FRPD1_HUMAN
ID FRPD1_HUMAN Reviewed; 1578 AA.
AC Q5SYB0; B4DZC8; B7Z807; D3DRQ3; Q14C73; Q5HY96; Q9Y2H3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=FERM and PDZ domain-containing protein 1;
DE AltName: Full=FERM domain-containing protein 2;
GN Name=FRMPD1; Synonyms=FRMD2, KIAA0967;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Retina;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(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 1), AND VARIANT ASP-846.
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 INTERACTION WITH GPSM1, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18566450; DOI=10.1074/jbc.m803497200;
RA An N., Blumer J.B., Bernard M.L., Lanier S.M.;
RT "The PDZ and band 4.1 containing protein Frmpd1 regulates the subcellular
RT location of activator of G-protein signaling 3 and its interaction with G-
RT proteins.";
RL J. Biol. Chem. 283:24718-24728(2008).
RN [8]
RP STRUCTURE BY NMR OF 54-136.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PDZ domain from human FERM and PDZ domain-
RT containing 1.";
RL Submitted (AUG-2007) to the PDB data bank.
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 901-938 IN COMPLEX WITH GPSM2,
RP INTERACTION WITH GPSM2, MUTAGENESIS OF GLU-924; GLU-929 AND LYS-931, AND
RP REGION.
RX PubMed=23318951; DOI=10.1016/j.jmb.2013.01.003;
RA Pan Z., Shang Y., Jia M., Zhang L., Xia C., Zhang M., Wang W., Wen W.;
RT "Structural and biochemical characterization of the interaction between LGN
RT and Frmpd1.";
RL J. Mol. Biol. 425:1039-1049(2013).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] ASP-572.
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: Stabilizes membrane-bound GPSM1, and thereby promotes its
CC interaction with GNAI1. {ECO:0000269|PubMed:18566450}.
CC -!- SUBUNIT: Interacts with GPSM1 (PubMed:18566450). Interacts with GPSM2
CC (via TPR repeat region) (PubMed:23318951).
CC {ECO:0000269|PubMed:18566450, ECO:0000269|PubMed:23318951}.
CC -!- INTERACTION:
CC Q5SYB0; P43360: MAGEA6; NbExp=3; IntAct=EBI-10245120, EBI-1045155;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18566450}.
CC Cell membrane {ECO:0000269|PubMed:18566450}; Peripheral membrane
CC protein {ECO:0000269|PubMed:18566450}; Cytoplasmic side
CC {ECO:0000269|PubMed:18566450}. Note=Found both in the cytoplasm and
CC associated with the cell membrane. {ECO:0000269|PubMed:18566450}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5SYB0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SYB0-2; Sequence=VSP_056060, VSP_056063, VSP_056064;
CC Name=3;
CC IsoId=Q5SYB0-3; Sequence=VSP_056061, VSP_056062, VSP_056063,
CC VSP_056064;
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DR EMBL; AB023184; BAA76811.1; -; mRNA.
DR EMBL; AK302739; BAH13793.1; -; mRNA.
DR EMBL; AK302854; BAG64040.1; -; mRNA.
DR EMBL; BX648967; CAI46019.1; -; mRNA.
DR EMBL; AL513165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591470; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58270.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58271.1; -; Genomic_DNA.
DR EMBL; BC114965; AAI14966.1; -; mRNA.
DR CCDS; CCDS6612.1; -. [Q5SYB0-1]
DR RefSeq; NP_055722.2; NM_014907.2. [Q5SYB0-1]
DR RefSeq; XP_011516105.1; XM_011517803.2.
DR RefSeq; XP_011516106.1; XM_011517804.2.
DR RefSeq; XP_016869969.1; XM_017014480.1.
DR PDB; 2EDV; NMR; -; A=54-136.
DR PDB; 4G2V; X-ray; 2.40 A; B=901-938.
DR PDBsum; 2EDV; -.
DR PDBsum; 4G2V; -.
DR AlphaFoldDB; Q5SYB0; -.
DR SMR; Q5SYB0; -.
DR BioGRID; 116516; 4.
DR ELM; Q5SYB0; -.
DR IntAct; Q5SYB0; 4.
DR MINT; Q5SYB0; -.
DR STRING; 9606.ENSP00000444411; -.
DR iPTMnet; Q5SYB0; -.
DR PhosphoSitePlus; Q5SYB0; -.
DR BioMuta; FRMPD1; -.
DR DMDM; 74754275; -.
DR EPD; Q5SYB0; -.
DR jPOST; Q5SYB0; -.
DR MassIVE; Q5SYB0; -.
DR PaxDb; Q5SYB0; -.
DR PeptideAtlas; Q5SYB0; -.
DR PRIDE; Q5SYB0; -.
DR ProteomicsDB; 5590; -.
DR ProteomicsDB; 64023; -. [Q5SYB0-1]
DR ProteomicsDB; 6913; -.
DR Antibodypedia; 26299; 108 antibodies from 24 providers.
DR DNASU; 22844; -.
DR Ensembl; ENST00000377765.8; ENSP00000366995.3; ENSG00000070601.10. [Q5SYB0-1]
DR Ensembl; ENST00000539465.5; ENSP00000444411.1; ENSG00000070601.10. [Q5SYB0-1]
DR GeneID; 22844; -.
DR KEGG; hsa:22844; -.
DR MANE-Select; ENST00000377765.8; ENSP00000366995.3; NM_014907.3; NP_055722.2.
DR UCSC; uc004aag.2; human. [Q5SYB0-1]
DR CTD; 22844; -.
DR DisGeNET; 22844; -.
DR GeneCards; FRMPD1; -.
DR HGNC; HGNC:29159; FRMPD1.
DR HPA; ENSG00000070601; Tissue enriched (retina).
DR MIM; 616919; gene.
DR neXtProt; NX_Q5SYB0; -.
DR OpenTargets; ENSG00000070601; -.
DR PharmGKB; PA134910182; -.
DR VEuPathDB; HostDB:ENSG00000070601; -.
DR eggNOG; KOG3552; Eukaryota.
DR GeneTree; ENSGT00950000183035; -.
DR HOGENOM; CLU_003698_0_0_1; -.
DR InParanoid; Q5SYB0; -.
DR OMA; ESMDDVC; -.
DR OrthoDB; 30821at2759; -.
DR PhylomeDB; Q5SYB0; -.
DR TreeFam; TF316497; -.
DR PathwayCommons; Q5SYB0; -.
DR SignaLink; Q5SYB0; -.
DR BioGRID-ORCS; 22844; 12 hits in 1068 CRISPR screens.
DR ChiTaRS; FRMPD1; human.
DR EvolutionaryTrace; Q5SYB0; -.
DR GenomeRNAi; 22844; -.
DR Pharos; Q5SYB0; Tbio.
DR PRO; PR:Q5SYB0; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5SYB0; protein.
DR Bgee; ENSG00000070601; Expressed in dorsal root ganglion and 105 other tissues.
DR ExpressionAtlas; Q5SYB0; baseline and differential.
DR Genevisible; Q5SYB0; HS.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IMP:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IMP:UniProtKB.
DR GO; GO:0090150; P:establishment of protein localization to membrane; IMP:UniProtKB.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13183; FERM_C_FRMPD1_FRMPD3_FRMPD4; 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 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.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm; Membrane;
KW Reference proteome.
FT CHAIN 1..1578
FT /note="FERM and PDZ domain-containing protein 1"
FT /id="PRO_0000306805"
FT DOMAIN 57..135
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 181..496
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 555..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..931
FT /note="Important for interaction with GPSM2"
FT /evidence="ECO:0000269|PubMed:23318951"
FT REGION 950..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1347..1374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..178
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056060"
FT VAR_SEQ 1..5
FT /note="MEELE -> MAEVG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056061"
FT VAR_SEQ 6..136
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056062"
FT VAR_SEQ 787..812
FT /note="PRDVSTAEPSATSLQNKASTSSPENS -> EPSLAGLQTRQAAPECLPGIKA
FT WGQA (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056063"
FT VAR_SEQ 813..1578
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056064"
FT VARIANT 6
FT /note="T -> P (in dbSNP:rs3747539)"
FT /id="VAR_035306"
FT VARIANT 44
FT /note="A -> T (in dbSNP:rs2296556)"
FT /id="VAR_035307"
FT VARIANT 50
FT /note="T -> N (in dbSNP:rs7031966)"
FT /id="VAR_035308"
FT VARIANT 225
FT /note="A -> V (in dbSNP:rs1359590)"
FT /id="VAR_035309"
FT VARIANT 572
FT /note="G -> D (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035445"
FT VARIANT 846
FT /note="Y -> D (in dbSNP:rs34233395)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035310"
FT VARIANT 1092
FT /note="G -> E (in dbSNP:rs35075933)"
FT /id="VAR_035311"
FT MUTAGEN 924
FT /note="E->A: Abolishes interaction with GPSM2."
FT /evidence="ECO:0000269|PubMed:23318951"
FT MUTAGEN 929
FT /note="E->A: Strongly reduces GPSM2 binding."
FT /evidence="ECO:0000269|PubMed:23318951"
FT MUTAGEN 931
FT /note="K->A: Strongly reduces GPSM2 binding."
FT /evidence="ECO:0000269|PubMed:23318951"
FT CONFLICT 404
FT /note="T -> A (in Ref. 3; CAI46019)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="I -> T (in Ref. 3; CAI46019)"
FT /evidence="ECO:0000305"
FT CONFLICT 1278
FT /note="S -> L (in Ref. 1; BAA76811)"
FT /evidence="ECO:0000305"
FT CONFLICT 1418
FT /note="T -> A (in Ref. 3; CAI46019)"
FT /evidence="ECO:0000305"
FT CONFLICT 1446
FT /note="H -> I (in Ref. 3; CAI46019)"
FT /evidence="ECO:0000305"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:2EDV"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:2EDV"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:2EDV"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:2EDV"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:2EDV"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:2EDV"
FT HELIX 113..122
FT /evidence="ECO:0007829|PDB:2EDV"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:2EDV"
SQ SEQUENCE 1578 AA; 173437 MW; DE1D285EEC3A743E CRC64;
MEELETSLFQ TRKAHRIEQM VARWLRRSRD SSARAKVAAA DGPARNPTQT LIPVRHTVKI
DKDTLLQDYG FHISESLPLT VVAVTAGGSA HGKLFPGDQI LQMNNEPAED LSWERAVDIL
REAEDSLSIT VVRCTSGVPK SSFLTEEKRA RLKTNPVKVH FAEEVLISGH SQGNSLLCMP
NVLKLYLENG QTKAFKFEAN TTVKDIILTV KEKLSIRSIE YFALALEEQY SISRLHLLHE
EELIQQVVER EESHDYRCLF RVCFVPKDPL DLLKEDPVAF EYLYLQSCSD VLQERFAVEM
KCSSALRLAA LHIQERIYAC AQPQKISLKY IEKDWGIENF ISPTLLRNMK GKDIKKAISF
HMKRNQNLLE PRQKQLISAA QLRLNYLQIL GELKTYGGRI FNATLMLQDR ESYIALLVGA
KYGISQVINS KLNIMSTLAE FANISRVELT EESEKVSVVK VYLQDVKVLT LLLESNSAKD
LACLIAGYYR LLVDPVTSIF LWPGNKQQAH RVSAEEGYES RACSDSEESS EVDCVLEPLS
DRRLVKLAPC RSLIKEEQPP GNSPTPEVAR RGPSTCGASS TTDSAESEAS DSANTESRGY
RTSGSSESMD ALEEDDLDTC SSSRSTFFHF GSPGLAESID SDSQEERSGI ETSGFLCLLD
LAQRANPQCQ KTEFSESAAL ETFGWAPELS TVRLDPRLYE GSHADYYSLC SSVSPASYLS
DSSESTASRQ GGAPPAWGQQ GWTEAQPSSM LEPLALHPPL AFEDGSSDEE YYDAADKLTP
PGPPSGPRDV STAEPSATSL QNKASTSSPE NSLPCGPDGR QPSRRGGVKK YAKTLRKRRS
FLQTDYTSQV SFPLVPSASL ESVDDVCYYD REPYLALGAP SPTVSSLQDM QGEPGLLETK
ALGLLAPLRE TKSTNPASRV MEMEPETMET KSVIDSRVSS ISAIRFRIDP NNKENSGVVP
AASSSASTPH CSNPGSSGPD TAQARPSQIL PLSQDLDGIA PKEPTIEHGD SSFSLSSGDP
NPDRACLASN PGLNNVSQGD TLELQLEPHV QLEMGLESFC TNHIQETAPK YTEPLLSPRD
EPRSDECGIN PGEKIASIPT KEEPQGQLSL ERDREVTNKN GTNVFQEESR KDSGDSPGDV
SNNVSQTLDI SSPAGKIVTS LSLDAPVTGT EQIPPHPPRD PQGQSREPPG QGCQAQEQKL
FVELDLDPDF FLGKQTVSPA VPPEGIKAEA PNHVTGQDIA PRDSPEWVCF NPEPSLPEPL
PCPQEDPHLE TSNHCLLSEG KSDSSSICLS AEKSFLCFAP ESHPEVSASL RVATSLGFAG
MNEMVAPRIG MDQCSCQFSY ATCFRGPQPE TEEEDRDLEA HPMAPLTSPP SAGSPVVLPW
RPARAHSCTT APLSRKSHIW PEYCSRALRQ LKATPASTPE GFIQLMESLL ELQDILETSW
GVGNKHPPEK CTWHFTESRS RLCMGSQKLL SSCRHVIRMD QSPEEMQGAV RDTFQHLVQL
AGLCFQFTDC SRCSARHREA AGNLRDVVYT YHQFIEAAKS TCERGYHDLS VKLLARQCTA
LTAAVFCLTQ KFRASTAL
