DLGP1_MOUSE
ID DLGP1_MOUSE Reviewed; 992 AA.
AC Q9D415; Q52KF6; Q5DTK5; Q6P6N4; Q6XBF4; Q8BZL7; Q8BZQ1; Q8C0G0;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Disks large-associated protein 1;
DE Short=DAP-1;
DE AltName: Full=Guanylate kinase-associated protein;
DE AltName: Full=PSD-95/SAP90-binding protein 1;
DE AltName: Full=SAP90/PSD-95-associated protein 1;
DE Short=SAPAP1;
GN Name=Dlgap1; Synonyms=Gkap, Kiaa4162;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
RC STRAIN=ICR;
RX PubMed=15024750; DOI=10.1002/cne.20060;
RA Welch J.M., Wang D., Feng G.;
RT "Differential mRNA expression and protein localization of the SAP90/PSD-95-
RT associated proteins (SAPAPs) in the nervous system of the mouse.";
RL J. Comp. Neurol. 472:24-39(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 660-992 (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 210-992 (ISOFORM 4).
RC STRAIN=C57BL/6J; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; SER-509; SER-516 AND
RP SER-947, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-362; SER-365;
RP SER-368; SER-372; SER-418; SER-421; SER-425; SER-437; SER-509; SER-516;
RP SER-578; THR-579; SER-581; SER-605; THR-606 AND SER-608, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP INTERACTION WITH SHANK3, AND SUBCELLULAR LOCATION.
RX PubMed=24153177; DOI=10.1038/nature12630;
RA Han K., Holder J.L. Jr., Schaaf C.P., Lu H., Chen H., Kang H., Tang J.,
RA Wu Z., Hao S., Cheung S.W., Yu P., Sun H., Breman A.M., Patel A., Lu H.C.,
RA Zoghbi H.Y.;
RT "SHANK3 overexpression causes manic-like behaviour with unique
RT pharmacogenetic properties.";
RL Nature 503:72-77(2013).
CC -!- FUNCTION: Part of the postsynaptic scaffold in neuronal cells.
CC -!- SUBUNIT: Interacts with the guanylate kinase-like domain of DLG1, DLG2,
CC DLG3, DLG4 and AIP1. Interacts with the PDZ domain of SHANK1, SHANK2
CC and SHANK3. Found in a complex with DLG4 and SHANK1, SHANK2 or SHANK3.
CC Found in a complex with DLG4 and BEGAIN. Interacts with DYL2 and LRFN1.
CC Interacts with MPP2 (via the SH3-Guanylate kinase-like sub-module) (By
CC similarity). {ECO:0000250|UniProtKB:P97836,
CC ECO:0000269|PubMed:24153177}.
CC -!- INTERACTION:
CC Q9D415; Q80YA9: Cnksr2; NbExp=3; IntAct=EBI-400152, EBI-771429;
CC Q9D415; P35436: Grin2a; NbExp=2; IntAct=EBI-400152, EBI-400115;
CC Q9D415; Q9Z2Y3: Homer1; NbExp=4; IntAct=EBI-400152, EBI-396980;
CC Q9D415; Q4ACU6: Shank3; NbExp=4; IntAct=EBI-400152, EBI-771450;
CC Q9D415; F6SEU4: Syngap1; NbExp=3; IntAct=EBI-400152, EBI-5797569;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Postsynaptic density {ECO:0000250}. Synapse
CC {ECO:0000269|PubMed:24153177}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=SAPAP1;
CC IsoId=Q9D415-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D415-2; Sequence=VSP_015409;
CC Name=3; Synonyms=GKAP1a;
CC IsoId=Q9D415-3; Sequence=VSP_015412;
CC Name=4; Synonyms=GKAP1b;
CC IsoId=Q9D415-4; Sequence=VSP_015409, VSP_015413, VSP_015414;
CC Name=5;
CC IsoId=Q9D415-5; Sequence=VSP_015410, VSP_015411;
CC Name=6;
CC IsoId=Q9D415-6; Sequence=VSP_015408;
CC -!- TISSUE SPECIFICITY: Highest levels in the neocortex, part of the
CC hippocampus, the granule cell layer of the cerebellum, the glomerular
CC layer of the olfactory bulb, the inner plexiform layer of the retina,
CC the ventral and dorsal horn of the spinal chord, the neuromuscular
CC junction and the submandibular ganglion. {ECO:0000269|PubMed:15024750}.
CC -!- SIMILARITY: Belongs to the SAPAP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90519.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY243846; AAP70755.2; -; mRNA.
DR EMBL; AK031410; BAC27391.1; -; mRNA.
DR EMBL; AK033901; BAC28508.1; -; mRNA.
DR EMBL; AK034182; BAC28619.1; -; mRNA.
DR EMBL; AK220515; BAD90519.1; ALT_INIT; mRNA.
DR EMBL; BC062120; AAH62120.1; -; mRNA.
DR EMBL; BC094369; AAH94369.1; -; mRNA.
DR CCDS; CCDS28953.1; -. [Q9D415-1]
DR CCDS; CCDS84331.1; -. [Q9D415-3]
DR CCDS; CCDS84332.1; -. [Q9D415-2]
DR RefSeq; NP_001334340.1; NM_001347411.1. [Q9D415-3]
DR RefSeq; NP_081988.3; NM_027712.3. [Q9D415-4]
DR RefSeq; NP_808307.2; NM_177639.6. [Q9D415-1]
DR RefSeq; XP_006524236.1; XM_006524173.2. [Q9D415-1]
DR RefSeq; XP_011244709.1; XM_011246407.2. [Q9D415-1]
DR AlphaFoldDB; Q9D415; -.
DR SMR; Q9D415; -.
DR BioGRID; 230347; 165.
DR IntAct; Q9D415; 157.
DR MINT; Q9D415; -.
DR STRING; 10090.ENSMUSP00000122896; -.
DR iPTMnet; Q9D415; -.
DR PhosphoSitePlus; Q9D415; -.
DR MaxQB; Q9D415; -.
DR PaxDb; Q9D415; -.
DR PeptideAtlas; Q9D415; -.
DR PRIDE; Q9D415; -.
DR ProteomicsDB; 279780; -. [Q9D415-1]
DR ProteomicsDB; 279781; -. [Q9D415-2]
DR ProteomicsDB; 279782; -. [Q9D415-3]
DR ProteomicsDB; 279783; -. [Q9D415-4]
DR ProteomicsDB; 279784; -. [Q9D415-5]
DR ProteomicsDB; 279785; -. [Q9D415-6]
DR ABCD; Q9D415; 3 sequenced antibodies.
DR Antibodypedia; 21914; 255 antibodies from 37 providers.
DR DNASU; 224997; -.
DR Ensembl; ENSMUST00000060072; ENSMUSP00000052858; ENSMUSG00000003279. [Q9D415-2]
DR Ensembl; ENSMUST00000133983; ENSMUSP00000116716; ENSMUSG00000003279. [Q9D415-2]
DR Ensembl; ENSMUST00000135938; ENSMUSP00000118497; ENSMUSG00000003279. [Q9D415-3]
DR Ensembl; ENSMUST00000155016; ENSMUSP00000122896; ENSMUSG00000003279. [Q9D415-1]
DR GeneID; 224997; -.
DR KEGG; mmu:224997; -.
DR UCSC; uc008dky.1; mouse. [Q9D415-6]
DR UCSC; uc008dla.1; mouse. [Q9D415-5]
DR UCSC; uc008dle.2; mouse. [Q9D415-1]
DR UCSC; uc008dlf.2; mouse. [Q9D415-4]
DR CTD; 9229; -.
DR MGI; MGI:1346065; Dlgap1.
DR VEuPathDB; HostDB:ENSMUSG00000003279; -.
DR eggNOG; KOG3971; Eukaryota.
DR GeneTree; ENSGT00940000156220; -.
DR HOGENOM; CLU_010880_0_0_1; -.
DR InParanoid; Q9D415; -.
DR OMA; AYMDGGP; -.
DR PhylomeDB; Q9D415; -.
DR TreeFam; TF321382; -.
DR Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR BioGRID-ORCS; 224997; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Dlgap1; mouse.
DR PRO; PR:Q9D415; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9D415; protein.
DR Bgee; ENSMUSG00000003279; Expressed in piriform cortex and 159 other tissues.
DR ExpressionAtlas; Q9D415; baseline and differential.
DR Genevisible; Q9D415; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:BHF-UCL.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0099572; C:postsynaptic specialization; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR GO; GO:0098919; F:structural constituent of postsynaptic density; ISO:MGI.
DR GO; GO:0070842; P:aggresome assembly; ISO:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:MGI.
DR GO; GO:0035418; P:protein localization to synapse; ISO:MGI.
DR GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; ISO:MGI.
DR InterPro; IPR030524; DLGAP1.
DR InterPro; IPR005026; SAPAP.
DR PANTHER; PTHR12353; PTHR12353; 1.
DR PANTHER; PTHR12353:SF7; PTHR12353:SF7; 1.
DR Pfam; PF03359; GKAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Membrane; Phosphoprotein;
KW Reference proteome; Synapse.
FT CHAIN 1..992
FT /note="Disks large-associated protein 1"
FT /id="PRO_0000174289"
FT REGION 150..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..676
FT /note="Interaction with DYL2"
FT /evidence="ECO:0000250"
FT REGION 687..698
FT /note="Interaction with DYL2"
FT /evidence="ECO:0000250"
FT REGION 914..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 990..992
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 174..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..962
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97836"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97836"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 579
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 606
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97836"
FT MOD_RES 947
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT VAR_SEQ 398..992
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015408"
FT VAR_SEQ 537..546
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.3"
FT /id="VSP_015409"
FT VAR_SEQ 538
FT /note="V -> E (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015410"
FT VAR_SEQ 539..992
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015411"
FT VAR_SEQ 547..574
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15024750"
FT /id="VSP_015412"
FT VAR_SEQ 924..944
FT /note="ERRAPPPVPKKPAKGPAPLIR -> VEQCRFCMVHLKPCTNAGQSK (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_015413"
FT VAR_SEQ 945..992
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_015414"
FT CONFLICT 383
FT /note="L -> P (in Ref. 3; BAD90519)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="K -> R (in Ref. 1; AAP70755)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="P -> H (in Ref. 2; BAC27391)"
FT /evidence="ECO:0000305"
FT CONFLICT 752
FT /note="S -> F (in Ref. 2; BAC28619)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 992 AA; 110374 MW; 9962C8B56A33EE13 CRC64;
MKGLSGSRSH HHGITCEAAC DSLSHHSDHK PYLLSPVDHH PADHPYYTQR NSFQAECVGP
FSDPLASSTF PRRHYTSQQE LKDESALVPR TLATKANRLP TNLLDQFERQ LPLSRDGYHT
LQYKRTAVEH RSDSPGRIRH LVHSVQKLFT KSHSLEGPSK GSVNGGKASP DESQTLRYGK
RSKSKERRSE SKARSNASNA SPTSPSWWSS DDNLDGDMCL YHTPSGVMTM GRCPDRSASQ
YFMEAYNTIS EQAVKASRSN NDIKCSTCAN LPVTLDAPLL KKSAWSSTLT VSRAREVYQK
ASVNMDQAMV KSEACQQERS CQYLQVPQDE WSGYTPRGKD DEIPCRRMRS GSYIKAMGDE
DSGDSDTSPK PSPKVAARRE SYLKATQPSL TELTTLKISN EHSPKLQIRS HSYLRAVSEV
SINRSLDSLD PAGLLTSPKF RSRNESYMRA MSTISQVSEM EVNGQFESVC ESVFSELESQ
AVEALDLPLP GCFRMRSHSY VRAIEKGCSQ DDECVSLRSS SPPRTTTTVR TIQSSTGVIK
LSSAVEVSSC ITTYKKTPPP VPPRTTTKPF ISITAQSSTE SAQDAYMDGQ GQRGDMISQS
GLSNSTESLD SMKALTAAIE AANAQIHGPA SQHMGSNAAA VTTTTTIATV TTEDRKKDFK
KNRCLSIGIQ VDDAEEPEKM AESKTSNKFQ SVGVQVEEEK CFRRFTRSNS VTTAVQADLD
FHDNLENSLE SIEDNSCPGP MARQFSRDAS TSTVSIQGSG NHYHACAADD DFDTDFDPSI
LPPPDPWIDS ITEDPLEAVQ RSVCHRDGHW FLKLLQAERD RMEGWCKLME REERENNLPE
DILGKIRTAV GSAQLLMAQK FYQFRELCEE NLNPNAHPRP TSQDLAGFWD MLQLSIENIS
MKFDELHQLK ANNWKQMDPL DKKERRAPPP VPKKPAKGPA PLIRERSLES SQRQEARKRL
MAAKRAASVR QNSATESAES IEIYIPEAQT RL
