441"
FT VARIANT 695
FT /note="R -> C (in dbSNP:rs60540208)"
FT /id="VAR_061722"
FT VARIANT 776
FT /note="R -> W (in dbSNP:rs9823779)"
FT /id="VAR_061723"
FT VARIANT 929
FT /note="L -> H (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_038442"
FT VARIANT 965
FT /note="H -> P (in dbSNP:rs11711871)"
FT /id="VAR_038443"
FT VARIANT 1046
FT /note="P -> A (in dbSNP:rs35649793)"
FT /id="VAR_038444"
FT VARIANT 1061
FT /note="A -> V (in dbSNP:rs35795536)"
FT /id="VAR_061724"
FT VARIANT 1604
FT /note="G -> R (in dbSNP:rs3732383)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038445"
FT VARIANT 1608
FT /note="A -> V (in dbSNP:rs34810344)"
FT /id="VAR_038446"
FT VARIANT 1634
FT /note="R -> K (in a breast cancer sample; somatic mutation;
FT dbSNP:rs768911526)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_038447"
FT VARIANT 1707
FT /note="Q -> H (in dbSNP:rs34053674)"
FT /id="VAR_061725"
FT VARIANT 1724
FT /note="I -> V (in dbSNP:rs9827576)"
FT /id="VAR_038448"
FT CONFLICT 21
FT /note="D -> G (in Ref. 5; CAH18268)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="I -> T (in Ref. 5; CAH18268)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="E -> G (in Ref. 5; CAH18268)"
FT /evidence="ECO:0000305"
FT CONFLICT 754
FT /note="Q -> P (in Ref. 5; CAH18268)"
FT /evidence="ECO:0000305"
FT CONFLICT 813
FT /note="G -> R (in Ref. 5; CAH18268)"
FT /evidence="ECO:0000305"
FT CONFLICT 1556
FT /note="K -> R (in Ref. 4; BAC04783)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1843 AA; 198561 MW; 41A5CC13FE1955CB CRC64;
MADTQTQVAP TPTMRMATAE DLPLPPPPAL EDLPLPPPKE SFSKFHQQRQ ASELRRLYRH
IHPELRKNLA EAVAEDLAEV LGSEEPTEGD VQCMRWIFEN WRLDAIGEHE RPAAKEPVLC
GDVQATSRKF EEGSFANSTD QEPTRPQPGG GDVRAARWLF ETKPLDELTG QAKELEATVR
EPAASGDVQG TRMLFETRPL DRLGSRPSLQ EQSPLELRSE IQELKGDVKK TVKLFQTEPL
CAIQDAEGAI HEVKAACREE IQSNAVRSAR WLFETRPLDA INQDPSQVRV IRGISLEEGA
RPDVSATRWI FETQPLDAIR EILVDEKDFQ PSPDLIPPGP DVQQQQHLFE TRALDTLKGD
EEAGAEAPPK EEVVPGDVRS TLWLFETKPL DAFRDKVQVG HLQRVDPQDG EGHLSSDSSS
ALPFSQSAPQ RDELKGDVKT FKNLFETLPL DSIGQGEVLA HGSPSREEGT DSAGQAQGIG
SPVYAMQDSK GRLHALTSVS REQIVGGDVQ GYRWMFETQP LDQLGRSPST IDVVRGITRQ
EVVAGDVGTA RWLFETQPLE MIHQREQQER QKEEGKSQGD PQPEAPPKGD VQTIRWLFET
CPMSELAEKQ GSEVTDPTAK AEAQSCTWMF KPQPVDRPVG SREQHLQVSQ VPAGERQTDR
HVFETEPLQA SGRPCGRRPV RYCSRVEIPS GQVSRQKEVF QALEAGKKEE QEPRVIAGSI
PAGSVHKFTW LFENCPMGSL AAESIQGGNL LEEQPMSPSG NRMQESQETA AEGTLRTLHA
TPGILHHGGI LMEARGPGEL CLAKYVLSGT GQGHPYIRKE ELVSGELPRI ICQVLRRPDV
DQQGLLVQED PTGQLQLKPL RLPTPGSSGN IEDMDPELQQ LLACGLGTSV ARTGLVMQET
EQGLVALTAY SLQPRLTSKA SERSSVQLLA SCIDKGDLSG LHSLRWEPPA DPSPVPASEG
AQSLHPTESI IHVPPLDPSM GMGHLRASGA TPCPPQAIGK AVPLAGEAAA PAQLQNTEKQ
EDSHSGQKGM AVLGKSEGAT TTPPGPGAPD LLAAMQSLRM ATAEAQSLHQ QVLNKHKQGP
TPTATSNPIQ DGLRKAGATQ SNIRPGGGSD PRIPAAPRKV SREEQALPRG LPGGWVTIQD
GIYTAHPVRT FDPPGGVQLS QREPQSRHRE TALSVQAPRP LQGGPGQSTG PGREEPGGCT
QMAWGPPGKA MAEVCPGGLQ AAETTLKTAP LGRHILASGP QAAGASPHPH NAFVPPPPTL
PAAVTGPDFP AGAHRAEDSI QQASEPLKDP LLHSHSSPAG QRTPGGSQTK TPKLDPTMPP
KKKPQLPPKP AHLTQSHPPQ RLPKPLPLSP SFSSEVGQRE HQRGERDTAI PQPAKVPTTV
DQGHIPLARC PSGHSQPSLQ HGLSTTAPRP TKNQATGSNA QSSEPPKLNA LNHDPTSPQW
GPGPSGEQPM EGSHQGAPES PDSLQRNQKE LQGLLNQVQA LEKEAASSVD VQALRRLFEA
VPQLGGAAPQ APAAHQKPEA SVEQAFGELT RVSTEVAQLK EQTLARLLDI EEAVHKALSS
MSSLQPEASA RGHFQGPPKD HSAHKISVTV SSSARPSGSG QEVGGQTAVK NQAKVECHTE
AQSQVKIRNH TEARGHTAST APSTRRQETS REYLCPPRVL PSSRDSPSSP TFISIQSATR
KPLETPSFKG NPDVSVKSTQ LAQDIGQALL HQKGVQDKTG KKDITQCSVQ PEPAPPSASP
LPRGWQKSVL ELQTGPGSSQ HYGAMRTVTE QYEEVDQFGN TVLMSSTTVT EQAEPPRNPG
SHLGLHASPL LRQFLHSPAG FSSDLTEAET VQVSCSYSQP AAQ
