LIPA3_HUMAN
ID LIPA3_HUMAN Reviewed; 1194 AA.
AC O75145; A8K142; Q3MJA0; Q9H8B5; Q9UEW4;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Liprin-alpha-3;
DE AltName: Full=Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-3;
DE Short=PTPRF-interacting protein alpha-3;
GN Name=PPFIA3; Synonyms=KIAA0654;
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=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 152-1194 (ISOFORM 2), AND VARIANT SER-563.
RC TISSUE=Brain;
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], AND VARIANT SER-563.
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 909-1194 (ISOFORM 2), AND VARIANT SER-563.
RC TISSUE=Brain, and Muscle;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 752-1194 (ISOFORM 1), TISSUE SPECIFICITY,
RP FUNCTION, INTERACTION WITH PTPRD; PTPRF AND PTPRS, OLIGOMERIZATION, AND
RP DOMAIN.
RX PubMed=9624153; DOI=10.1074/jbc.273.25.15611;
RA Serra-Pages C., Medley Q.G., Tang M., Hart A., Streuli M.;
RT "Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-
RT interacting proteins.";
RL J. Biol. Chem. 273:15611-15620(1998).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-207 AND THR-714, AND
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23124857; DOI=10.1007/s00418-012-1044-y;
RA Joshi C.S., Suryawanshi A.R., Khan S.A., Balasinor N.H., Khole V.V.;
RT "Liprin alpha3: a putative estrogen regulated acrosomal protein.";
RL Histochem. Cell Biol. 139:535-548(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-142; SER-683; THR-714
RP AND SER-1164, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: May regulate the disassembly of focal adhesions. May localize
CC receptor-like tyrosine phosphatases type 2A at specific sites on the
CC plasma membrane, possibly regulating their interaction with the
CC extracellular environment and their association with substrates.
CC {ECO:0000269|PubMed:9624153}.
CC -!- SUBUNIT: Forms homodimers and heterodimers with liprins-alpha and
CC liprins-beta (PubMed:9624153). Interacts with the second PTPase domain
CC of PTPRD, PTPRF and PTPRS (PubMed:9624153). Binds RIMS1, RIMS2, RIMS3
CC and RIMS4 (By similarity). {ECO:0000250|UniProtKB:Q91Z79,
CC ECO:0000269|PubMed:9624153}.
CC -!- INTERACTION:
CC O75145; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-1763225, EBI-11524851;
CC O75145; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-1763225, EBI-11988027;
CC O75145; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-1763225, EBI-1105153;
CC O75145; O60504: SORBS3; NbExp=3; IntAct=EBI-1763225, EBI-741237;
CC O75145; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-1763225, EBI-1105213;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q91Z79}.
CC Cytoplasmic vesicle, secretory vesicle, acrosome
CC {ECO:0000269|PubMed:23124857}. Note=Also detected in epididymosome.
CC {ECO:0000250|UniProtKB:Q91Z79}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75145-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75145-2; Sequence=VSP_009392;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain (PubMed:9624153).
CC Also detected in sperm (at protein level) (PubMed:23124857).
CC {ECO:0000269|PubMed:23124857, ECO:0000269|PubMed:9624153}.
CC -!- DOMAIN: The N-terminal coiled coil regions mediate homodimerization
CC preferentially and heterodimerization type alpha/alpha. The C-terminal,
CC non-coiled coil regions mediate heterodimerization type alpha/beta and
CC interaction with PTPRD, PTPRF and PTPRS. {ECO:0000269|PubMed:9624153}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to exon skipping. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the liprin family. Liprin-alpha subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31629.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB014554; BAA31629.2; ALT_INIT; mRNA.
DR EMBL; AK023850; BAB14702.1; -; mRNA.
DR EMBL; AK025972; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK289757; BAF82446.1; -; mRNA.
DR EMBL; CH471177; EAW52457.1; -; Genomic_DNA.
DR EMBL; BC021255; AAH21255.2; -; mRNA.
DR EMBL; BC101518; AAI01519.1; -; mRNA.
DR EMBL; BC101520; AAI01521.1; -; mRNA.
DR EMBL; AF034800; AAC26101.1; -; mRNA.
DR CCDS; CCDS12758.1; -. [O75145-1]
DR RefSeq; NP_003651.1; NM_003660.3. [O75145-1]
DR RefSeq; XP_016882896.1; XM_017027407.1. [O75145-2]
DR AlphaFoldDB; O75145; -.
DR SMR; O75145; -.
DR BioGRID; 114111; 40.
DR IntAct; O75145; 14.
DR MINT; O75145; -.
DR STRING; 9606.ENSP00000335614; -.
DR GlyGen; O75145; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75145; -.
DR PhosphoSitePlus; O75145; -.
DR BioMuta; PPFIA3; -.
DR EPD; O75145; -.
DR jPOST; O75145; -.
DR MassIVE; O75145; -.
DR MaxQB; O75145; -.
DR PaxDb; O75145; -.
DR PeptideAtlas; O75145; -.
DR PRIDE; O75145; -.
DR ProteomicsDB; 49808; -. [O75145-1]
DR ProteomicsDB; 49809; -. [O75145-2]
DR Antibodypedia; 31915; 72 antibodies from 23 providers.
DR DNASU; 8541; -.
DR Ensembl; ENST00000334186.9; ENSP00000335614.3; ENSG00000177380.14. [O75145-1]
DR Ensembl; ENST00000602351.5; ENSP00000473622.1; ENSG00000177380.14. [O75145-2]
DR GeneID; 8541; -.
DR KEGG; hsa:8541; -.
DR MANE-Select; ENST00000334186.9; ENSP00000335614.3; NM_003660.4; NP_003651.1.
DR UCSC; uc002pmr.5; human. [O75145-1]
DR CTD; 8541; -.
DR DisGeNET; 8541; -.
DR GeneCards; PPFIA3; -.
DR HGNC; HGNC:9247; PPFIA3.
DR HPA; ENSG00000177380; Tissue enhanced (brain, pituitary gland, skin).
DR MIM; 603144; gene.
DR neXtProt; NX_O75145; -.
DR OpenTargets; ENSG00000177380; -.
DR PharmGKB; PA33568; -.
DR VEuPathDB; HostDB:ENSG00000177380; -.
DR eggNOG; KOG0249; Eukaryota.
DR GeneTree; ENSGT01050000244900; -.
DR HOGENOM; CLU_006923_0_0_1; -.
DR InParanoid; O75145; -.
DR OMA; LMMMCEV; -.
DR OrthoDB; 440941at2759; -.
DR PhylomeDB; O75145; -.
DR TreeFam; TF314207; -.
DR PathwayCommons; O75145; -.
DR Reactome; R-HSA-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-HSA-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-HSA-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-HSA-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-HSA-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-HSA-388844; Receptor-type tyrosine-protein phosphatases.
DR SignaLink; O75145; -.
DR BioGRID-ORCS; 8541; 13 hits in 1081 CRISPR screens.
DR ChiTaRS; PPFIA3; human.
DR GenomeRNAi; 8541; -.
DR Pharos; O75145; Tbio.
DR PRO; PR:O75145; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O75145; protein.
DR Bgee; ENSG00000177380; Expressed in right hemisphere of cerebellum and 122 other tissues.
DR ExpressionAtlas; O75145; baseline and differential.
DR Genevisible; O75145; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0098875; C:epididymosome; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IEA:Ensembl.
DR GO; GO:0007269; P:neurotransmitter secretion; ISS:ParkinsonsUK-UCL.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; ISS:ParkinsonsUK-UCL.
DR GO; GO:0050808; P:synapse organization; IBA:GO_Central.
DR GO; GO:0016081; P:synaptic vesicle docking; IEA:Ensembl.
DR CDD; cd09562; SAM_liprin-alpha1_2_3_4_repeat1; 1.
DR CDD; cd09565; SAM_liprin-alpha1_2_3_4_repeat2; 1.
DR CDD; cd09568; SAM_liprin-alpha1_2_3_4_repeat3; 1.
DR Gene3D; 1.10.150.50; -; 3.
DR InterPro; IPR029515; Liprin.
DR InterPro; IPR037620; Liprin-alpha_SAM_rpt_1.
DR InterPro; IPR037621; Liprin-alpha_SAM_rpt_2.
DR InterPro; IPR037622; Liprin-alpha_SAM_rpt_3.
DR InterPro; IPR030440; PPFIA3.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR12587; PTHR12587; 1.
DR PANTHER; PTHR12587:SF4; PTHR12587:SF4; 1.
DR Pfam; PF00536; SAM_1; 2.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00454; SAM; 3.
DR SUPFAM; SSF47769; SSF47769; 3.
DR PROSITE; PS50105; SAM_DOMAIN; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1194
FT /note="Liprin-alpha-3"
FT /id="PRO_0000191029"
FT DOMAIN 838..904
FT /note="SAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 953..1017
FT /note="SAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 1041..1110
FT /note="SAM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 26..133
FT /evidence="ECO:0000255"
FT COILED 161..501
FT /evidence="ECO:0000255"
FT COILED 596..644
FT /evidence="ECO:0000255"
FT COILED 1014..1040
FT /evidence="ECO:0000255"
FT COMPBIAS 544..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13136"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60469"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13136"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60469"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13136"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 714
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13136"
FT MOD_RES 792
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q91Z79"
FT MOD_RES 794
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91Z79"
FT MOD_RES 1123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13136"
FT MOD_RES 1164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 937..945
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_009392"
FT VARIANT 563
FT /note="A -> S (in dbSNP:rs2303053)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4"
FT /id="VAR_017757"
FT CONFLICT 878
FT /note="E -> K (in Ref. 6; AAC26101)"
FT /evidence="ECO:0000305"
FT CONFLICT 1011
FT /note="I -> V (in Ref. 6; AAC26101)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1194 AA; 133496 MW; 4DD92531AD8AE12D CRC64;
MMCEVMPTIS EDGRRGSALG PDEAGGELER LMVTMLTERE RLLETLREAQ DGLATAQLRL
RELGHEKDSL QRQLSIALPQ EFAALTKELN LCREQLLERE EEIAELKAER NNTRLLLEHL
ECLVSRHERS LRMTVVKRQA QSPGGVSSEV EVLKALKSLF EHHKALDEKV RERLRMALER
VAVLEEELEL SNQETLNLRE QLSRRRSGLE EPGKDGDGQT LANGLGPGGD SNRRTAELEE
ALERQRAEVC QLRERLAVLC RQMSQLEEEL GTAHRELGKA EEANSKLQRD LKEALAQRED
MEERITTLEK RYLSAQREAT SLHDANDKLE NELASKESLY RQSEEKSRQL AEWLDDAKQK
LQQTLQKAET LPEIEAQLAQ RVAALNKAEE RHGNFEERLR QLEAQLEEKN QELQRARQRE
KMNDDHNKRL SETVDKLLSE SNERLQLHLK ERMGALEEKN SLSEEIANMK KLQDELLLNK
EQLLAEMERM QMEIDQLRGR PPSSYSRSLP GSALELRYSQ APTLPSGAHL DPYVAGSGRA
GKRGRWSGVK EEPSKDWERS APAGSIPPPF PGELDGSDEE EAEGMFGAEL LSPSGQADVQ
TLAIMLQEQL EAINKEIKLI QEEKETTEQR AEELESRVSS SGLDSLGRYR SSCSLPPSLT
TSTLASPSPP SSGHSTPRLA PPSPAREGTD KANHVPKEEA GAPRGEGPAI PGDTPPPTPR
SARLERMTQA LALQAGSLED GGPPRGSEGT PDSLHKAPKK KSIKSSIGRL FGKKEKGRMG
PPGRDSSSLA GTPSDETLAT DPLGLAKLTG PGDKDRRNKR KHELLEEACR QGLPFAAWDG
PTVVSWLELW VGMPAWYVAA CRANVKSGAI MANLSDTEIQ REIGISNPLH RLKLRLAIQE
MVSLTSPSAP ASSRTSTGNV WMTHEEMESL TATTKPETKE ISWEQILAYG DMNHEWVGND
WLPSLGLPQY RSYFMESLVD ARMLDHLNKK ELRGQLKMVD SFHRVSLHYG IMCLKRLNYD
RKDLERRREE SQTQIRDVMV WSNERVMGWV SGLGLKEFAT NLTESGVHGA LLALDETFDY
SDLALLLQIP TQNAQARQLL EKEFSNLISL GTDRRLDEDS AKSFSRSPSW RKMFREKDLR
GVTPDSAEML PPNFRSAAAG ALGSPGLPLR KLQPEGQTSG SSRADGVSVR TYSC
