NHRF4_HUMAN
ID NHRF4_HUMAN Reviewed; 571 AA.
AC Q86UT5; Q8N6R4; Q8NAW7; Q8NEX7; Q9H5Z3;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Na(+)/H(+) exchange regulatory cofactor NHE-RF4;
DE Short=NHERF-4;
DE AltName: Full=Intestinal and kidney-enriched PDZ protein;
DE AltName: Full=Natrium-phosphate cotransporter IIa C-terminal-associated protein 2;
DE Short=Na/Pi cotransporter C-terminal-associated protein 2;
DE Short=NaPi-Cap2;
DE AltName: Full=PDZ domain-containing protein 2;
DE AltName: Full=PDZ domain-containing protein 3;
DE AltName: Full=Sodium-hydrogen exchanger regulatory factor 4;
GN Name=PDZD3; Synonyms=IKEPP, NHERF4, PDZK2; ORFNames=DLNB27;
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] {ECO:0000305, ECO:0000312|EMBL:AAL10686.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH GUCY2C,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Intestinal epithelium {ECO:0000269|PubMed:11950846};
RX PubMed=11950846; DOI=10.1074/jbc.m202434200;
RA Scott R.O., Thelin W.R., Milgram S.L.;
RT "A novel PDZ protein regulates the activity of guanylyl cyclase C, the
RT heat-stable enterotoxin receptor.";
RL J. Biol. Chem. 277:22934-22941(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC76050.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Kubo T., Arai Y., Ohira M., Gamou T., Maeno G., Sakiyama T., Toyoda A.,
RA Hattori M., Sakaki Y., Nakagawara A., Ohki M.;
RT "Identification of a 500-kb region of common allelic loss in chromosome
RT 11q23 in non-MYCN amplified type of neuroblastoma.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAC03780.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC TISSUE=Ileal mucosa {ECO:0000312|EMBL:BAB15474.1}, and
RC Kidney {ECO:0000312|EMBL:BAC03780.1};
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=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAH29042.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SLC9A3.
RX PubMed=19088451; DOI=10.1159/000185553;
RA Zachos N.C., Hodson C., Kovbasnjuk O., Li X., Thelin W.R., Cha B.,
RA Milgram S., Donowitz M.;
RT "Elevated intracellular calcium stimulates NHE3 activity by an IKEPP
RT (NHERF4) dependent mechanism.";
RL Cell. Physiol. Biochem. 22:693-704(2008).
RN [7] {ECO:0000305, ECO:0000312|EMBL:BAC76050.1}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 326-415.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the 3rd PDZ domain of intestine- and kidney-enriched
RT PDZ domain IKEPP (PDZD3).";
RL Submitted (JUL-2011) to the PDB data bank.
RN [8]
RP INTERACTION WITH USP2.
RX PubMed=26756164; DOI=10.1371/journal.pone.0145155;
RA Pouly D., Chenaux S., Martin V., Babis M., Koch R., Nagoshi E.,
RA Katanaev V.L., Gachon F., Staub O.;
RT "USP2-45 is a circadian clock output effector regulating calcium absorption
RT at the post-translational level.";
RL PLoS ONE 11:E0145155-E0145155(2016).
CC -!- FUNCTION: Acts as a regulatory protein that associates with GUCY2C and
CC negatively modulates its heat-stable enterotoxin-mediated activation
CC (PubMed:11950846). Stimulates SLC9A3 activity in the presence of
CC elevated calcium ions (PubMed:19088451). {ECO:0000269|PubMed:11950846,
CC ECO:0000269|PubMed:19088451}.
CC -!- SUBUNIT: Interacts with the C-terminal region of GUCY2C
CC (PubMed:11950846). Interacts with the C-terminal region SLC9A3 and the
CC interactions decrease in response to elevated calcium ion levels
CC (PubMed:19088451). Interacts with the C-terminal region of SLC34A1 (By
CC similarity). Interacts with USP2 isoform 4 (PubMed:26756164).
CC {ECO:0000250|UniProtKB:Q99MJ6, ECO:0000269|PubMed:11950846,
CC ECO:0000269|PubMed:19088451, ECO:0000269|PubMed:26756164}.
CC -!- INTERACTION:
CC Q86UT5; Q8TDY4: ASAP3; NbExp=3; IntAct=EBI-8744528, EBI-2609717;
CC Q86UT5; Q13698: CACNA1S; NbExp=3; IntAct=EBI-8744528, EBI-5329490;
CC Q86UT5; Q96GZ6: SLC41A3; NbExp=3; IntAct=EBI-8744528, EBI-7225508;
CC Q86UT5; Q5W111: SPRYD7; NbExp=3; IntAct=EBI-8744528, EBI-10248098;
CC Q86UT5-2; P25092: GUCY2C; NbExp=4; IntAct=EBI-8299496, EBI-2816795;
CC Q86UT5-3; Q8TDY4: ASAP3; NbExp=3; IntAct=EBI-12092811, EBI-2609717;
CC Q86UT5-3; Q9NYW2: TAS2R8; NbExp=3; IntAct=EBI-12092811, EBI-12092809;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11950846,
CC ECO:0000269|PubMed:19088451}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11950846, ECO:0000269|PubMed:19088451}. Cytoplasm
CC {ECO:0000269|PubMed:19088451}. Note=Preferentially accumulates at the
CC apical surface and ileal brush border of intestinal epithelial cells
CC (PubMed:11950846, PubMed:19088451). {ECO:0000269|PubMed:11950846,
CC ECO:0000269|PubMed:19088451}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1 {ECO:0000269|Ref.2};
CC IsoId=Q86UT5-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:11950846};
CC IsoId=Q86UT5-2; Sequence=VSP_051786, VSP_051787;
CC Name=3 {ECO:0000305};
CC IsoId=Q86UT5-3; Sequence=VSP_051786, VSP_051787, VSP_051788;
CC Name=4 {ECO:0000305};
CC IsoId=Q86UT5-4; Sequence=VSP_051790, VSP_051791;
CC Name=5 {ECO:0000305};
CC IsoId=Q86UT5-5; Sequence=VSP_051786, VSP_051787, VSP_051789;
CC -!- TISSUE SPECIFICITY: Expressed in kidney and the gastrointestinal tract.
CC Not detected in brain, heart, skeletal muscle or cells of hematopoietic
CC origin. {ECO:0000269|PubMed:11950846}.
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DR EMBL; AY047359; AAL10686.1; -; mRNA.
DR EMBL; AB094096; BAC76050.1; -; mRNA.
DR EMBL; AK026409; BAB15474.1; -; mRNA.
DR EMBL; AK091966; BAC03780.1; -; mRNA.
DR EMBL; AP002956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029042; AAH29042.1; -; mRNA.
DR CCDS; CCDS53719.1; -. [Q86UT5-2]
DR CCDS; CCDS8417.1; -. [Q86UT5-3]
DR RefSeq; NP_001161940.1; NM_001168468.1. [Q86UT5-2]
DR RefSeq; NP_079067.3; NM_024791.3. [Q86UT5-3]
DR RefSeq; XP_011541302.1; XM_011543000.2. [Q86UT5-1]
DR RefSeq; XP_011541303.1; XM_011543001.2. [Q86UT5-1]
DR RefSeq; XP_011541304.1; XM_011543002.2. [Q86UT5-1]
DR PDB; 2V90; X-ray; 2.00 A; A/B/C/D/E/F=326-415.
DR PDBsum; 2V90; -.
DR AlphaFoldDB; Q86UT5; -.
DR SMR; Q86UT5; -.
DR BioGRID; 122940; 10.
DR IntAct; Q86UT5; 8.
DR MINT; Q86UT5; -.
DR STRING; 9606.ENSP00000347742; -.
DR iPTMnet; Q86UT5; -.
DR PhosphoSitePlus; Q86UT5; -.
DR BioMuta; PDZD3; -.
DR DMDM; 308153467; -.
DR MassIVE; Q86UT5; -.
DR MaxQB; Q86UT5; -.
DR PaxDb; Q86UT5; -.
DR PeptideAtlas; Q86UT5; -.
DR PRIDE; Q86UT5; -.
DR ProteomicsDB; 69882; -. [Q86UT5-1]
DR ProteomicsDB; 69883; -. [Q86UT5-2]
DR ProteomicsDB; 69884; -. [Q86UT5-3]
DR ProteomicsDB; 69885; -. [Q86UT5-4]
DR ProteomicsDB; 69886; -. [Q86UT5-5]
DR TopDownProteomics; Q86UT5-4; -. [Q86UT5-4]
DR Antibodypedia; 32648; 184 antibodies from 24 providers.
DR DNASU; 79849; -.
DR Ensembl; ENST00000322712.4; ENSP00000327107.4; ENSG00000172367.16. [Q86UT5-3]
DR Ensembl; ENST00000355547.10; ENSP00000347742.5; ENSG00000172367.16. [Q86UT5-2]
DR Ensembl; ENST00000531114.5; ENSP00000431164.1; ENSG00000172367.16. [Q86UT5-1]
DR GeneID; 79849; -.
DR KEGG; hsa:79849; -.
DR MANE-Select; ENST00000355547.10; ENSP00000347742.5; NM_001168468.2; NP_001161940.1. [Q86UT5-2]
DR UCSC; uc001pvy.4; human. [Q86UT5-1]
DR CTD; 79849; -.
DR DisGeNET; 79849; -.
DR GeneCards; PDZD3; -.
DR HGNC; HGNC:19891; PDZD3.
DR HPA; ENSG00000172367; Group enriched (intestine, kidney).
DR MIM; 607146; gene.
DR neXtProt; NX_Q86UT5; -.
DR OpenTargets; ENSG00000172367; -.
DR PharmGKB; PA134911718; -.
DR VEuPathDB; HostDB:ENSG00000172367; -.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00950000182849; -.
DR InParanoid; Q86UT5; -.
DR OMA; LPAKPRC; -.
DR OrthoDB; 880632at2759; -.
DR PhylomeDB; Q86UT5; -.
DR TreeFam; TF350449; -.
DR PathwayCommons; Q86UT5; -.
DR Reactome; R-HSA-8942233; Intestinal infectious diseases.
DR SignaLink; Q86UT5; -.
DR BioGRID-ORCS; 79849; 34 hits in 1063 CRISPR screens.
DR EvolutionaryTrace; Q86UT5; -.
DR GenomeRNAi; 79849; -.
DR Pharos; Q86UT5; Tbio.
DR PRO; PR:Q86UT5; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q86UT5; protein.
DR Bgee; ENSG00000172367; Expressed in mucosa of transverse colon and 112 other tissues.
DR ExpressionAtlas; Q86UT5; baseline and differential.
DR Genevisible; Q86UT5; HS.
DR GO; GO:0043296; C:apical junction complex; IDA:UniProtKB.
DR GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:UniProtKB.
DR GO; GO:0030251; F:guanylate cyclase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0008200; F:ion channel inhibitor activity; TAS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IBA:GO_Central.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:UniProtKB.
DR GO; GO:0006811; P:ion transport; NAS:UniProtKB.
DR GO; GO:0010754; P:negative regulation of cGMP-mediated signaling; IDA:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IC:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; TAS:UniProtKB.
DR GO; GO:0006833; P:water transport; NAS:UniProtKB.
DR Gene3D; 2.30.42.10; -; 4.
DR InterPro; IPR031200; NHERF-4.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR14191:SF20; PTHR14191:SF20; 1.
DR Pfam; PF00595; PDZ; 3.
DR Pfam; PF17820; PDZ_6; 1.
DR SMART; SM00228; PDZ; 4.
DR SUPFAM; SSF50156; SSF50156; 4.
DR PROSITE; PS50106; PDZ; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm; Membrane;
KW Reference proteome; Repeat.
FT CHAIN 1..571
FT /note="Na(+)/H(+) exchange regulatory cofactor NHE-RF4"
FT /id="PRO_0000058292"
FT DOMAIN 115..196
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 223..301
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 329..412
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 467..548
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 52..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..66
FT /note="Missing (in isoform 2, isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:11950846,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_051786"
FT VAR_SEQ 67..105
FT /note="TRQKLPSTLSGHRVCQAHGEPVLGLCPLLPLFCCPPHPP -> MEKAADLQD
FT TASLTLKFKFNPKLGIDNPVLSLAEDHDPY (in isoform 2, isoform 3 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:11950846,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_051787"
FT VAR_SEQ 272..285
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11950846,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_051788"
FT VAR_SEQ 287..571
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11950846,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_051789"
FT VAR_SEQ 355..386
FT /note="QFLWEVDPGLPAKKAGMQAGDRLVAVAGESVE -> EWEPWGRWGKVGLGVG
FT TQAYIHLSVHRRGVPV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11950846,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_051790"
FT VAR_SEQ 387..571
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11950846,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_051791"
FT CONFLICT 112
FT /note="R -> P (in Ref. 3; BAB15474)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="S -> G (in Ref. 3; BAC03780)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="L -> V (in Ref. 3; BAB15474)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="R -> Q (in Ref. 2; BAC76050 and 5; AAH29042)"
FT /evidence="ECO:0000305"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:2V90"
FT STRAND 341..347
FT /evidence="ECO:0007829|PDB:2V90"
FT STRAND 353..360
FT /evidence="ECO:0007829|PDB:2V90"
FT HELIX 365..368
FT /evidence="ECO:0007829|PDB:2V90"
FT STRAND 375..380
FT /evidence="ECO:0007829|PDB:2V90"
FT HELIX 390..398
FT /evidence="ECO:0007829|PDB:2V90"
FT TURN 399..402
FT /evidence="ECO:0007829|PDB:2V90"
FT STRAND 403..409
FT /evidence="ECO:0007829|PDB:2V90"
SQ SEQUENCE 571 AA; 61032 MW; B56CDC91348EE592 CRC64;
MVTPSPPGNH SLSLEAPRLH TASDLLGNHS LGLPLITALV GSRDRRGRVF SPVPVPLPTN
PTTQHPTRQK LPSTLSGHRV CQAHGEPVLG LCPLLPLFCC PPHPPDPWSL ERPRFCLLSK
EEGKSFGFHL QQELGRAGHV VCRVDPGTSA QRQGLQEGDR ILAVNNDVVE HEDYAVVVRR
IRASSPRVLL TVLARHAHDV ARAQLGEDAH LCPTLGPGVR PRLCHIVKDE GGFGFSVTHG
NQGPFWLVLS TGGAAERAGV PPGARLLEVN GVSVEKFTHN QLTRKLWQSG QQVTLLVAGP
EVEEQCRQLG LPLAAPLAEG WALPTKPRCL HLEKGPQGFG FLLREEKGLD GRPGQFLWEV
DPGLPAKKAG MQAGDRLVAV AGESVEGLGH EETVSRIQGQ GSCVSLTVVD PEADRFFSMV
RLSPLLFLEN TEAPASPRGS SSASLVETED PSLEDTSVPS VPLGSRQCFL YPGPGGSYGF
RLSCVASGPR LFISQVTPGG SAARAGLQVG DVILEVNGYP VGGQNDLERL QQLPEAEPPL
CLKLAARSLR GLEAWIPPGA AEDWALASDL L
