CAR11_MOUSE
ID CAR11_MOUSE Reviewed; 1159 AA.
AC Q8CIS0; Q4VA14; Q6KAS3; Q8BYV0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Caspase recruitment domain-containing protein 11 {ECO:0000303|PubMed:12356734};
DE AltName: Full=CARD-containing MAGUK protein 1 {ECO:0000303|PubMed:16356855};
DE Short=Carma 1 {ECO:0000303|PubMed:16356855};
GN Name=Card11 {ECO:0000303|PubMed:12356734, ECO:0000312|MGI:MGI:1916978};
GN Synonyms=Carma1 {ECO:0000303|PubMed:16356855};
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 1), AND FUNCTION.
RC TISSUE=Thymus;
RX PubMed=12356734; DOI=10.1093/emboj/cdf505;
RA Pomerantz J.L., Denny E.M., Baltimore D.;
RT "CARD11 mediates factor-specific activation of NF-kappaB by the T cell
RT receptor complex.";
RL EMBO J. 21:5184-5194(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=129; 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 611-1159.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12154356; DOI=10.1038/ni824;
RA Wang D., You Y., Case S.M., McAllister-Lucas L.M., Wang L., DiStefano P.S.,
RA Nunez G., Bertin J., Lin X.;
RT "A requirement for CARMA1 in TCR-induced NF-kappa B activation.";
RL Nat. Immunol. 3:830-835(2002).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, AND PHOSPHORYLATION AT SER-564; SER-649 AND
RP SER-657.
RX PubMed=16356855; DOI=10.1016/j.immuni.2005.09.014;
RA Sommer K., Guo B., Pomerantz J.L., Bandaranayake A.D., Moreno-Garcia M.E.,
RA Ovechkina Y.L., Rawlings D.J.;
RT "Phosphorylation of the CARMA1 linker controls NF-kappaB activation.";
RL Immunity 23:561-574(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; SER-512 AND SER-891, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
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] {ECO:0007744|PDB:4I16}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 18-110, INTERACTION WITH BCL10,
RP AND MUTAGENESIS OF ARG-35; LYS-41; LYS-69 AND ARG-72.
RX PubMed=22880103; DOI=10.1371/journal.pone.0042775;
RA Li S., Yang X., Shao J., Shen Y.;
RT "Structural insights into the assembly of CARMA1 and BCL10.";
RL PLoS ONE 7:e42775-e42775(2012).
CC -!- FUNCTION: Adapter protein that plays a key role in adaptive immune
CC response by transducing the activation of NF-kappa-B downstream of T-
CC cell receptor (TCR) and B-cell receptor (BCR) engagement
CC (PubMed:12356734, PubMed:12154356, PubMed:16356855). Transduces signals
CC downstream TCR or BCR activation via the formation of a multiprotein
CC complex together with BCL10 and MALT1 that induces NF-kappa-B and MAP
CC kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways
CC (PubMed:12356734, PubMed:12154356, PubMed:16356855). Upon activation in
CC response to TCR or BCR triggering, CARD11 homooligomerizes to form a
CC nucleating helical template that recruits BCL10 via CARD-CARD
CC interaction, thereby promoting polymerization of BCL10 and subsequent
CC recruitment of MALT1: this leads to I-kappa-B kinase (IKK)
CC phosphorylation and degradation, and release of NF-kappa-B proteins for
CC nuclear translocation (By similarity). Its binding to DPP4 induces T-
CC cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-
CC dependent manner (By similarity). Promotes linear ubiquitination of
CC BCL10 by promoting the targeting of BCL10 to RNF31/HOIP (By
CC similarity). Stimulates the phosphorylation of BCL10 (By similarity).
CC Also activates the TORC1 signaling pathway (By similarity).
CC {ECO:0000250|UniProtKB:Q9BXL7, ECO:0000269|PubMed:12154356,
CC ECO:0000269|PubMed:12356734, ECO:0000269|PubMed:16356855}.
CC -!- ACTIVITY REGULATION: Maintained in an autoinhibited state via
CC homodimerization in which the CARD domain forms an extensive
CC interaction with the adjacent linker and coiled-coil regions (By
CC similarity). Activation downstream of T-cell receptor (TCR) by
CC phosphorylation by PRKCB and PRKCQ triggers CARD11 homooligomerization
CC and BCL10 recruitment, followed by activation of NF-kappa-B
CC (PubMed:16356855). {ECO:0000250|UniProtKB:Q9BXL7,
CC ECO:0000269|PubMed:16356855}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Homomultimer;
CC polymerizes following activation, forming a nucleating helical template
CC that seeds BCL10-filament formation via a CARD-CARD interaction (By
CC similarity). Interacts (via CARD domain) with BCL10 (via CARD domain);
CC interaction takes place following CARD11 activation and polymerization,
CC leading to the formation of a filamentous CBM complex assembly
CC (PubMed:22880103). Component of a CBM complex (CARD11-BCL10-MALT1)
CC complex involved in NF-kappa-B activation (By similarity). Found in a
CC membrane raft complex, at least composed of BCL10, CARD11, DPP4 and
CC IKBKB (By similarity). Interacts (via PDZ domain) with DPP4 (via
CC cytoplasmic tail) (By similarity). {ECO:0000250|UniProtKB:Q9BXL7,
CC ECO:0000269|PubMed:22880103}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BXL7}.
CC Membrane raft {ECO:0000250|UniProtKB:Q9BXL7}. Note=Colocalized with
CC DPP4 in membrane rafts. {ECO:0000250|UniProtKB:Q9BXL7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CIS0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CIS0-2; Sequence=VSP_031595;
CC -!- DOMAIN: The linker region, also named autoinhibitory interface, is less
CC inhibitory on its own than that of CARD9. The linker region together
CC with the inhibitory domain (ID) are required to prevent constitutive
CC activation and maintain CARD11 in an autoinhibitory state. Disruption
CC of the inhibitory domain (ID) region triggers polymerization and
CC activation, leading to formation of BCL10-nucleating filaments.
CC {ECO:0000250|UniProtKB:Q9BXL7}.
CC -!- PTM: Phosphorylation at Ser-564, Ser-649 and Ser-657 by PRKCB and PRKCQ
CC leads to a shift from an inactive to an active form that activates the
CC NF-kappa-B signaling. {ECO:0000269|PubMed:16356855}.
CC -!- DISRUPTION PHENOTYPE: Impaired activation of NF-kappa-B downstream of
CC T-cell receptor (TCR), leading to defects in interleukin-2 (IL2)
CC production. {ECO:0000269|PubMed:12154356}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD21384.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY135367; AAN10150.1; -; mRNA.
DR EMBL; AK131134; BAD21384.1; ALT_INIT; mRNA.
DR EMBL; BC096592; AAH96592.1; -; mRNA.
DR EMBL; AK037968; BAC29910.1; -; mRNA.
DR CCDS; CCDS51686.1; -. [Q8CIS0-2]
DR RefSeq; NP_780571.2; NM_175362.2. [Q8CIS0-2]
DR PDB; 4I16; X-ray; 1.75 A; A=18-110.
DR PDBsum; 4I16; -.
DR AlphaFoldDB; Q8CIS0; -.
DR SMR; Q8CIS0; -.
DR BioGRID; 224389; 8.
DR DIP; DIP-49692N; -.
DR IntAct; Q8CIS0; 7.
DR MINT; Q8CIS0; -.
DR STRING; 10090.ENSMUSP00000082941; -.
DR iPTMnet; Q8CIS0; -.
DR PhosphoSitePlus; Q8CIS0; -.
DR SwissPalm; Q8CIS0; -.
DR EPD; Q8CIS0; -.
DR jPOST; Q8CIS0; -.
DR MaxQB; Q8CIS0; -.
DR PaxDb; Q8CIS0; -.
DR PeptideAtlas; Q8CIS0; -.
DR PRIDE; Q8CIS0; -.
DR ProteomicsDB; 265276; -. [Q8CIS0-1]
DR ProteomicsDB; 265277; -. [Q8CIS0-2]
DR Antibodypedia; 11155; 331 antibodies from 45 providers.
DR Ensembl; ENSMUST00000085786; ENSMUSP00000082941; ENSMUSG00000036526. [Q8CIS0-2]
DR GeneID; 108723; -.
DR KEGG; mmu:108723; -.
DR UCSC; uc009aik.2; mouse. [Q8CIS0-2]
DR UCSC; uc012egd.1; mouse. [Q8CIS0-1]
DR CTD; 84433; -.
DR MGI; MGI:1916978; Card11.
DR VEuPathDB; HostDB:ENSMUSG00000036526; -.
DR eggNOG; KOG0708; Eukaryota.
DR GeneTree; ENSGT00940000158573; -.
DR HOGENOM; CLU_009760_1_0_1; -.
DR InParanoid; Q8CIS0; -.
DR OMA; MWSSVEE; -.
DR OrthoDB; 115953at2759; -.
DR PhylomeDB; Q8CIS0; -.
DR TreeFam; TF351139; -.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR BioGRID-ORCS; 108723; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Card11; mouse.
DR PRO; PR:Q8CIS0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8CIS0; protein.
DR Bgee; ENSMUSG00000036526; Expressed in mesenteric lymph node and 44 other tissues.
DR Genevisible; Q8CIS0; MM.
DR GO; GO:0032449; C:CBM complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0001772; C:immunological synapse; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0050700; F:CARD domain binding; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0030183; P:B cell differentiation; IMP:MGI.
DR GO; GO:0042100; P:B cell proliferation; IMP:MGI.
DR GO; GO:0035739; P:CD4-positive, alpha-beta T cell proliferation; IMP:MGI.
DR GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0046649; P:lymphocyte activation; IMP:MGI.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:MGI.
DR GO; GO:2000563; P:positive regulation of CD4-positive, alpha-beta T cell proliferation; IMP:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0050870; P:positive regulation of T cell activation; IMP:MGI.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0045577; P:regulation of B cell differentiation; IMP:MGI.
DR GO; GO:0050776; P:regulation of immune response; IMP:MGI.
DR GO; GO:0045580; P:regulation of T cell differentiation; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IDA:MGI.
DR GO; GO:0042110; P:T cell activation; IMP:MGI.
DR GO; GO:0031295; P:T cell costimulation; ISS:UniProtKB.
DR GO; GO:0045061; P:thymic T cell selection; IMP:MGI.
DR GO; GO:0038202; P:TORC1 signaling; ISS:UniProtKB.
DR CDD; cd08808; CARD_CARD11_CARMA1; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR033538; CARD11.
DR InterPro; IPR042141; CARD_CARD11.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR14559:SF4; PTHR14559:SF4; 1.
DR Pfam; PF00619; CARD; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50209; CARD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Disulfide bond;
KW Immunity; Isopeptide bond; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..1159
FT /note="Caspase recruitment domain-containing protein 11"
FT /id="PRO_0000320102"
FT DOMAIN 18..110
FT /note="CARD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT DOMAIN 672..760
FT /note="PDZ"
FT DOMAIN 978..1145
FT /note="Guanylate kinase-like"
FT REGION 111..128
FT /note="Linker"
FT /evidence="ECO:0000250|UniProtKB:Q9BXL7"
FT REGION 441..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..671
FT /note="Inhibitory domain (ID)"
FT /evidence="ECO:0000250|UniProtKB:Q9BXL7"
FT REGION 532..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 176..449
FT /evidence="ECO:0000255"
FT COMPBIAS 453..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXL7"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXL7"
FT MOD_RES 564
FT /note="Phosphoserine; by PKC/PRKCB and PKC/PRKCQ"
FT /evidence="ECO:0000269|PubMed:16356855"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXL7"
FT MOD_RES 649
FT /note="Phosphoserine; by PKC/PRKCB and PKC/PRKCQ"
FT /evidence="ECO:0000269|PubMed:16356855"
FT MOD_RES 657
FT /note="Phosphoserine; by PKC/PRKCB and PKC/PRKCQ"
FT /evidence="ECO:0000269|PubMed:16356855"
FT MOD_RES 891
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 930
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXL7"
FT DISULFID 28
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q9BXL7"
FT VAR_SEQ 524..528
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15449545,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_031595"
FT MUTAGEN 35
FT /note="R->A: Strongly decreased interaction with BCL10."
FT /evidence="ECO:0000269|PubMed:22880103"
FT MUTAGEN 41
FT /note="K->A: Slightly decreased interaction with BCL10."
FT /evidence="ECO:0000269|PubMed:22880103"
FT MUTAGEN 69
FT /note="K->A: Decreased interaction with BCL10."
FT /evidence="ECO:0000269|PubMed:22880103"
FT MUTAGEN 72
FT /note="R->A: Decreased interaction with BCL10."
FT /evidence="ECO:0000269|PubMed:22880103"
FT CONFLICT 258
FT /note="E -> Q (in Ref. 1; AAN10150)"
FT /evidence="ECO:0000305"
FT CONFLICT 860
FT /note="R -> L (in Ref. 4; BAC29910)"
FT /evidence="ECO:0000305"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:4I16"
FT HELIX 30..36
FT /evidence="ECO:0007829|PDB:4I16"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:4I16"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:4I16"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:4I16"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:4I16"
FT HELIX 84..98
FT /evidence="ECO:0007829|PDB:4I16"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:4I16"
SQ SEQUENCE 1159 AA; 134040 MW; 2ED53905B99DD94E CRC64;
MPGGGPAMDD YMETLKDEEE ALWDNVECNR HMLSRYINPA KLTPYLRQCK VIDEQDEDEV
LNAPMLPSKI NRAGRLLDIL HTKGQRGYVV FLESLEFYYP ELYKLVTGKE PTRRFSTIVV
EEGHEGLTHF LMNEVIKLQQ QVKAKDLQRC ELLAKSRQLE DEKKQLSLIR VELLTFQERY
YKMKEERDSY NDELVKVKDD NYNLAMRYAQ LSEEKNMAVM RSRDLQLEID QLKHRLNKME
EECKLERNQS LKLKNDIENR PRKEQVLELE RENEMLKTKI QELQSIIQAG KRSLPDSDKA
ILDILEHDRK EALEDRQELV NKIYNLQEEV RQAEELRDKY LEEKEDLELK CSTLGKDCEM
YKHRMNTVML QLEEVERERD QAFHSRDEAQ TQYSQCLIEK DKYRKQIREL EEKNDEMRIE
MVRREACIVN LESKLRRLSK DNGSLDQSLP RHLPATIISQ NLGDTSPRTN GQEADDSSTS
EESPEDSKYF LPYHPPRRRM NLKGIQLQRA KSPISMKQAS EFQALMRTVK GHEEDFTDGS
PSSSRSLPVT SSFSKMQPHR SRSSIMSITA EPPGNDSIVR RCKEDAPHRS TVEEDNDSCG
FDALDLDDEN HERYSFGPPS IHSSSSSHQS EGLDAYDLEQ VNLMLRKFSL ERPFRPSVTS
GGHVRGTGPL VQHTTLNGDG LITQLTLLGG NARGSFIHSV KPGSLAERAG LREGHQLLLL
EGCIRGERQS VPLDACTKEE ARWTIQRCSG LITLHYKVNH EGYRKLLKEM EDGLITSGDS
FYIRLNLNIS SQLDACSMSL KCDDVVHVLD TMYQDRHEWL CARVDPFTDQ DLDTGTIPSY
SRAQQLLLVK LQRLVHRGNR EEADSAHHTL RSLRNTLQPE EMLSTSDPRV SPRLSRASFF
FGQLLQFVSR SENKYKRMNS NERVRIISGS PLGSLSRSSL DATKLLTEKH EELDPENELS
RNLTLIPYSL VRAFHCERRR PVLFTPTMLA KTLVQKLLNS GGAMEFTICK SDIVTRDEFL
RKQKTETIIY SREKNPNTFE CIVPANIEAV AAKNKHCLLE AGIGCVRDLI KCKVYPIVLL
IRVSEKNIKR FRKLLPRPET EEEFLRVCRL KEKELEALPC LYATVEAEMW SSVEELLRVL
KDKIVEEQRK TIWVDEDQL
