ID   AKAP6_HUMAN             Reviewed;        2319 AA.
AC   Q13023; A7E242; A7E2D4; O15028;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 3.
DT   27-MAR-2024, entry version 188.
DE   RecName: Full=A-kinase anchor protein 6;
DE            Short=AKAP-6;
DE   AltName: Full=A-kinase anchor protein 100 kDa;
DE            Short=AKAP 100;
DE   AltName: Full=Protein kinase A-anchoring protein 6;
DE            Short=PRKA6;
DE   AltName: Full=mAKAP;
GN   Name=AKAP6; Synonyms=AKAP100, KIAA0311;
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 1), AND VARIANT VAL-1492.
RX   PubMed=10413680; DOI=10.1242/jcs.112.16.2725;
RA   Kapiloff M.S., Shillace R.V., Westphal A.M., Scott J.D.;
RT   "mAKAP: an A-kinase anchoring protein targeted to the nuclear membrane of
RT   differentiated myocytes.";
RL   J. Cell Sci. 112:2725-2736(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA   Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. VII. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 4:141-150(1997).
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1666-2319 (ISOFORM 1).
RC   TISSUE=Hippocampus;
RX   PubMed=7721854; DOI=10.1074/jbc.270.16.9327;
RA   McCartney S., Little B.M., Langeberg L.K., Scott J.D.;
RT   "Cloning and characterization of A-kinase anchor protein 100 (AKAP100). A
RT   protein that targets A-kinase to the sarcoplasmic reticulum.";
RL   J. Biol. Chem. 270:9327-9333(1995).
RN   [8]
RP   INTERACTION WITH SYNPO2.
RX   PubMed=17923693; DOI=10.1128/mcb.00950-07;
RA   Faul C., Dhume A., Schecter A.D., Mundel P.;
RT   "Protein kinase A, Ca2+/calmodulin-dependent kinase II, and calcineurin
RT   regulate the intracellular trafficking of myopodin between the Z-disc and
RT   the nucleus of cardiac myocytes.";
RL   Mol. Cell. Biol. 27:8215-8227(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   VARIANTS [LARGE SCALE ANALYSIS] MET-910; ILE-1192; GLN-1702 AND THR-1839.
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).
CC   -!- FUNCTION: Binds to type II regulatory subunits of protein kinase A and
CC       anchors/targets them to the nuclear membrane or sarcoplasmic reticulum.
CC       May act as an adapter for assembling multiprotein complexes.
CC   -!- SUBUNIT: Interacts with RII subunit of PKA, phosphatase 2B
CC       (calcineurin) and AKAP79. Interacts with SYNPO2.
CC       {ECO:0000269|PubMed:17923693}.
CC   -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum. Nucleus membrane. Note=In
CC       heart muscle. Participation of multiple targeting signals allow correct
CC       intracellular targeting. These may be repeated motifs rich in basic and
CC       hydrophobic amino acids, palmitoylated/myristoylated motifs or
CC       alternatively splice targeting sequences.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q13023-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q13023-2; Sequence=VSP_054497, VSP_054498;
CC   -!- TISSUE SPECIFICITY: Highly expressed in cardiac and skeletal muscle,
CC       followed by brain.
CC   -!- DOMAIN: RII-alpha binding site, predicted to form an amphipathic helix,
CC       could participate in protein-protein interactions with a complementary
CC       surface on the R-subunit dimer.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA20770.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U17195; AAA92354.2; -; mRNA.
DR   EMBL; AB002309; BAA20770.2; ALT_INIT; mRNA.
DR   EMBL; AL049781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL117672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL132988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL136298; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471078; EAW65931.1; -; Genomic_DNA.
DR   EMBL; BC150185; AAI50186.1; -; mRNA.
DR   EMBL; BC150288; AAI50289.1; -; mRNA.
DR   EMBL; BC154413; AAI54414.1; -; mRNA.
DR   CCDS; CCDS9644.1; -. [Q13023-1]
DR   RefSeq; NP_004265.3; NM_004274.4. [Q13023-1]
DR   AlphaFoldDB; Q13023; -.
DR   BioGRID; 114857; 15.
DR   ELM; Q13023; -.
DR   IntAct; Q13023; 18.
DR   MINT; Q13023; -.
DR   STRING; 9606.ENSP00000280979; -.
DR   GlyCosmos; Q13023; 1 site, 1 glycan.
DR   GlyGen; Q13023; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; Q13023; -.
DR   PhosphoSitePlus; Q13023; -.
DR   BioMuta; AKAP6; -.
DR   DMDM; 116241243; -.
DR   EPD; Q13023; -.
DR   jPOST; Q13023; -.
DR   MassIVE; Q13023; -.
DR   MaxQB; Q13023; -.
DR   PaxDb; 9606-ENSP00000280979; -.
DR   PeptideAtlas; Q13023; -.
DR   ProteomicsDB; 1788; -.
DR   ProteomicsDB; 59109; -. [Q13023-1]
DR   Antibodypedia; 23117; 158 antibodies from 29 providers.
DR   DNASU; 9472; -.
DR   Ensembl; ENST00000280979.9; ENSP00000280979.4; ENSG00000151320.11. [Q13023-1]
DR   Ensembl; ENST00000557354.5; ENSP00000450531.1; ENSG00000151320.11. [Q13023-2]
DR   GeneID; 9472; -.
DR   KEGG; hsa:9472; -.
DR   MANE-Select; ENST00000280979.9; ENSP00000280979.4; NM_004274.5; NP_004265.3.
DR   UCSC; uc001wrq.4; human. [Q13023-1]
DR   AGR; HGNC:376; -.
DR   CTD; 9472; -.
DR   DisGeNET; 9472; -.
DR   GeneCards; AKAP6; -.
DR   HGNC; HGNC:376; AKAP6.
DR   HPA; ENSG00000151320; Group enriched (brain, heart muscle, retina, skeletal muscle, tongue).
DR   MIM; 604691; gene.
DR   neXtProt; NX_Q13023; -.
DR   OpenTargets; ENSG00000151320; -.
DR   PharmGKB; PA24670; -.
DR   VEuPathDB; HostDB:ENSG00000151320; -.
DR   eggNOG; ENOG502QSMH; Eukaryota.
DR   GeneTree; ENSGT00810000125473; -.
DR   HOGENOM; CLU_231193_0_0_1; -.
DR   InParanoid; Q13023; -.
DR   OMA; PECFFEA; -.
DR   OrthoDB; 4505223at2759; -.
DR   PhylomeDB; Q13023; -.
DR   TreeFam; TF105405; -.
DR   PathwayCommons; Q13023; -.
DR   SignaLink; Q13023; -.
DR   BioGRID-ORCS; 9472; 14 hits in 1154 CRISPR screens.
DR   ChiTaRS; AKAP6; human.
DR   GeneWiki; AKAP6; -.
DR   GenomeRNAi; 9472; -.
DR   Pharos; Q13023; Tbio.
DR   PRO; PR:Q13023; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q13023; Protein.
DR   Bgee; ENSG00000151320; Expressed in cortical plate and 151 other cell types or tissues.
DR   ExpressionAtlas; Q13023; baseline and differential.
DR   GO; GO:0034704; C:calcium channel complex; IDA:BHF-UCL.
DR   GO; GO:0005901; C:caveola; ISS:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR   GO; GO:0014704; C:intercalated disc; ISS:BHF-UCL.
DR   GO; GO:0014701; C:junctional sarcoplasmic reticulum membrane; ISS:BHF-UCL.
DR   GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0030315; C:T-tubule; ISS:BHF-UCL.
DR   GO; GO:0008179; F:adenylate cyclase binding; ISS:BHF-UCL.
DR   GO; GO:0060090; F:molecular adaptor activity; ISS:BHF-UCL.
DR   GO; GO:0051018; F:protein kinase A binding; IBA:GO_Central.
DR   GO; GO:0034237; F:protein kinase A regulatory subunit binding; ISS:BHF-UCL.
DR   GO; GO:0043495; F:protein-membrane adaptor activity; ISS:BHF-UCL.
DR   GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR   GO; GO:0001508; P:action potential; IC:BHF-UCL.
DR   GO; GO:0019933; P:cAMP-mediated signaling; NAS:BHF-UCL.
DR   GO; GO:0071320; P:cellular response to cAMP; IDA:BHF-UCL.
DR   GO; GO:0071345; P:cellular response to cytokine stimulus; ISS:BHF-UCL.
DR   GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; ISS:BHF-UCL.
DR   GO; GO:0030307; P:positive regulation of cell growth; ISS:BHF-UCL.
DR   GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; ISS:BHF-UCL.
DR   GO; GO:1902261; P:positive regulation of delayed rectifier potassium channel activity; IDA:BHF-UCL.
DR   GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IDA:BHF-UCL.
DR   GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISS:BHF-UCL.
DR   GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; ISS:BHF-UCL.
DR   GO; GO:0006605; P:protein targeting; NAS:UniProtKB.
DR   GO; GO:0060306; P:regulation of membrane repolarization; IDA:BHF-UCL.
DR   GO; GO:0010738; P:regulation of protein kinase A signaling; ISS:BHF-UCL.
DR   GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IC:BHF-UCL.
DR   CDD; cd00176; SPEC; 1.
DR   Gene3D; 1.20.58.60; -; 2.
DR   InterPro; IPR026696; AKAP6/CEP68.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   PANTHER; PTHR14514:SF2; A-KINASE ANCHOR PROTEIN 6; 1.
DR   PANTHER; PTHR14514; PKA ANCHORING PROTEIN; 1.
DR   Pfam; PF00435; Spectrin; 1.
DR   SMART; SM00150; SPEC; 3.
DR   SUPFAM; SSF46966; Spectrin repeat; 3.
DR   Genevisible; Q13023; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Membrane; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Sarcoplasmic reticulum.
FT   CHAIN           1..2319
FT                   /note="A-kinase anchor protein 6"
FT                   /id="PRO_0000064530"
FT   REPEAT          762..848
FT                   /note="Spectrin 1"
FT   REPEAT          1036..1150
FT                   /note="Spectrin 2"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          301..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          493..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          566..614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          691..757
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1250..1272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1821..1842
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1900..1925
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1963..1983
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2063..2076
FT                   /note="PKA-RII subunit binding domain"
FT   REGION          2198..2319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..366
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..507
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..532
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..592
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        695..713
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        735..750
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2198..2222
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2246..2261
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1073
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WVC7"
FT   MOD_RES         1570
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WVC7"
FT   MOD_RES         1595
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WVC7"
FT   VAR_SEQ         1050..1075
FT                   /note="KTLGEKIQDTMAGHSGSSPRDLLSPE -> VFAFLLLFVGYVYIFCVVKYSV
FT                   RFLI (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_054497"
FT   VAR_SEQ         1076..2319
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_054498"
FT   VARIANT         337
FT                   /note="A -> V (in dbSNP:rs3742926)"
FT                   /id="VAR_028171"
FT   VARIANT         408
FT                   /note="N -> S (in dbSNP:rs17099240)"
FT                   /id="VAR_028172"
FT   VARIANT         558
FT                   /note="N -> D (in dbSNP:rs35210906)"
FT                   /id="VAR_050653"
FT   VARIANT         892
FT                   /note="E -> K (in dbSNP:rs34572259)"
FT                   /id="VAR_050654"
FT   VARIANT         910
FT                   /note="K -> M (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035781"
FT   VARIANT         1192
FT                   /note="M -> I (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035782"
FT   VARIANT         1492
FT                   /note="A -> V (in dbSNP:rs11845640)"
FT                   /evidence="ECO:0000269|PubMed:10413680"
FT                   /id="VAR_028173"
FT   VARIANT         1516
FT                   /note="T -> A (in dbSNP:rs17099587)"
FT                   /id="VAR_050655"
FT   VARIANT         1522
FT                   /note="V -> I (in dbSNP:rs34711402)"
FT                   /id="VAR_050656"
FT   VARIANT         1702
FT                   /note="E -> Q (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035783"
FT   VARIANT         1839
FT                   /note="P -> T (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs745389246)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035784"
FT   VARIANT         2035
FT                   /note="N -> D (in dbSNP:rs1051695)"
FT                   /id="VAR_028174"
FT   VARIANT         2171
FT                   /note="F -> Y (in dbSNP:rs4647899)"
FT                   /id="VAR_028175"
FT   VARIANT         2209
FT                   /note="D -> H (in dbSNP:rs4402458)"
FT                   /id="VAR_028176"
FT   VARIANT         2267
FT                   /note="E -> D (in dbSNP:rs35977369)"
FT                   /id="VAR_050657"
FT   CONFLICT        974
FT                   /note="W -> C (in Ref. 1; AAA92354)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2319 AA;  256720 MW;  7607B71AD2140727 CRC64;
     MLTMSVTLSP LRSQDLDPMA TDASPMAINM TPTVEQGEGE EAMKDMDSDQ QYEKPPPLHT
     GADWKIVLHL PEIETWLRMT SERVRDLTYS VQQDSDSKHV DVHLVQLKDI CEDISDHVEQ
     IHALLETEFS LKLLSYSVNV IVDIHAVQLL WHQLRVSVLV LRERILQGLQ DANGNYTRQT
     DILQAFSEET KEGRLDSLTE VDDSGQLTIK CSQNYLSLDC GITAFELSDY SPSEDLLSGL
     GDMTSSQVKT KPFDSWSYSE MEKEFPELIR SVGLLTVAAD SISTNGSEAV TEEVSQVSLS
     VDDKGGCEED NASAVEEQPG LTLGVSSSSG EALTNAAQPS SETVQQESSS SSHHDAKNQQ
     PVPCENATPK RTIRDCFNYN EDSPTQPTLP KRGLFLKEET FKNDLKGNGG KRQMVDLKPE
     MSRSTPSLVD PPDRSKLCLV LQSSYPNSPS AASQSYECLH KVGNGNLENT VKFHIKEISS
     SLGRLNDCYK EKSRLKKPHK TSEEVPPCRT PKRGTGSGKQ AKNTKSSAVP NGELSYTSKA
     IEGPQTNSAS TSSLEPCNQR SWNAKLQLQS ETSSSPAFTQ SSESSVGSDN IMSPVPLLSK
     HKSKKGQASS PSHVTRNGEV VEAWYGSDEY LALPSHLKQT EVLALKLENL TKLLPQKPRG
     ETIQNIDDWE LSEMNSDSEI YPTYHVKKKH TRLGRVSPSS SSDIASSLGE SIESGPLSDI
     LSDEESSMPL AGMKKYADEK SERASSSEKN ESHSATKSAL IQKLMQDIQH QDNYEAIWEK
     IEGFVNKLDE FIQWLNEAME TTENWTPPKA EMDDLKLYLE THLSFKLNVD SHCALKEAVE
     EEGHQLLELI ASHKAGLKDM LRMIASQWKE LQRQIKRQHS WILRALDTIK AEILATDVSV
     EDEEGTGSPK AEVQLCYLEA QRDAVEQMSL KLYSEQYTSS SKRKEEFADM SKVHSVGSNG
     LLDFDSEYQE LWDWLIDMES LVMDSHDLMM SEEQQQHLYK RYSVEMSIRH LKKTELLSKV
     EALKKGGVLL PNDLLEKVDS INEKWELLGK TLGEKIQDTM AGHSGSSPRD LLSPESGSLV
     RQLEVRIKEL KGWLRDTELF IFNSCLRQEK EGTMNTEKQL QYFKSLCREI KQRRRGVASI
     LRLCQHLLDD RETCNLNADH QPMQLIIVNL ERRWEAIVMQ AVQWQTRLQK KMGKESETLN
     VIDPGLMDLN GMSEDALEWD EMDISNKLIS LNEESNDLDQ ELQPVIPSLK LGETSNEDPG
     YDEEADNHGG SQYASNITAP SSPHIYQVYS LHNVELYEDN HMPFLKNNPK VTGMTQPNVL
     TKSLSKDSSF SSTKSLPDLL GGSNLVKPCA CHGGDMSQNS GSESGIVSEG DTETTTNSEM
     CLLNAVDGSP SNLETEHLDP QMGDAVNVLK QKFTDEGESI KLPNSSQSSI SPVGCVNGKV
     GDLNSITKHT PDCLGEELQG KHDVFTFYDY SYLQGSKLKL PMIMKQSQSE KAHVEDPLLR
     GFYFDKKSCK SKHQTTELQP DVPPHERILA SASHEMDRIS YKSGNIEKTF TGMQNAKQLS
     LLSHSSSIES LSPGGDLFGL GIFKNGSDSL QRSTSLESWL TSYKSNEDLF SCHSSGDISV
     SSGSVGELSK RTLDLLNRLE NIQSPSEQKI KRSVSDITLQ SSSQKMSFTG QMSLDIASSI
     NEDSAASLTE LSSSDELSLC SEDIVLHKNK IPESNASFRK RLTRSVADES DVNVSMIVNV
     SCTSACTDDE DDSDLLSSST LTLTEEELCI KDEDDDSSIA TDDEIYEDCT LMSGLDYIKN
     ELQTWIRPKL SLTRDKKRCN VSDEMKGSKD ISSSEMTNPS DTLNIETLLN GSVKRVSENN
     GNGKNSSHTH ELGTKRENKK TIFKVNKDPY VADMENGNIE GIPERQKGKP NVTSKVSENL
     GSHGKEISES EHCKCKALMD SLDDSNTAGK EFVSQDVRHL PKKCPNHHHF ENQSTASTPT
     EKSFSELALE TRFNNRQDSD ALKSSDDAPS MAGKSAGCCL ALEQNGTEEN ASISNISCCN
     CEPDVFHQKD AEDCSVHNFV KEIIDMASTA LKSKSQPENE VAAPTSLTQI KEKVLEHSHR
     PIQLRKGDFY SYLSLSSHDS DCGEVTNYIE EKSSTPLPLD TTDSGLDDKE DIECFFEACV
     EGDSDGEEPC FSSAPPNESA VPSEAAMPLQ ATACSSEFSD SSLSADDADT VALSSPSSQE
     RAEVGKEVNG LPQTSSGCAE NLEFTPSKLD SEKESSGKPG ESGMPEEHNA ASAKSKVQDL
     SLKANQPTDK AALHPSPKTL TCEENLLNLH EKRHRNMHR
//