ID   PSD3_MOUSE              Reviewed;        1037 AA.
AC   Q2PFD7; Q3TTA1; Q80TN6; Q80UZ7; Q8CEA6;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   12-OCT-2022, entry version 132.
DE   RecName: Full=PH and SEC7 domain-containing protein 3;
DE   AltName: Full=Exchange factor for ADP-ribosylation factor guanine nucleotide factor 6 D;
DE            Short=Exchange factor for ARF6 D;
DE   AltName: Full=Pleckstrin homology and SEC7 domain-containing protein 3;
GN   Name=Psd3; Synonyms=Efa6d {ECO:0000303|PubMed:23603394}, Kiaa0942;
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 5), FUNCTION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16707115; DOI=10.1016/j.brainres.2006.02.058;
RA   Sakagami H., Suzuki H., Kamata A., Owada Y., Fukunaga K., Mayanagi H.,
RA   Kondo H.;
RT   "Distinct spatiotemporal expression of EFA6D, a guanine nucleotide exchange
RT   factor for ARF6, among the EFA6 family in mouse brain.";
RL   Brain Res. 1093:1-11(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1-729 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Skin, 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] OF 714-1037 (ISOFORM 4).
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 823-1037 (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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-1009, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1009, AND IDENTIFICATION BY
RP   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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1009, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759; SER-998; SER-1000;
RP   SER-1001; SER-1003 AND SER-1009, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Liver, Pancreas, Spleen, and Testis;
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   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=23603394; DOI=10.1016/j.febslet.2013.03.042;
RA   Ueda T., Hanai A., Takei T., Kubo K., Ohgi M., Sakagami H., Takahashi S.,
RA   Shin H.W., Nakayama K.;
RT   "EFA6 activates Arf6 and participates in its targeting to the Flemming body
RT   during cytokinesis.";
RL   FEBS Lett. 587:1617-1623(2013).
CC   -!- FUNCTION: Guanine nucleotide exchange factor for ARF6.
CC       {ECO:0000269|PubMed:16707115}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23603394}. Cell
CC       projection, ruffle membrane {ECO:0000269|PubMed:23603394}. Postsynaptic
CC       density {ECO:0000269|PubMed:16707115}. Note=In interphase associated
CC       with the plasma membrane, in particular with membrane ruffling regions.
CC       {ECO:0000269|PubMed:23603394}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q2PFD7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q2PFD7-2; Sequence=VSP_029160;
CC       Name=3;
CC         IsoId=Q2PFD7-3; Sequence=VSP_029157, VSP_029159, VSP_029160;
CC       Name=4;
CC         IsoId=Q2PFD7-4; Sequence=VSP_029161;
CC       Name=5;
CC         IsoId=Q2PFD7-5; Sequence=VSP_029158;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC       liver. Present in brain, with highest levels in olfactory bulb, cortex,
CC       hippocampal pyramidal cell layer and cerebellar granule cell layer (at
CC       protein level). {ECO:0000269|PubMed:16707115}.
CC   -!- DEVELOPMENTAL STAGE: Expressed only in spinal cord at 13 dpc. At 18 dpc
CC       and P0, appears weakly in forebrain. Expression in brain increases
CC       after birth and peaks at P10. {ECO:0000269|PubMed:16707115}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB220685; BAE73186.1; -; mRNA.
DR   EMBL; AK028684; BAC26065.1; -; mRNA.
DR   EMBL; AK161498; BAE36424.1; -; mRNA.
DR   EMBL; AK122405; BAC65687.1; -; mRNA.
DR   EMBL; BC042208; AAH42208.1; -; mRNA.
DR   CCDS; CCDS22340.1; -. [Q2PFD7-3]
DR   CCDS; CCDS40355.3; -. [Q2PFD7-5]
DR   RefSeq; NP_081902.1; NM_027626.1.
DR   RefSeq; NP_084539.2; NM_030263.5. [Q2PFD7-3]
DR   RefSeq; NP_808366.2; NM_177698.4. [Q2PFD7-5]
DR   RefSeq; XP_017168191.1; XM_017312702.1. [Q2PFD7-2]
DR   AlphaFoldDB; Q2PFD7; -.
DR   SMR; Q2PFD7; -.
DR   BioGRID; 231513; 3.
DR   IntAct; Q2PFD7; 2.
DR   MINT; Q2PFD7; -.
DR   STRING; 10090.ENSMUSP00000091178; -.
DR   iPTMnet; Q2PFD7; -.
DR   PhosphoSitePlus; Q2PFD7; -.
DR   SwissPalm; Q2PFD7; -.
DR   jPOST; Q2PFD7; -.
DR   MaxQB; Q2PFD7; -.
DR   PaxDb; Q2PFD7; -.
DR   PeptideAtlas; Q2PFD7; -.
DR   PRIDE; Q2PFD7; -.
DR   ProteomicsDB; 291692; -. [Q2PFD7-1]
DR   ProteomicsDB; 291693; -. [Q2PFD7-2]
DR   ProteomicsDB; 291694; -. [Q2PFD7-3]
DR   ProteomicsDB; 291695; -. [Q2PFD7-4]
DR   ProteomicsDB; 291696; -. [Q2PFD7-5]
DR   Antibodypedia; 9043; 150 antibodies from 21 providers.
DR   DNASU; 234353; -.
DR   Ensembl; ENSMUST00000093468; ENSMUSP00000091178; ENSMUSG00000030465. [Q2PFD7-3]
DR   Ensembl; ENSMUST00000093469; ENSMUSP00000091179; ENSMUSG00000030465. [Q2PFD7-5]
DR   Ensembl; ENSMUST00000098696; ENSMUSP00000096293; ENSMUSG00000030465. [Q2PFD7-5]
DR   GeneID; 234353; -.
DR   KEGG; mmu:234353; -.
DR   UCSC; uc009lvz.2; mouse. [Q2PFD7-3]
DR   UCSC; uc009lwc.1; mouse. [Q2PFD7-2]
DR   UCSC; uc057alt.1; mouse. [Q2PFD7-5]
DR   CTD; 23362; -.
DR   MGI; MGI:1918215; Psd3.
DR   VEuPathDB; HostDB:ENSMUSG00000030465; -.
DR   eggNOG; KOG0932; Eukaryota.
DR   GeneTree; ENSGT00940000156591; -.
DR   HOGENOM; CLU_011021_1_1_1; -.
DR   InParanoid; Q2PFD7; -.
DR   OMA; YDIYVSI; -.
DR   PhylomeDB; Q2PFD7; -.
DR   TreeFam; TF319755; -.
DR   BioGRID-ORCS; 234353; 4 hits in 70 CRISPR screens.
DR   ChiTaRS; Psd3; mouse.
DR   PRO; PR:Q2PFD7; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q2PFD7; protein.
DR   Bgee; ENSMUSG00000030465; Expressed in subiculum and 235 other tissues.
DR   ExpressionAtlas; Q2PFD7; baseline and differential.
DR   Genevisible; Q2PFD7; MM.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:MGI.
DR   GO; GO:0032011; P:ARF protein signal transduction; IC:MGI.
DR   GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR   CDD; cd00171; Sec7; 1.
DR   Gene3D; 1.10.1000.11; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR041681; PH_9.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR023394; Sec7_C_sf.
DR   InterPro; IPR000904; Sec7_dom.
DR   InterPro; IPR035999; Sec7_dom_sf.
DR   Pfam; PF15410; PH_9; 1.
DR   Pfam; PF01369; Sec7; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00222; Sec7; 1.
DR   SUPFAM; SSF48425; SSF48425; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50190; SEC7; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cell projection; Coiled coil;
KW   Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW   Reference proteome; Synapse.
FT   CHAIN           1..1037
FT                   /note="PH and SEC7 domain-containing protein 3"
FT                   /id="PRO_0000309454"
FT   DOMAIN          515..723
FT                   /note="SEC7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT   DOMAIN          774..887
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          37..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          169..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          304..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          353..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          730..762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          984..1037
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          911..941
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        262..278
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..319
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        730..750
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        993..1008
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1016..1037
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         76
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYI0"
FT   MOD_RES         759
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         998
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1000
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1001
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1003
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1009
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15345747,
FT                   ECO:0007744|PubMed:16452087, ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1..518
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_029157"
FT   VAR_SEQ         1..44
FT                   /note="MEGRNAAAEPFVWVNSASAHSQSVAKAKYEFLFGKSEEKTPDSS -> MGNC
FT                   WSYSNLC (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:16707115"
FT                   /id="VSP_029158"
FT   VAR_SEQ         519..530
FT                   /note="TRGPQEIAFWGS -> MGIIMCLIYCYC (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_029159"
FT   VAR_SEQ         684
FT                   /note="Missing (in isoform 3 and isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_029160"
FT   VAR_SEQ         919..966
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:12693553"
FT                   /id="VSP_029161"
FT   CONFLICT        190
FT                   /note="D -> E (in Ref. 2; BAC26065)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1037 AA;  114722 MW;  E6E3C240AC7A61E8 CRC64;
     MEGRNAAAEP FVWVNSASAH SQSVAKAKYE FLFGKSEEKT PDSSDHGGST LLPPTVTNEF
     PEYGTMEEGG EGLRASLDFD AKSPPCRLPG QQAVHLLAGQ DSILNSVTEG PNDAPQCHPQ
     EQSLQPIDSL ISALKATEAR IASGTFQATK VLDKDANFSV YQVDKELSTA SHKPQRAHRT
     FPVGPGKSPD IPLSAEVPTE ENLSLHIQED LSALLPEEAQ AHRSQITNYR RQGPLRVPES
     ACPVSSSSAG SHNPVDRVGA LREQRSDLGR EHPRGYDRGG SMGRQGRIKH VEFQGVEILW
     TGEEAESRHP PERTASPVSK EFAKRPSHSS PACGVCSTST HLTGDVWDET CKAPSERPGT
     SAGTLSPMPL GESGEDDVFL RESKEHLEEN FAIQGDKERI LDQEEHLRGD DDILGPGYTE
     DSTDVYSSQF ETILDNTSLY YSAESLETLY SEPDSYFSFE MPLTPMIQQR IKEGGQFLER
     TSVGGQHDVL SVSADGGIVM GYSAGITNGL HDSANSVYTR GPQEIAFWGS RDRCFAEGKT
     TGVDAGSEMG STDILEKETT ESLSNGTNSN VEAAKRLAKR LYHLDRFKRS DVAKHLGKNN
     EFSKLVAEEY LKFFDFTGMT LDQSLRYFLK AFSLVGETQE RERVLIHFSN RYFSCNPDTI
     TSKDGVHCLT CAMMLLNTDL HGHVNIGKKM TCQEFITNLQ GVNEGGDFSK DLLKALYNSI
     KNEKLEWAVD DEEKKKSPSE GTDEKANGTH PKTISRIGST TNPFLDIPHD PNAAVYKSGF
     LARKIHADMD GKKTPRGKRG WKTFYAVLKG TVLYLQKDEY KPEKSLSDED LKNAVSVHHA
     LASKATDYEK KPNVFKLKTA DWRVLLFQTQ SPEEMQGWIN KINCVAAVFS APPFPAAIGS
     QKKFSRPLLP ATTTKLSQEE QLKSHESKLK QITTELAEHR SYPPDKKVKA KDVDEYKLKD
     HYLEFEKTRY EIYVSVLKEG GKELLTTDGN EPVGLKKSHS SPSLNPDASP VTAKVKRNVS
     ERKDHRPETP GIKQKVT
//