MRP7_MOUSE
ID MRP7_MOUSE Reviewed; 1501 AA.
AC Q8R4P9; Q3TCQ0; Q3V0D1; Q8R4S1;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=ATP-binding cassette sub-family C member 10;
DE EC=7.6.2.2 {ECO:0000250|UniProtKB:Q5T3U5};
DE EC=7.6.2.3 {ECO:0000250|UniProtKB:Q5T3U5};
DE AltName: Full=Multidrug resistance-associated protein 7;
GN Name=Abcc10; Synonyms=Mrp7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Spleen;
RX PubMed=11943485; DOI=10.1016/s0378-1119(02)00461-4;
RA Kao H.-H., Huang J.-D., Chang M.-S.;
RT "cDNA cloning and genomic organization of the murine MRP7, a new ATP-
RT binding cassette transporter.";
RL Gene 286:299-306(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-1422 (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=21576088; DOI=10.1158/0008-5472.can-10-3623;
RA Hopper-Borge E.A., Churchill T., Paulose C., Nicolas E., Jacobs J.D.,
RA Ngo O., Kuang Y., Grinberg A., Westphal H., Chen Z.S., Klein-Szanto A.J.,
RA Belinsky M.G., Kruh G.D.;
RT "Contribution of Abcc10 (Mrp7) to in vivo paclitaxel resistance as assessed
RT in Abcc10(-/-) mice.";
RL Cancer Res. 71:3649-3657(2011).
CC -!- FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC)
CC family that actively extrudes physiological compounds, and xenobiotics
CC from cells. Lipophilic anion transporter that mediates ATP-dependent
CC transport of glucuronide conjugates such as estradiol-17-beta-o-
CC glucuronide and GSH conjugates such as leukotriene C4 (LTC4). Does not
CC transport glycocholic acid, taurocholic acid, MTX, folic acid, cAMP, or
CC cGMP. {ECO:0000250|UniProtKB:Q5T3U5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC Evidence={ECO:0000250|UniProtKB:Q5T3U5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted glutathione(in) + ATP + H2O = ADP + an S-
CC substituted glutathione(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:19121, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:90779,
CC ChEBI:CHEBI:456216; EC=7.6.2.3;
CC Evidence={ECO:0000250|UniProtKB:Q5T3U5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122;
CC Evidence={ECO:0000250|UniProtKB:Q5T3U5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ATP + H2O =
CC 17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:60128, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:82961, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q5T3U5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129;
CC Evidence={ECO:0000250|UniProtKB:Q5T3U5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + leukotriene C4(in) = ADP + H(+) + leukotriene
CC C4(out) + phosphate; Xref=Rhea:RHEA:38963, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57973, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q5T3U5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964;
CC Evidence={ECO:0000250|UniProtKB:Q5T3U5};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5T3U5};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5T3U5,
CC ECO:0000255|PROSITE-ProRule:PRU00441}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q5T3U5}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Mrp7B;
CC IsoId=Q8R4P9-1; Sequence=Displayed;
CC Name=2; Synonyms=Mrp7A;
CC IsoId=Q8R4P9-2; Sequence=VSP_021081, VSP_021082;
CC Name=3;
CC IsoId=Q8R4P9-3; Sequence=VSP_021083;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested including liver,
CC brain, heart, skeletal muscle, kidney and spleen.
CC {ECO:0000269|PubMed:11943485}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo.
CC {ECO:0000269|PubMed:11943485}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice exhibit increased sensitivity to
CC paclitaxel-induced mortality associated with weight loss, decreased
CC white blood cell, and small spleen and thymus cortex due to apoptosis
CC and/or depopulation of lymphoid cells. {ECO:0000269|PubMed:21576088}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {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; AF406642; AAM18535.1; -; mRNA.
DR EMBL; AF417121; AAM18536.1; -; mRNA.
DR EMBL; AK133240; BAE21573.1; -; mRNA.
DR EMBL; AK170600; BAE41905.1; -; mRNA.
DR CCDS; CCDS28825.1; -. [Q8R4P9-2]
DR CCDS; CCDS50124.1; -. [Q8R4P9-1]
DR CCDS; CCDS84315.1; -. [Q8R4P9-3]
DR RefSeq; NP_001334325.1; NM_001347396.1. [Q8R4P9-3]
DR RefSeq; NP_660122.1; NM_145140.2. [Q8R4P9-2]
DR RefSeq; NP_733780.1; NM_170680.2. [Q8R4P9-1]
DR AlphaFoldDB; Q8R4P9; -.
DR SMR; Q8R4P9; -.
DR STRING; 10090.ENSMUSP00000131843; -.
DR iPTMnet; Q8R4P9; -.
DR PhosphoSitePlus; Q8R4P9; -.
DR SwissPalm; Q8R4P9; -.
DR MaxQB; Q8R4P9; -.
DR PaxDb; Q8R4P9; -.
DR PRIDE; Q8R4P9; -.
DR ProteomicsDB; 291412; -. [Q8R4P9-1]
DR ProteomicsDB; 291413; -. [Q8R4P9-2]
DR ProteomicsDB; 291414; -. [Q8R4P9-3]
DR Antibodypedia; 30398; 275 antibodies from 30 providers.
DR DNASU; 224814; -.
DR Ensembl; ENSMUST00000047970; ENSMUSP00000038041; ENSMUSG00000032842. [Q8R4P9-3]
DR Ensembl; ENSMUST00000095261; ENSMUSP00000092895; ENSMUSG00000032842. [Q8R4P9-2]
DR Ensembl; ENSMUST00000167360; ENSMUSP00000131843; ENSMUSG00000032842. [Q8R4P9-1]
DR GeneID; 224814; -.
DR KEGG; mmu:224814; -.
DR UCSC; uc008csn.1; mouse. [Q8R4P9-2]
DR UCSC; uc008cso.1; mouse. [Q8R4P9-1]
DR UCSC; uc012auq.1; mouse. [Q8R4P9-3]
DR CTD; 89845; -.
DR MGI; MGI:2386976; Abcc10.
DR VEuPathDB; HostDB:ENSMUSG00000032842; -.
DR eggNOG; KOG0054; Eukaryota.
DR GeneTree; ENSGT00940000161082; -.
DR HOGENOM; CLU_000604_27_1_1; -.
DR InParanoid; Q8R4P9; -.
DR OMA; PPYAWPS; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; Q8R4P9; -.
DR TreeFam; TF105203; -.
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR BioGRID-ORCS; 224814; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Abcc10; mouse.
DR PRO; PR:Q8R4P9; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8R4P9; protein.
DR Bgee; ENSMUSG00000032842; Expressed in substantia nigra and 125 other tissues.
DR ExpressionAtlas; Q8R4P9; baseline and differential.
DR Genevisible; Q8R4P9; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0015431; F:ABC-type glutathione S-conjugate transporter activity; ISS:UniProtKB.
DR GO; GO:0140359; F:ABC-type transporter activity; ISS:UniProtKB.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006691; P:leukotriene metabolic process; ISS:UniProtKB.
DR GO; GO:0071716; P:leukotriene transport; ISS:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Lipid transport;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1501
FT /note="ATP-binding cassette sub-family C member 10"
FT /id="PRO_0000253577"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 508..528
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 539..559
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 877..897
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 969..989
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1033..1053
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1056..1076
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1158..1178
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1187..1207
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 286..564
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 599..825
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 887..1215
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1255..1488
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 634..641
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1289..1296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 464
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5T3U5"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T3U5"
FT VAR_SEQ 1..41
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11943485"
FT /id="VSP_021081"
FT VAR_SEQ 42..53
FT /note="LAVLSACHLGTP -> MICGLLFFSFFP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11943485"
FT /id="VSP_021082"
FT VAR_SEQ 1377
FT /note="M -> MGESQACQRSQREAKNGHWQCSALLT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021083"
SQ SEQUENCE 1501 AA; 163735 MW; 573D5CFA52DDF3BA CRC64;
MEGLLAQLCG TDAARPLPLW EGDTTGHCFT QLVLSALPHA LLAVLSACHL GTPRTTNHSP
ALNPGWRLRL AASFLLSIFP LLDLLPVVLP PGSRPGPLWL EVLAGCVTAV AWFTHSLALW
ALVHSPHGRS RGPLALALAA FLPTPALVLT LLWHCQRGTF LPPLLPGPLG RVCLLILQLA
AVLAYGLGWA APGGPQEPWT HDPFLSSESQ ETEVAEDGES WLSRFSYAWL APLLARGVRG
ELQQPRDTCR LPRRLHPAFL ARVFQAHWKE GAQLWRALYR AFGCCYLALG LLKMVGTMLG
FSGPLLLSLL VGFLEEGQEP LSHGLLYVLG LAGGTVISAV LQNQYGYEVR KVTLQARVAV
LSTLYRKALK LGPSRPPTGE VLNLLGTDSE RLLNFAGSFH EAWGLPLQLA ITLYLLYQQV
GMAFLAGLVL ALLLVPVNKV IATRIMASNQ EMLRHKDARV KLMTELLSGI RVIKFFRWEQ
ALGDRVKACR TKELGRLRVI KYLDAACVYL WAALPVVICI TIFITYVLMG HQLTATKVFT
ALALVRMLIL PLNNFPWVIN GLLESKVSLD RIQRFLDLPS YSPEAYYSPD PPAEPSTALE
LHEALFSWDP IGASQKTFIS HLQVKKGMLV GIVGKVGCGK SSLLAAITGE LHRLCGWVAV
SELSKGFGLA TQEPWIQCAT IRDNILFGKT FDAQLYREVL EACALNDDLS ILPAGDQTEV
GEKGVTLSGG QRARIALARA VYQEKALYLL DDPLAAVDAD VANHLLHRCI LGVLSHTTRL
LCTHRTEYLE RADVVLLMEA GQLVRTGPPS EILPLVQAVP TAWAEKEQVA TSGQSPSVCD
LERTTEEELE VEQSTCGCLV QEESKSEGAV ALHVYRAYWR AMGSGLAAAI LVSLLLMQAT
RNGADWWLAH WLSQLKAGRN GSREDPASCS PGSTALFSPR LLLFSPGNLY TPLLSTPLHK
AASNGTADVH FYLIVYATIA GVNSLCTLLR AVLFAAGALQ AAASLHHRLL HRLLMAPVTF
YDSTPSGRVL NRFSSDVACV DDSLPFLLNI LLANSVGLLG LLAVLGSGLP WLLLLLPPLS
FVYYSVQGYY RASFRELRRL GSLTWSPLYS HLADTLAGLP VLRAAGATYR FEEENQRLLE
LNQRCQFASY ATMQWLDIRL QLMGAAVVSA IAGIALVQHQ QGLANPGLVG LVLSYALSLT
GLLSGLVSSF TQTEAMMVSV ERLEEYSCDV PQEPHSQPLQ SPHQQRISWL TQGSVEFQDV
VLVYRPGLPN ALDGVTFRVE PGEKLGIVGR TGSGKSSLFL VLFRLLEPNA GRVLLDNVDT
SQLELAELRS QLAVIPQEPF LFSGTIRENL DPQGLHEDRA LWQALEQCHL SEVAVAMGGL
DGELGERGQN LSLGQRQLLC LARALLTDAK ILCIDEATAS VDQKTDQLLQ QTICKRFANK
TVLTIAHRLN TILNSDRVLV LQAGRVVELD SPSALRNQPH SLFQQLLQSS QQGAHSGPSG
C
