FRPD4_HUMAN
ID FRPD4_HUMAN Reviewed; 1322 AA.
AC Q14CM0; A8K0X9; O15032;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=FERM and PDZ domain-containing protein 4;
DE AltName: Full=PDZ domain-containing protein 10;
DE AltName: Full=PSD-95-interacting regulator of spine morphogenesis;
DE Short=Preso;
GN Name=FRMPD4; Synonyms=KIAA0316, PDZD10, PDZK10;
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].
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Nomura N.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
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 MRNA].
RC TISSUE=Brain;
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 [5]
RP FUNCTION, INTERACTION WITH DLG1; DLG2; DLG3; DLG4; ARHGEF7 AND
RP PHOSPHATIDYLINOSITOL-4,5-BIPHOSPHATE, DOMAIN FERM, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF ARG-102; 1319-GLU--VAL-1322 AND THR-1320.
RX PubMed=19118189; DOI=10.1523/jneurosci.3112-08.2008;
RA Lee H.W., Choi J., Shin H., Kim K., Yang J., Na M., Choi S.Y., Kang G.B.,
RA Eom S.H., Kim H., Kim E.;
RT "Preso, a novel PSD-95-interacting FERM and PDZ domain protein that
RT regulates dendritic spine morphogenesis.";
RL J. Neurosci. 28:14546-14556(2008).
RN [6]
RP IDENTIFICATION BY 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 [7]
RP INVOLVEMENT IN XLID104, AND VARIANT XLID104 ARG-553.
RX PubMed=25644381; DOI=10.1038/mp.2014.193;
RA Hu H., Haas S.A., Chelly J., Van Esch H., Raynaud M., de Brouwer A.P.,
RA Weinert S., Froyen G., Frints S.G., Laumonnier F., Zemojtel T., Love M.I.,
RA Richard H., Emde A.K., Bienek M., Jensen C., Hambrock M., Fischer U.,
RA Langnick C., Feldkamp M., Wissink-Lindhout W., Lebrun N., Castelnau L.,
RA Rucci J., Montjean R., Dorseuil O., Billuart P., Stuhlmann T., Shaw M.,
RA Corbett M.A., Gardner A., Willis-Owen S., Tan C., Friend K.L., Belet S.,
RA van Roozendaal K.E., Jimenez-Pocquet M., Moizard M.P., Ronce N., Sun R.,
RA O'Keeffe S., Chenna R., van Boemmel A., Goeke J., Hackett A., Field M.,
RA Christie L., Boyle J., Haan E., Nelson J., Turner G., Baynam G.,
RA Gillessen-Kaesbach G., Mueller U., Steinberger D., Budny B.,
RA Badura-Stronka M., Latos-Bielenska A., Ousager L.B., Wieacker P.,
RA Rodriguez Criado G., Bondeson M.L., Anneren G., Dufke A., Cohen M.,
RA Van Maldergem L., Vincent-Delorme C., Echenne B., Simon-Bouy B.,
RA Kleefstra T., Willemsen M., Fryns J.P., Devriendt K., Ullmann R.,
RA Vingron M., Wrogemann K., Wienker T.F., Tzschach A., van Bokhoven H.,
RA Gecz J., Jentsch T.J., Chen W., Ropers H.H., Kalscheuer V.M.;
RT "X-exome sequencing of 405 unresolved families identifies seven novel
RT intellectual disability genes.";
RL Mol. Psychiatry 21:133-148(2016).
RN [8] {ECO:0007744|PDB:4WND, ECO:0007744|PDB:4WNE, ECO:0007744|PDB:4WNF, ECO:0007744|PDB:4WNG}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 978-1025 IN COMPLEX WITH GPSM2,
RP INTERACTION WITH GPSM2, AND MUTAGENESIS OF LEU-990 AND 1010-TYR-PHE-1011.
RX PubMed=25664792; DOI=10.1107/s2053230x14028143;
RA Takayanagi H., Yuzawa S., Sumimoto H.;
RT "Structural basis for the recognition of the scaffold protein Frmpd4/Preso1
RT by the TPR domain of the adaptor protein LGN.";
RL Acta Crystallogr. F 71:175-183(2015).
CC -!- FUNCTION: Positive regulator of dendritic spine morphogenesis and
CC density. Required for the maintenance of excitatory synaptic
CC transmission. Binds phosphatidylinositol 4,5-bisphosphate.
CC {ECO:0000269|PubMed:19118189}.
CC -!- SUBUNIT: Interacts (via C-terminus) with DLG1, DLG2, DLG3 and
CC DLG4/PSD95. Interacts (via N-terminus) with ARHGEF7; the interaction is
CC mediated by the PDZ domain (PubMed:19118189). Interacts with GPSM2 (via
CC TPR repeat region) (PubMed:25664792). {ECO:0000269|PubMed:19118189,
CC ECO:0000269|PubMed:25664792}.
CC -!- INTERACTION:
CC Q14CM0; Q12959: DLG1; NbExp=4; IntAct=EBI-311279, EBI-357481;
CC Q14CM0; Q14160: SCRIB; NbExp=2; IntAct=EBI-311279, EBI-357345;
CC Q14CM0; Q9Z214-1: Homer1; Xeno; NbExp=2; IntAct=EBI-311279, EBI-4410552;
CC -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine
CC {ECO:0000269|PubMed:19118189}.
CC -!- DOMAIN: The FERM domain mediates the interaction with
CC phosphatidylinositol 4,5-bisphosphate. {ECO:0000269|PubMed:19118189}.
CC -!- DISEASE: Intellectual developmental disorder, X-linked 104 (XLID104)
CC [MIM:300983]: A form of intellectual disability, a disorder
CC characterized by significantly below average general intellectual
CC functioning associated with impairments in adaptive behavior and
CC manifested during the developmental period. Intellectual deficiency is
CC the only primary symptom of non-syndromic X-linked forms, while
CC syndromic forms present with associated physical, neurological and/or
CC psychiatric manifestations. {ECO:0000269|PubMed:25644381}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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DR EMBL; AB002314; BAA20774.3; -; mRNA.
DR EMBL; AK289694; BAF82383.1; -; mRNA.
DR EMBL; BC113700; AAI13701.1; -; mRNA.
DR EMBL; BC113702; AAI13703.1; -; mRNA.
DR CCDS; CCDS35201.1; -.
DR RefSeq; NP_055543.2; NM_014728.3.
DR PDB; 4WND; X-ray; 1.50 A; B=978-1025.
DR PDB; 4WNE; X-ray; 2.00 A; B=987-1011.
DR PDB; 4WNF; X-ray; 2.90 A; B=978-1025.
DR PDB; 4WNG; X-ray; 2.11 A; B=978-1025.
DR PDB; 7BYJ; X-ray; 2.49 A; A=193-527.
DR PDBsum; 4WND; -.
DR PDBsum; 4WNE; -.
DR PDBsum; 4WNF; -.
DR PDBsum; 4WNG; -.
DR PDBsum; 7BYJ; -.
DR AlphaFoldDB; Q14CM0; -.
DR SMR; Q14CM0; -.
DR BioGRID; 115105; 8.
DR IntAct; Q14CM0; 15.
DR MINT; Q14CM0; -.
DR STRING; 9606.ENSP00000370057; -.
DR GlyGen; Q14CM0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14CM0; -.
DR PhosphoSitePlus; Q14CM0; -.
DR SwissPalm; Q14CM0; -.
DR BioMuta; FRMPD4; -.
DR DMDM; 121948742; -.
DR EPD; Q14CM0; -.
DR MassIVE; Q14CM0; -.
DR MaxQB; Q14CM0; -.
DR PaxDb; Q14CM0; -.
DR PeptideAtlas; Q14CM0; -.
DR PRIDE; Q14CM0; -.
DR ProteomicsDB; 60327; -.
DR Antibodypedia; 49701; 42 antibodies from 18 providers.
DR DNASU; 9758; -.
DR Ensembl; ENST00000380682.5; ENSP00000370057.1; ENSG00000169933.17.
DR GeneID; 9758; -.
DR KEGG; hsa:9758; -.
DR UCSC; uc004cuz.2; human.
DR CTD; 9758; -.
DR DisGeNET; 9758; -.
DR GeneCards; FRMPD4; -.
DR HGNC; HGNC:29007; FRMPD4.
DR HPA; ENSG00000169933; Group enriched (brain, parathyroid gland, retina).
DR MalaCards; FRMPD4; -.
DR MIM; 300838; gene.
DR MIM; 300983; phenotype.
DR neXtProt; NX_Q14CM0; -.
DR OpenTargets; ENSG00000169933; -.
DR Orphanet; 777; X-linked non-syndromic intellectual disability.
DR PharmGKB; PA134977575; -.
DR VEuPathDB; HostDB:ENSG00000169933; -.
DR eggNOG; KOG3552; Eukaryota.
DR GeneTree; ENSGT00950000183035; -.
DR HOGENOM; CLU_002690_0_0_1; -.
DR InParanoid; Q14CM0; -.
DR OrthoDB; 57420at2759; -.
DR PhylomeDB; Q14CM0; -.
DR TreeFam; TF316497; -.
DR PathwayCommons; Q14CM0; -.
DR SignaLink; Q14CM0; -.
DR BioGRID-ORCS; 9758; 10 hits in 691 CRISPR screens.
DR ChiTaRS; FRMPD4; human.
DR GenomeRNAi; 9758; -.
DR Pharos; Q14CM0; Tbio.
DR PRO; PR:Q14CM0; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q14CM0; protein.
DR Bgee; ENSG00000169933; Expressed in middle temporal gyrus and 82 other tissues.
DR ExpressionAtlas; Q14CM0; baseline and differential.
DR Genevisible; Q14CM0; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0051835; P:positive regulation of synapse structural plasticity; IMP:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13183; FERM_C_FRMPD1_FRMPD3_FRMPD4; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR041779; FRMPD1/3/4_FERM_C.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001202; WW_dom.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00295; B41; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Disease variant; Intellectual disability;
KW Lipid-binding; Reference proteome; Synapse.
FT CHAIN 1..1322
FT /note="FERM and PDZ domain-containing protein 4"
FT /id="PRO_0000307132"
FT DOMAIN 33..66
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 78..155
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 204..519
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 809..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1207..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 553
FT /note="C -> R (in XLID104; dbSNP:rs886038209)"
FT /evidence="ECO:0000269|PubMed:25644381"
FT /id="VAR_077481"
FT MUTAGEN 102
FT /note="R->A: Abolishes the interaction with ARHGEF7. Mutant
FT overexpression in cultured neurons does not induce a
FT significant increase in spine density contrary to wild
FT type."
FT /evidence="ECO:0000269|PubMed:19118189"
FT MUTAGEN 990
FT /note="L->A: Nearly abolishes interaction with GPSM2; when
FT associated with 1010-A-A-1011."
FT /evidence="ECO:0000269|PubMed:25664792"
FT MUTAGEN 1010..1011
FT /note="YF->AA: Nearly abolishes interaction with GPSM2;
FT when associated with A-990."
FT /evidence="ECO:0000269|PubMed:25664792"
FT MUTAGEN 1319..1322
FT /note="Missing: Abolishes the interaction with DLG1, DLG2,
FT DLG3 and DLG4/PSD95. Reduces protein localization to
FT dendritic spines."
FT /evidence="ECO:0000269|PubMed:19118189"
FT MUTAGEN 1320
FT /note="T->D: Abolishes the interaction with DLG4/PSD95.
FT Reduces protein localization to dendritic spines."
FT /evidence="ECO:0000269|PubMed:19118189"
FT CONFLICT 130
FT /note="A -> T (in Ref. 1; BAA20774)"
FT /evidence="ECO:0000305"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:7BYJ"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:7BYJ"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:7BYJ"
FT HELIX 226..237
FT /evidence="ECO:0007829|PDB:7BYJ"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:7BYJ"
FT STRAND 245..252
FT /evidence="ECO:0007829|PDB:7BYJ"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:7BYJ"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:7BYJ"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:7BYJ"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:7BYJ"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:7BYJ"
FT HELIX 294..300
FT /evidence="ECO:0007829|PDB:7BYJ"
FT HELIX 302..317
FT /evidence="ECO:0007829|PDB:7BYJ"
FT HELIX 327..343
FT /evidence="ECO:0007829|PDB:7BYJ"
FT HELIX 353..359
FT /evidence="ECO:0007829|PDB:7BYJ"
FT HELIX 362..365
FT /evidence="ECO:0007829|PDB:7BYJ"
FT HELIX 368..373
FT /evidence="ECO:0007829|PDB:7BYJ"
FT HELIX 376..393
FT /evidence="ECO:0007829|PDB:7BYJ"
FT HELIX 402..414
FT /evidence="ECO:0007829|PDB:7BYJ"
FT TURN 417..420
FT /evidence="ECO:0007829|PDB:7BYJ"
FT STRAND 422..430
FT /evidence="ECO:0007829|PDB:7BYJ"
FT STRAND 433..442
FT /evidence="ECO:0007829|PDB:7BYJ"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:7BYJ"
FT STRAND 446..452
FT /evidence="ECO:0007829|PDB:7BYJ"
FT TURN 453..456
FT /evidence="ECO:0007829|PDB:7BYJ"
FT STRAND 457..462
FT /evidence="ECO:0007829|PDB:7BYJ"
FT HELIX 464..466
FT /evidence="ECO:0007829|PDB:7BYJ"
FT STRAND 467..472
FT /evidence="ECO:0007829|PDB:7BYJ"
FT STRAND 476..486
FT /evidence="ECO:0007829|PDB:7BYJ"
FT STRAND 492..497
FT /evidence="ECO:0007829|PDB:7BYJ"
FT HELIX 498..515
FT /evidence="ECO:0007829|PDB:7BYJ"
FT HELIX 1007..1009
FT /evidence="ECO:0007829|PDB:4WND"
SQ SEQUENCE 1322 AA; 144379 MW; 79B73E41B89E2D08 CRC64;
MDVFSFVKIA KLSSHRTKSS GWPPPSGTWG LSQVPPYGWE MTANRDGRDY FINHMTQAIP
FDDPRLESCQ IIPPAPRKVE MRRDPVLGFG FVAGSEKPVV VRSVTPGGPS EGKLIPGDQI
VMINDEPVSA APRERVIDLV RSCKESILLT VIQPYPSPKS AFISAAKKAR LKSNPVKVRF
SEEVIINGQV SETVKDNSLL FMPNVLKVYL ENGQTKSFRF DCSTSIKDVI LTLQEKLSIK
GIEHFSLMLE QRTEGAGTKL LLLHEQETLT QVTQRPSSHK MRCLFRISFV PKDPIDLLRR
DPVAFEYLYV QSCNDVVQER FGPELKYDIA LRLAALQMYI ATVTTKQTQK ISLKYIEKEW
GLETFLPSAV LQSMKEKNIK KALSHLVKAN QNLVPPGKKL SALQAKVHYL KFLSDLRLYG
GRVFKATLVQ AEKRSEVTLL VGPRYGISHV INTKTNLVAL LADFSHVNRI EMFSEEESLV
RVELHVLDVK PITLLMESSD AMNLACLTAG YYRLLVDSRR SIFNMANKKN TATQETGPEN
KGKHNLLGPD WNCIPQMTTF IGEGEQEAQI TYIDSKQKTV EITDSTMCPK EHRHLYIDNA
YSSDGLNQQL SQPGEAPCEA DYRSLAQRSL LTLSGPETLK KAQESPRGAK VSFIFGDFAL
DDGISPPTLG YETLLDEGPE MLEKQRNLYI GSANDMKGLD LTPEAEGIQF VENSVYANIG
DVKSFQAAEG IEEPLLHDIC YAENTDDAED EDEVSCEEDL VVGEMNQPAI LNLSGSSDDI
IDLTSLPPPE GDDNEDDFLL RSLNMAIAAP PPGFRDSSDE EDSQSQAASF PEDKEKGSSL
QNDEIPVSLI DAVPTSAEGK CEKGLDNAVV STLGALEALS VSEEQQTSDN SGVAILRAYS
PESSSDSGNE TNSSEMTESS ELATAQKQSE NLSRMFLATH EGYHPLAEEQ TEFPASKTPA
GGLPPKSSHA LAARPATDLP PKVVPSKQLL HSDHMEMEPE TMETKSVTDY FSKLHMGSVA
YSCTSKRKSK LADGEGKAPP NGNTTGKKQQ GTKTAEMEEE ASGKFGTVSS RDSQHLSTFN
LERTAFRKDS QRWYVATEGG MAEKSGLEAA TGKTFPRASG LGAREAEGKE EGAPDGETSD
GSGLGQGDRF LTDVTCASSA KDLDNPEDAD SSTCDHPSKL PEADESVARL CDYHLAKRMS
SLQSEGHFSL QSSQGSSVDA GCGTGSSGSA CATPVESPLC PSLGKHLIPD ASGKGVNYIP
SEERAPGLPN HGATFKELHP QTEGMCPRMT VPALHTAINT EPLFGTLRDG CHRLPKIKET
TV
