DDHD1_HUMAN
ID DDHD1_HUMAN Reviewed; 900 AA.
AC Q8NEL9; G5E9D1; Q8WVH3; Q96LL2; Q9C0F8;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Phospholipase DDHD1 {ECO:0000305};
DE EC=3.1.1.-;
DE AltName: Full=DDHD domain-containing protein 1;
DE AltName: Full=Phosphatidic acid-preferring phospholipase A1 homolog;
DE Short=PA-PLA1;
GN Name=DDHD1 {ECO:0000312|HGNC:HGNC:19714}; Synonyms=KIAA1705;
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 3).
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 357-900 (ISOFORMS 2/4).
RC TISSUE=Fetal brain, and 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 GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Testis;
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 TISSUE SPECIFICITY.
RX PubMed=9488669; DOI=10.1074/jbc.273.10.5468;
RA Higgs H.N., Han M.H., Johnson G.E., Glomset J.A.;
RT "Cloning of a phosphatidic acid-preferring phospholipase A1 from bovine
RT testis.";
RL J. Biol. Chem. 273:5468-5477(1998).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=15623529; DOI=10.1074/jbc.m409673200;
RA Shimoi W., Ezawa I., Nakamoto K., Uesaki S., Gabreski G., Aridor M.,
RA Yamamoto A., Nagahama M., Tagaya M., Tani K.;
RT "p125 is localized in endoplasmic reticulum exit sites and involved in
RT their organization.";
RL J. Biol. Chem. 280:10141-10148(2005).
RN [8]
RP FUNCTION, AND INTERACTION WITH SEC23A AND SEC24C.
RX PubMed=17428803; DOI=10.1074/jbc.m611237200;
RA Iinuma T., Shiga A., Nakamoto K., O'Brien M.B., Aridor M., Arimitsu N.,
RA Tagaya M., Tani K.;
RT "Mammalian Sec16/p250 plays a role in membrane traffic from the endoplasmic
RT reticulum.";
RL J. Biol. Chem. 282:17632-17639(2007).
RN [9]
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 [10]
RP INVOLVEMENT IN SPG28.
RX PubMed=23176821; DOI=10.1016/j.ajhg.2012.11.001;
RA Tesson C., Nawara M., Salih M.A., Rossignol R., Zaki M.S., Al Balwi M.,
RA Schule R., Mignot C., Obre E., Bouhouche A., Santorelli F.M., Durand C.M.,
RA Oteyza A.C., El-Hachimi K.H., Al Drees A., Bouslam N., Lamari F.,
RA Elmalik S.A., Kabiraj M.M., Seidahmed M.Z., Esteves T., Gaussen M.,
RA Monin M.L., Gyapay G., Lechner D., Gonzalez M., Depienne C., Mochel F.,
RA Lavie J., Schols L., Lacombe D., Yahyaoui M., Al Abdulkareem I.,
RA Zuchner S., Yamashita A., Benomar A., Goizet C., Durr A., Gleeson J.G.,
RA Darios F., Brice A., Stevanin G.;
RT "Alteration of fatty-acid-metabolizing enzymes affects mitochondrial form
RT and function in hereditary spastic paraplegia.";
RL Am. J. Hum. Genet. 91:1051-1064(2012).
RN [11]
RP FUNCTION, SUBUNIT, HOMOOLIGOMER FORMATION, INTERACTION WITH DDHD2,
RP MUTAGENESIS OF LEU-590; ILE-593; ASP-662; ASP-848; HIS-867 AND ASP-875, AND
RP CATALYTIC ACTIVITY.
RX PubMed=22922100; DOI=10.1016/j.bbamcr.2012.02.002;
RA Inoue H., Baba T., Sato S., Ohtsuki R., Takemori A., Watanabe T.,
RA Tagaya M., Tani K.;
RT "Roles of SAM and DDHD domains in mammalian intracellular phospholipase A1
RT KIAA0725p.";
RL Biochim. Biophys. Acta 1823:930-939(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-11, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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: Phospholipase that hydrolyzes phosphatidic acid, including
CC 1,2-dioleoyl-sn-phosphatidic acid. The different isoforms may change
CC the substrate specificity (PubMed:22922100). Required for the
CC organization of the endoplasmic reticulum exit sites (ERES), also known
CC as transitional endoplasmic reticulum (tER) (PubMed:17428803).
CC {ECO:0000269|PubMed:17428803, ECO:0000269|PubMed:22922100}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = (9Z)-
CC octadecenoate + 2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+);
CC Xref=Rhea:RHEA:45128, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:74546, ChEBI:CHEBI:77593;
CC Evidence={ECO:0000269|PubMed:22922100};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45129;
CC Evidence={ECO:0000305|PubMed:22922100};
CC -!- SUBUNIT: Forms homooligomers and, to a much smaller extent,
CC heterooligomers with DDHD2 (PubMed:22922100). Interacts with SEC23A and
CC SEC24C (PubMed:17428803). {ECO:0000269|PubMed:17428803,
CC ECO:0000269|PubMed:22922100}.
CC -!- INTERACTION:
CC Q8NEL9-2; Q2VPA4: CR1L; NbExp=3; IntAct=EBI-11062258, EBI-12330477;
CC Q8NEL9-2; O43167: ZBTB24; NbExp=3; IntAct=EBI-11062258, EBI-744471;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15623529}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8NEL9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NEL9-2; Sequence=VSP_008629;
CC Name=3;
CC IsoId=Q8NEL9-3; Sequence=VSP_008628, VSP_008629;
CC Name=4;
CC IsoId=Q8NEL9-4; Sequence=VSP_045340, VSP_008629;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis. Also expressed in
CC brain, spleen and lung. Only expressed in cerebellum in fetal brain.
CC {ECO:0000269|PubMed:9488669}.
CC -!- DISEASE: Spastic paraplegia 28, autosomal recessive (SPG28)
CC [MIM:609340]: A form of spastic paraplegia, a neurodegenerative
CC disorder characterized by a slow, gradual, progressive weakness and
CC spasticity of the lower limbs. Rate of progression and the severity of
CC symptoms are quite variable. Initial symptoms may include difficulty
CC with balance, weakness and stiffness in the legs, muscle spasms, and
CC dragging the toes when walking. In some forms of the disorder, bladder
CC symptoms (such as incontinence) may appear, or the weakness and
CC stiffness may spread to other parts of the body. Some SPG28 patients
CC also have distal sensory impairment. {ECO:0000269|PubMed:23176821}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the PA-PLA1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB21796.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB71679.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB051492; BAB21796.1; ALT_INIT; mRNA.
DR EMBL; AK058137; BAB71679.1; ALT_INIT; mRNA.
DR EMBL; AK125372; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL352979; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW80623.1; -; Genomic_DNA.
DR EMBL; BC018014; AAH18014.1; -; mRNA.
DR EMBL; BC030703; AAH30703.1; -; mRNA.
DR CCDS; CCDS53895.1; -. [Q8NEL9-1]
DR CCDS; CCDS53896.1; -. [Q8NEL9-4]
DR CCDS; CCDS9714.1; -. [Q8NEL9-2]
DR RefSeq; NP_001153619.1; NM_001160147.1. [Q8NEL9-4]
DR RefSeq; NP_001153620.1; NM_001160148.1. [Q8NEL9-1]
DR RefSeq; NP_085140.2; NM_030637.2. [Q8NEL9-2]
DR AlphaFoldDB; Q8NEL9; -.
DR BioGRID; 123318; 34.
DR IntAct; Q8NEL9; 9.
DR STRING; 9606.ENSP00000327104; -.
DR SwissLipids; SLP:000001079; -. [Q8NEL9-2]
DR GlyGen; Q8NEL9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NEL9; -.
DR PhosphoSitePlus; Q8NEL9; -.
DR BioMuta; DDHD1; -.
DR DMDM; 37999716; -.
DR EPD; Q8NEL9; -.
DR jPOST; Q8NEL9; -.
DR MassIVE; Q8NEL9; -.
DR MaxQB; Q8NEL9; -.
DR PaxDb; Q8NEL9; -.
DR PeptideAtlas; Q8NEL9; -.
DR PRIDE; Q8NEL9; -.
DR ProteomicsDB; 33905; -.
DR ProteomicsDB; 73175; -. [Q8NEL9-1]
DR ProteomicsDB; 73176; -. [Q8NEL9-2]
DR ProteomicsDB; 73177; -. [Q8NEL9-3]
DR Antibodypedia; 23915; 41 antibodies from 9 providers.
DR DNASU; 80821; -.
DR Ensembl; ENST00000357758.3; ENSP00000350401.3; ENSG00000100523.16. [Q8NEL9-2]
DR Ensembl; ENST00000395606.5; ENSP00000378970.1; ENSG00000100523.16. [Q8NEL9-4]
DR Ensembl; ENST00000673822.2; ENSP00000500986.2; ENSG00000100523.16. [Q8NEL9-1]
DR GeneID; 80821; -.
DR KEGG; hsa:80821; -.
DR MANE-Select; ENST00000673822.2; ENSP00000500986.2; NM_001160148.2; NP_001153620.1.
DR UCSC; uc001xah.4; human. [Q8NEL9-1]
DR CTD; 80821; -.
DR DisGeNET; 80821; -.
DR GeneCards; DDHD1; -.
DR HGNC; HGNC:19714; DDHD1.
DR HPA; ENSG00000100523; Tissue enhanced (testis).
DR MalaCards; DDHD1; -.
DR MIM; 609340; phenotype.
DR MIM; 614603; gene.
DR neXtProt; NX_Q8NEL9; -.
DR OpenTargets; ENSG00000100523; -.
DR Orphanet; 101008; Autosomal recessive spastic paraplegia type 28.
DR PharmGKB; PA134861440; -.
DR VEuPathDB; HostDB:ENSG00000100523; -.
DR eggNOG; KOG2308; Eukaryota.
DR GeneTree; ENSGT00940000156065; -.
DR InParanoid; Q8NEL9; -.
DR OMA; WQNENIV; -.
DR OrthoDB; 777968at2759; -.
DR PhylomeDB; Q8NEL9; -.
DR TreeFam; TF314133; -.
DR BioCyc; MetaCyc:ENSG00000100523-MON; -.
DR BRENDA; 3.1.1.118; 2681.
DR BRENDA; 3.1.1.32; 2681.
DR PathwayCommons; Q8NEL9; -.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR SignaLink; Q8NEL9; -.
DR SIGNOR; Q8NEL9; -.
DR BioGRID-ORCS; 80821; 17 hits in 1077 CRISPR screens.
DR ChiTaRS; DDHD1; human.
DR GenomeRNAi; 80821; -.
DR Pharos; Q8NEL9; Tbio.
DR PRO; PR:Q8NEL9; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q8NEL9; protein.
DR Bgee; ENSG00000100523; Expressed in sperm and 187 other tissues.
DR ExpressionAtlas; Q8NEL9; baseline and differential.
DR Genevisible; Q8NEL9; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IDA:MGI.
DR InterPro; IPR004177; DDHD_dom.
DR Pfam; PF02862; DDHD; 1.
DR SMART; SM01127; DDHD; 1.
DR PROSITE; PS51043; DDHD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Hereditary spastic paraplegia; Hydrolase;
KW Lipid degradation; Lipid metabolism; Neurodegeneration; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..900
FT /note="Phospholipase DDHD1"
FT /id="PRO_0000079845"
FT DOMAIN 611..886
FT /note="DDHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00378"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..152
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 706..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 537
FT /evidence="ECO:0000250"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80YA3"
FT VAR_SEQ 1..418
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11214970,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_008628"
FT VAR_SEQ 337
FT /note="D -> DGSGINYS (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_045340"
FT VAR_SEQ 813..841
FT /note="YFRLQESFFNLPQLLFPENVMQNKDNALV -> L (in isoform 2,
FT isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11214970,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_008629"
FT MUTAGEN 590
FT /note="L->S: No effect on homooligomer formation; when
FT associated with S-593."
FT /evidence="ECO:0000269|PubMed:22922100"
FT MUTAGEN 593
FT /note="I->S: No effect on homooligomer formation; when
FT associated with S-590."
FT /evidence="ECO:0000269|PubMed:22922100"
FT MUTAGEN 662
FT /note="D->A: Markedly decreased enzymatic activity."
FT /evidence="ECO:0000269|PubMed:22922100"
FT MUTAGEN 848
FT /note="D->A: Markedly decreased enzymatic activity."
FT /evidence="ECO:0000269|PubMed:22922100"
FT MUTAGEN 867
FT /note="H->A: Markedly decreased enzymatic activity."
FT /evidence="ECO:0000269|PubMed:22922100"
FT MUTAGEN 875
FT /note="D->A: No effect on enzymatic activity."
FT /evidence="ECO:0000269|PubMed:22922100"
FT CONFLICT 109
FT /note="G -> GGG (in Ref. 2; AK125372)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="H -> R (in Ref. 5; AAH30703)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 900 AA; 100435 MW; D70DAD1A73AC22B8 CRC64;
MNYPGRGSPR SPEHNGRGGG GGAWELGSDA RPAFGGGVCC FEHLPGGDPD DGDVPLALLR
GEPGLHLAPG TDDHNHHLAL DPCLSDENYD FSSAESGSSL RYYSEGESGG GGSSLSLHPP
QQPPLVPTNS GGGGATGGSP GERKRTRLGG PAARHRYEVV TELGPEEVRW FYKEDKKTWK
PFIGYDSLRI ELAFRTLLQT TGARPQGGDR DGDHVCSPTG PASSSGEDDD EDRACGFCQS
TTGHEPEMVE LVNIEPVCVR GGLYEVDVTQ GECYPVYWNQ ADKIPVMRGQ WFIDGTWQPL
EEEESNLIEQ EHLNCFRGQQ MQENFDIEVS KSIDGKDAVH SFKLSRNHVD WHSVDEVYLY
SDATTSKIAR TVTQKLGFSK ASSSGTRLHR GYVEEATLED KPSQTTHIVF VVHGIGQKMD
QGRIIKNTAM MREAARKIEE RHFSNHATHV EFLPVEWRSK LTLDGDTVDS ITPDKVRGLR
DMLNSSAMDI MYYTSPLYRD ELVKGLQQEL NRLYSLFCSR NPDFEEKGGK VSIVSHSLGC
VITYDIMTGW NPVRLYEQLL QKEEELPDER WMSYEERHLL DELYITKRRL KEIEERLHGL
KASSMTQTPA LKFKVENFFC MGSPLAVFLA LRGIRPGNTG SQDHILPREI CNRLLNIFHP
TDPVAYRLEP LILKHYSNIS PVQIHWYNTS NPLPYEHMKP SFLNPAKEPT SVSENEGIST
IPSPVTSPVL SRRHYGESIT NIGKASILGA ASIGKGLGGM LFSRFGRSST TQSSETSKDS
MEDEKKPVAS PSATTVGTQT LPHSSSGFLD SAYFRLQESF FNLPQLLFPE NVMQNKDNAL
VELDHRIDFE LREGLVESRY WSAVTSHTAY WSSLDVALFL LTFMYKHEHD DDAKPNLDPI
