FRPD2_HUMAN
ID FRPD2_HUMAN Reviewed; 1309 AA.
AC Q68DX3; B7WNW0; B7ZML5; Q2VY07; Q6GMQ9; Q6ZN38; Q6ZWI2; Q8N5T9;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=FERM and PDZ domain-containing protein 2;
DE AltName: Full=PDZ domain-containing protein 4;
DE AltName: Full=PDZ domain-containing protein 5C;
GN Name=FRMPD2; Synonyms=PDZD5C, PDZK4, PDZK5C;
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 5).
RA Xu J., Xie Y., Mao Y.;
RT "Identification of a novel PDZ domain-containing gene.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANTS
RP GLU-534 AND LYS-1021.
RC TISSUE=Hippocampus, and Teratocarcinoma;
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), AND VARIANT LYS-1021.
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=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
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 [6]
RP FUNCTION, INTERACTION WITH ARVCF; CTNND2 AND PKP4, MUTAGENESIS OF LYS-955,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19706687; DOI=10.1242/jcs.046854;
RA Stenzel N., Fetzer C.P., Heumann R., Erdmann K.S.;
RT "PDZ-domain-directed basolateral targeting of the peripheral membrane
RT protein FRMPD2 in epithelial cells.";
RL J. Cell Sci. 122:3374-3384(2009).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] TRP-727.
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).
RN [8]
RP VARIANT ARG-351.
RX PubMed=22068589; DOI=10.1093/hmg/ddr509;
RA Khan K., Logan C.V., McKibbin M., Sheridan E., Elcioglu N.H., Yenice O.,
RA Parry D.A., Fernandez-Fuentes N., Abdelhamed Z.I., Al-Maskari A.,
RA Poulter J.A., Mohamed M.D., Carr I.M., Morgan J.E., Jafri H., Raashid Y.,
RA Taylor G.R., Johnson C.A., Inglehearn C.F., Toomes C., Ali M.;
RT "Next generation sequencing identifies mutations in Atonal homolog 7
RT (ATOH7) in families with global eye developmental defects.";
RL Hum. Mol. Genet. 21:776-783(2012).
CC -!- FUNCTION: May play a role in the regulation of tight junction
CC formation. Binds phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2).
CC {ECO:0000269|PubMed:19706687}.
CC -!- SUBUNIT: Interacts (via the PDZ 2 domain) with CTNND2 (via the extreme
CC C-terminus). Interacts (via the PDZ 2 domain) with PKP4 (via the
CC extreme C-terminus); this interaction directed FRMPD2 to the
CC basolateral membranes. Interacts (via the PDZ 2 domain) with ARVCF (via
CC the extreme C-terminus). {ECO:0000269|PubMed:19706687}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Basolateral cell
CC membrane {ECO:0000269|PubMed:19706687}. Cell junction, tight junction
CC {ECO:0000269|PubMed:19706687}. Note=Colocalizes with CTNNB1, CDH1 and
CC PKP4 at the basolateral membrane. Colocalizes with TJP1 at tight
CC junctions. Its recruitment to cell-cell contacts requires CDH1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q68DX3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q68DX3-2; Sequence=VSP_028523, VSP_028524, VSP_028527;
CC Name=3;
CC IsoId=Q68DX3-3; Sequence=VSP_028525, VSP_028526;
CC Name=4;
CC IsoId=Q68DX3-4; Sequence=VSP_028522, VSP_028528;
CC Name=5;
CC IsoId=Q68DX3-5; Sequence=VSP_028521;
CC -!- TISSUE SPECIFICITY: Expressed in epithelial cells.
CC {ECO:0000269|PubMed:19706687}.
CC -!- DOMAIN: The FERM and PDZ 2 domains are necessary for localization to
CC the basolateral cell membrane. The FERM domain binds to
CC phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) and is sufficient
CC for membrane localization.
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DR EMBL; AY491519; AAS79660.1; -; mRNA.
DR EMBL; AK123038; BAC85520.1; -; mRNA.
DR EMBL; AK131386; BAD18537.1; -; mRNA.
DR EMBL; CR749241; CAH18097.1; -; mRNA.
DR EMBL; AC013284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC074325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031614; AAH31614.1; -; mRNA.
DR EMBL; BC073954; AAH73954.1; -; mRNA.
DR EMBL; BC144635; AAI44636.1; -; mRNA.
DR EMBL; BC144639; AAI44640.1; -; mRNA.
DR CCDS; CCDS31195.1; -. [Q68DX3-1]
DR CCDS; CCDS81460.1; -. [Q68DX3-2]
DR RefSeq; NP_001018081.3; NM_001018071.3. [Q68DX3-1]
DR RefSeq; NP_001035977.2; NM_001042512.2. [Q68DX3-4]
DR RefSeq; NP_001305120.1; NM_001318191.1.
DR RefSeq; XP_016871233.1; XM_017015744.1. [Q68DX3-5]
DR AlphaFoldDB; Q68DX3; -.
DR SMR; Q68DX3; -.
DR BioGRID; 126788; 17.
DR IntAct; Q68DX3; 2.
DR STRING; 9606.ENSP00000363317; -.
DR iPTMnet; Q68DX3; -.
DR PhosphoSitePlus; Q68DX3; -.
DR BioMuta; FRMPD2; -.
DR DMDM; 334302902; -.
DR jPOST; Q68DX3; -.
DR MassIVE; Q68DX3; -.
DR PaxDb; Q68DX3; -.
DR PeptideAtlas; Q68DX3; -.
DR PRIDE; Q68DX3; -.
DR ProteomicsDB; 66110; -. [Q68DX3-1]
DR ProteomicsDB; 66111; -. [Q68DX3-2]
DR ProteomicsDB; 66112; -. [Q68DX3-3]
DR Antibodypedia; 13728; 62 antibodies from 20 providers.
DR DNASU; 143162; -.
DR Ensembl; ENST00000305531.3; ENSP00000307079.3; ENSG00000170324.21. [Q68DX3-2]
DR Ensembl; ENST00000374201.8; ENSP00000363317.3; ENSG00000170324.21. [Q68DX3-1]
DR GeneID; 143162; -.
DR KEGG; hsa:143162; -.
DR MANE-Select; ENST00000374201.8; ENSP00000363317.3; NM_001018071.4; NP_001018081.4.
DR UCSC; uc001jgg.5; human. [Q68DX3-1]
DR CTD; 143162; -.
DR DisGeNET; 143162; -.
DR GeneCards; FRMPD2; -.
DR HGNC; HGNC:28572; FRMPD2.
DR HPA; ENSG00000170324; Tissue enriched (retina).
DR MIM; 613323; gene.
DR neXtProt; NX_Q68DX3; -.
DR OpenTargets; ENSG00000170324; -.
DR PharmGKB; PA134947461; -.
DR VEuPathDB; HostDB:ENSG00000170324; -.
DR eggNOG; KOG0792; Eukaryota.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00940000161964; -.
DR HOGENOM; CLU_079375_0_0_1; -.
DR InParanoid; Q68DX3; -.
DR OMA; CEDQPSR; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; Q68DX3; -.
DR TreeFam; TF315388; -.
DR PathwayCommons; Q68DX3; -.
DR SignaLink; Q68DX3; -.
DR BioGRID-ORCS; 143162; 10 hits in 1069 CRISPR screens.
DR ChiTaRS; FRMPD2; human.
DR GenomeRNAi; 143162; -.
DR Pharos; Q68DX3; Tbio.
DR PRO; PR:Q68DX3; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q68DX3; protein.
DR Bgee; ENSG00000170324; Expressed in superior frontal gyrus and 95 other tissues.
DR ExpressionAtlas; Q68DX3; baseline and differential.
DR Genevisible; Q68DX3; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0070830; P:bicellular tight junction assembly; IMP:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 3.
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; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR029906; FRMPD2.
DR InterPro; IPR011019; KIND_dom.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR19964:SF56; PTHR19964:SF56; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF00595; PDZ; 3.
DR PRINTS; PR00935; BAND41.
DR SMART; SM00295; B41; 1.
DR SMART; SM01196; FERM_C; 1.
DR SMART; SM00750; KIND; 1.
DR SMART; SM00228; PDZ; 3.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF50156; SSF50156; 3.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS51377; KIND; 1.
DR PROSITE; PS50106; PDZ; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Cytoplasm; Membrane;
KW Reference proteome; Repeat; Tight junction.
FT CHAIN 1..1309
FT /note="FERM and PDZ domain-containing protein 2"
FT /id="PRO_0000306854"
FT DOMAIN 15..197
FT /note="KIND"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00709"
FT DOMAIN 342..642
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 775..861
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 950..1035
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1079..1167
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 214..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1204..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..1048
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_028521"
FT VAR_SEQ 1..989
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028522"
FT VAR_SEQ 1..8
FT /note="MQPLTKDA -> MHVFIV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028523"
FT VAR_SEQ 103..124
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028524"
FT VAR_SEQ 391..392
FT /note="KE -> GE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028525"
FT VAR_SEQ 393..1309
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028526"
FT VAR_SEQ 486
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028527"
FT VAR_SEQ 990..996
FT /note="KEGQILQ -> MTSIPFP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028528"
FT VARIANT 20
FT /note="A -> T (in dbSNP:rs11101272)"
FT /id="VAR_055540"
FT VARIANT 239
FT /note="T -> M (in dbSNP:rs55802136)"
FT /id="VAR_061034"
FT VARIANT 351
FT /note="G -> R (in dbSNP:rs116143480)"
FT /evidence="ECO:0000269|PubMed:22068589"
FT /id="VAR_072402"
FT VARIANT 534
FT /note="K -> E (in dbSNP:rs1864345)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_055541"
FT VARIANT 727
FT /note="R -> W (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs115907611)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035446"
FT VARIANT 1021
FT /note="T -> K (in dbSNP:rs1898784)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_065253"
FT MUTAGEN 955
FT /note="K->E: Abolishes the basolateral membrane
FT localization."
FT /evidence="ECO:0000269|PubMed:19706687"
FT CONFLICT 601
FT /note="K -> E (in Ref. 3; CAH18097)"
FT /evidence="ECO:0000305"
FT CONFLICT 624
FT /note="S -> G (in Ref. 3; CAH18097)"
FT /evidence="ECO:0000305"
FT CONFLICT 826
FT /note="I -> T (in Ref. 3; CAH18097)"
FT /evidence="ECO:0000305"
FT CONFLICT 874
FT /note="S -> G (in Ref. 2; BAC85520)"
FT /evidence="ECO:0000305"
FT CONFLICT 895
FT /note="L -> S (in Ref. 2; BAC85520)"
FT /evidence="ECO:0000305"
FT CONFLICT 969
FT /note="N -> M (in Ref. 5; AAH73954/AAI44636/AAI44640)"
FT /evidence="ECO:0000305"
FT CONFLICT 1077
FT /note="K -> N (in Ref. 1; AAS79660)"
FT /evidence="ECO:0000305"
FT CONFLICT 1174
FT /note="L -> M (in Ref. 2; BAC85520)"
FT /evidence="ECO:0000305"
FT CONFLICT 1214
FT /note="S -> F (in Ref. 1; AAS79660)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1309 AA; 144282 MW; 7684E687FA8522B4 CRC64;
MQPLTKDAGM SLSSVTLASA LQVRGEALSE EEIWSLLFLA AEQLLEDLRN DSSDYVVCPW
SALLSAAGSL SFQGRVSHIE AAPFKAPELL QGQSEDEQPD ASQMHVYSLG MTLYWSAGFH
VPPHQPLQLC EPLHSILLTM CEDQPHRRCT LQSVLEACRV HEKEVSVYPA PAGLHIRRLV
GLVLGTISEV EKRVVEESSS VQQNRSYLLR KRLRGTSSES PAAQAPECLH PCRVSERSTE
TQSSPEPHWS TLTHSHCSLL VNRALPGADP QDQQAGRRLS SGSVHSAADS SWPTTPSQRG
FLQRRSKFSR PEFILLAGEA PMTLHLPGSV VTKKGKSYLA LRDLCVVLLN GQHLEVKCDV
ESTVGAVFNA VTSFANLEEL TYFGLAYMKS KEFFFLDSET RLCKIAPEGW REQPQKTSMN
TFTLFLRIKF FVSHYGLLQH SLTRHQFYLQ LRKDILEERL YCNEEILLQL GVLALQAEFG
NYPKEQVESK PYFHVEDYIP ASLIERMTAL RVQVEVSEMH RLSSALWGED AELKFLRVTQ
QLPEYGVLVH QVFSEKRRPE EEMALGICAK GVIVYEVKNN SRIAMLRFQW RETGKISTYQ
KKFTITSSVT GKKHTFVTDS AKTSKYLLDL CSAQHGFNAQ MGSGQPSHVL FDHDKFVQMA
NLSPAHQARS KPLIWIQRLS CSENELFVSR LQGAAGGLLS TSMDNFNVDG SKEAGAEGIG
RSPCTGREQL KSACVIQKPM TWDSLSGPPV QSMHAGSKNN RRKSFIAEPG REIVRVTLKR
DPHRGFGFVI NEGEYSGQAD PGIFISSIIP GGPAEKAKTI KPGGQILALN HISLEGFTFN
MAVRMIQNSP DNIELIISQS KGVGGNNPDE EKNSTANSGV SSTDILSFGY QGSLLSHTQD
QDRNTEELDM AGVQSLVPRL RHQLSFLPLK GAGSSCPPSP PEISAGEIYF VELVKEDGTL
GFSVTGGINT SVPYGGIYVK SIVPGGPAAK EGQILQGDRL LQVDGVILCG LTHKQAVQCL
TGPGQVARLV LERRVPRSTQ QCPSANDSMG DERTAVSLVT ALPGRPSSCV SVTDGPKFEV
KLKKNANGLG FSFVQMEKES CSHLKSDLVR IKRLFPGQPA EENGAIAAGD IILAVNGRST
EGLIFQEVLH LLRGAPQEVT LLLCRPPPGA LPELEQEWQT PELSADKEFT RATCTDSCTS
PILDQEDSWR DSASPDAGEG LGLRPESSQK AIREAQWGQN RERPWASSLT HSPESHPHLC
KLHQERDEST LATSLEKDVR QNCYSVCDIM RLGRYSFSSP LTRLSTDIF
