NLRP6_RAT
ID NLRP6_RAT Reviewed; 881 AA.
AC Q63035; A5X5C9; D3ZYC0; F1LSH2;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 4.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=NACHT, LRR and PYD domains-containing protein 6 {ECO:0000305};
DE AltName: Full=Angiotensin II/vasopressin receptor {ECO:0000303|PubMed:18413781};
DE AltName: Full=Non-angiotensin-vasopressin receptor {ECO:0000303|PubMed:18413781};
DE Short=Non-AVR {ECO:0000303|PubMed:18413781};
DE AltName: Full=PYRIN-containing APAF1-like protein 5-like;
GN Name=Nlrp6 {ECO:0000312|RGD:708549};
GN Synonyms=Nalp6 {ECO:0000303|PubMed:18413781}, Navr,
GN Pypaf5 {ECO:0000303|PubMed:18413781};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND ALTERNATIVE PROMOTER USAGE (ISOFORM 2).
RC STRAIN=SR;
RX PubMed=18413781; DOI=10.1152/physiolgenomics.00199.2007;
RA Herrera V.L., Bagamasbad P., Didishvili T., Decano J.L., Ruiz-Opazo N.;
RT "Overlapping genes in Nalp6/PYPAF5 locus encode two V2-type vasopressin
RT isoreceptors: angiotensin-vasopressin receptor (AVR) and non-AVR.";
RL Physiol. Genomics 34:65-77(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 370-881, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=7489366; DOI=10.1038/nm1095-1074;
RA Ruiz-Opazo N., Akimoto K., Herrera V.L.M.;
RT "Identification of a novel dual angiotensin II/vasopressin receptor on the
RT basis of molecular recognition theory.";
RL Nat. Med. 1:1074-1081(1995).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=21088234; DOI=10.1152/ajpgi.00397.2010;
RA Kempster S.L., Belteki G., Forhead A.J., Fowden A.L., Catalano R.D.,
RA Lam B.Y., McFarlane I., Charnock-Jones D.S., Smith G.C.;
RT "Developmental control of the Nlrp6 inflammasome and a substrate, IL-18, in
RT mammalian intestine.";
RL Am. J. Physiol. 300:G253-G263(2011).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [6]
RP VARIANTS SALT-SENSITIVE HYPERTENSION SER-518 AND ARG-562.
RX PubMed=11984003; DOI=10.1007/s00894-001-0064-7;
RA Ruiz-Opazo N., Lopez L.V., Herrera V.L.M.;
RT "The dual AngII/AVP receptor gene N119S/C163R variant exhibits sodium-
RT induced dysfunction and cosegregates with salt-sensitive hypertension in
RT the Dahl salt-sensitive hypertensive rat model.";
RL Mol. Med. 8:24-32(2002).
RN [7]
RP IDENTIFICATION OF MAMMALIAN ORTHOLOGS OF PYPAF5.
RX PubMed=12633874; DOI=10.1016/s0014-5793(03)00161-3;
RA Albrecht M., Domingues F.S., Schreiber S., Lengauer T.;
RT "Identification of mammalian orthologs associates PYPAF5 with distinct
RT functional roles.";
RL FEBS Lett. 538:173-177(2003).
CC -!- FUNCTION: Acts as the sensor component of the NLRP6 inflammasome, which
CC mediates inflammasome activation in response to various pathogen-
CC associated signals, leading to maturation and secretion of IL1B and
CC IL18. Inflammasomes are supramolecular complexes that assemble in the
CC cytosol in response to pathogens and other damage-associated signals
CC and play critical roles in innate immunity and inflammation. Acts as a
CC recognition receptor (PRR): recognizes and binds specific pathogens and
CC other damage-associated signals, such as lipoteichoic acid (LTA), a
CC cell-wall component of Gram-positive bacteria, or double stranded RNA
CC (dsRNA). May also recognize and bind lipopolysaccharide (LPS), a major
CC component of the outer membrane of Gram-negative bacteria; however, LPS
CC is probably not a major activator of the NLRP6 inflammasome. Following
CC LTA- or dsRNA-binding, NLRP6 undergoes liquid-liquid phase separation
CC (LLPS), enhancing multivalent interactions, an essential step for the
CC formation of the NLRP6 inflammasome polymeric complex. The NLRP6
CC inflammasome acts by promoting recruitment of effector pro-inflammatory
CC caspases (CASP1 and/or CASP4) that catalyze maturation and secretion of
CC IL1B and IL18 in the extracellular milieu. The NLRP6 inflammasome plays
CC a central role in the maintenance of epithelial integrity and host
CC defense against microbial infections in the intestine. Required to
CC restrict infection against Gram-positive bacteria by recognizing
CC lipoteichoic acid (LTA), leading to recruitment of CASP4 and CASP1, and
CC subsequent maturation and secretion of IL1B and IL18. Involved in
CC intestinal antiviral innate immunity together with DHX15: recognizes
CC and binds viral dsRNA to restrict infection by enteric viruses through
CC the interferon pathway and GSDMD-dependent release of IL18 (By
CC similarity). Required to prevent infection by the apicomplexan parasite
CC Cryptosporidium in enterocytes by promoting GSDMD-dependent release of
CC IL18. The NLRP6 inflammasome may also regulate the gut microbiota
CC composition by acting as a sensor of microbiota-associated metabolites
CC to form a PYCARD/ASC-dependent inflammasome for downstream IL18 release
CC and secretion of antimicrobial peptides. Essential for gut mucosal
CC self-renewal and proliferation. Regulate mucus secretion in an
CC inflammasome- and autophagy-dependent manner to prevent invasion by
CC enteric bacteria,. During systemic bacterial infections, the NLRP6
CC inflammasome negatively regulates neutrophil recruitment and neutrophil
CC extracellular traps (NETs) formation. May promote peripheral nerve
CC recovery following injury via an inflammasome-independent mechanism (By
CC similarity). {ECO:0000250|UniProtKB:P59044,
CC ECO:0000250|UniProtKB:Q91WS2}.
CC -!- SUBUNIT: Homomultimer; forms the NLRP6 inflammasome polymeric complex,
CC a filament composed of homopolymers in response to pathogens and other
CC damage-associated signals. The core of NLRP6 inflammasomes consists of
CC a signal sensor component (NLRP6), an adapter (PYCARD/ASC), which
CC recruits effector pro-inflammatory caspases (CASP1 and CASP4).
CC Interacts (via pyrin domain) with PYCARD/ASC (via pyrin domain);
CC interaction takes place following NLRP6 activation and formation of
CC liquid-liquid phase separation (LLPS), initiating nucleation which
CC greatly enhances further addition of soluble PYCARD/ASC molecules to
CC the speck in a prion-like polymerization process. Clustered PYCARD/ASC
CC nucleates the formation of CASP1 (or possibly CASP4) filaments through
CC the interaction of their respective CARD domains, acting as a platform
CC for CASP1 polymerization. CASP1 filament formation increases local
CC enzyme concentration, resulting in trans-autocleavage and activation.
CC Active CASP1 then processes IL1B and IL18 precursors, leading to the
CC release of mature cytokines in the extracellular milieu and
CC inflammatory response. Interacts with DHX15.
CC {ECO:0000250|UniProtKB:Q91WS2}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:18413781}. Inflammasome
CC {ECO:0000250|UniProtKB:P59044}. Cell membrane
CC {ECO:0000269|PubMed:18413781}. Nucleus membrane
CC {ECO:0000269|PubMed:18413781}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:18413781}. Cell membrane
CC {ECO:0000269|PubMed:18413781}. Note=Predominantly expressed at the cell
CC membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=1; Synonyms=Non-Avr, Navr {ECO:0000303|PubMed:18413781};
CC IsoId=Q63035-1; Sequence=Displayed;
CC Name=2; Synonyms=Avr {ECO:0000303|PubMed:18413781};
CC IsoId=Q63035-2; Sequence=VSP_042302;
CC -!- TISSUE SPECIFICITY: Detected in several tissues (PubMed:7489366).
CC Expressed in renal epithelial cells in medullary thick ascending limb
CC of Henle, as well as in salivary gland apical epithelium (at protein
CC level). Isoform 1 is widely expressed. Isoform 2 is primarily expressed
CC in kidney (at protein level) (PubMed:18413781).
CC {ECO:0000269|PubMed:18413781, ECO:0000269|PubMed:7489366}.
CC -!- DEVELOPMENTAL STAGE: Strongly up-regulated in the intestine in late
CC gestation. {ECO:0000269|PubMed:21088234}.
CC -!- DOMAIN: The poly-Lys disordered region (350-354) mediates the formation
CC of liquid-liquid phase separation (LLPS), an essential step for
CC nucleation and formation of the NLRP6 inflammasome complex.
CC {ECO:0000250|UniProtKB:Q91WS2}.
CC -!- PTM: Polyubiquitinated with 'Lys-63'-linked chains, promoting the
CC interaction with PYCARD/ASC and formation of the NLRP6 inflammasome.
CC Deubiquitination by CYLD decreases the interaction with PYCARD/ASC.
CC {ECO:0000250|UniProtKB:Q91WS2}.
CC -!- DISEASE: Note=Defects in Nlrp6 may be a cause of salt-sensitive
CC hypertension. {ECO:0000305|PubMed:11984003}.
CC -!- SIMILARITY: Belongs to the NLRP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA03623.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ631800; ABG66707.1; -; mRNA.
DR EMBL; AABR07006017; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07006018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M85183; AAA03623.1; ALT_INIT; mRNA.
DR PIR; S27880; S27880.
DR RefSeq; NP_599202.2; NM_134375.3. [Q63035-1]
DR AlphaFoldDB; Q63035; -.
DR SMR; Q63035; -.
DR STRING; 10116.ENSRNOP00000019808; -.
DR iPTMnet; Q63035; -.
DR PhosphoSitePlus; Q63035; -.
DR PaxDb; Q63035; -.
DR PRIDE; Q63035; -.
DR GeneID; 171390; -.
DR KEGG; rno:171390; -.
DR UCSC; RGD:708549; rat. [Q63035-1]
DR CTD; 171389; -.
DR RGD; 708549; Nlrp6.
DR VEuPathDB; HostDB:ENSRNOG00000045677; -.
DR eggNOG; ENOG502SANB; Eukaryota.
DR InParanoid; Q63035; -.
DR OMA; QCRVQKL; -.
DR OrthoDB; 114368at2759; -.
DR PRO; PR:Q63035; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000045677; Expressed in jejunum and 7 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0061702; C:inflammasome complex; ISO:RGD.
DR GO; GO:0140738; C:NLRP6 inflammasome complex; ISS:UniProtKB.
DR GO; GO:0043228; C:non-membrane-bounded organelle; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0001530; F:lipopolysaccharide binding; ISS:UniProtKB.
DR GO; GO:0070891; F:lipoteichoic acid binding; ISS:UniProtKB.
DR GO; GO:0140693; F:molecular condensate scaffold activity; ISS:UniProtKB.
DR GO; GO:0038187; F:pattern recognition receptor activity; ISS:UniProtKB.
DR GO; GO:0042277; F:peptide binding; IMP:RGD.
DR GO; GO:0005000; F:vasopressin receptor activity; IDA:UniProtKB.
DR GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; ISO:RGD.
DR GO; GO:0002526; P:acute inflammatory response; ISO:RGD.
DR GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; ISO:RGD.
DR GO; GO:0140374; P:antiviral innate immune response; ISS:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0048874; P:host-mediated regulation of intestinal microbiota composition; ISO:RGD.
DR GO; GO:0070266; P:necroptotic process; IEA:Ensembl.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0050777; P:negative regulation of immune response; ISO:RGD.
DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; ISO:RGD.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; ISO:RGD.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0034122; P:negative regulation of toll-like receptor signaling pathway; ISO:RGD.
DR GO; GO:0070946; P:neutrophil-mediated killing of gram-positive bacterium; ISO:RGD.
DR GO; GO:0140739; P:NLRP6 inflammasome complex assembly; ISS:UniProtKB.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:2000494; P:positive regulation of interleukin-18-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0070269; P:pyroptosis; ISO:RGD.
DR GO; GO:0010506; P:regulation of autophagy; ISO:RGD.
DR GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0070255; P:regulation of mucus secretion; ISO:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0042060; P:wound healing; ISO:RGD.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR004020; DAPIN.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR041267; NLRP_HD2.
DR InterPro; IPR041075; NOD2_WH.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF05729; NACHT; 1.
DR Pfam; PF17776; NLRC4_HD2; 1.
DR Pfam; PF17779; NOD2_WH; 1.
DR Pfam; PF02758; PYRIN; 1.
DR SMART; SM01289; PYRIN; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50824; DAPIN; 1.
DR PROSITE; PS50837; NACHT; 1.
PE 1: Evidence at protein level;
KW Alternative promoter usage; ATP-binding; Cell membrane; Cytoplasm;
KW Immunity; Inflammasome; Inflammatory response; Innate immunity;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..881
FT /note="NACHT, LRR and PYD domains-containing protein 6"
FT /id="PRO_0000080894"
FT DOMAIN 1..129
FT /note="Pyrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00061"
FT DOMAIN 194..510
FT /note="NACHT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT REPEAT 459..484
FT /note="LRR 1"
FT REPEAT 637..660
FT /note="LRR 2"
FT REPEAT 749..772
FT /note="LRR 3"
FT REPEAT 839..863
FT /note="LRR 4"
FT REGION 154..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..611
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 200..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..423
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:18413781"
FT /id="VSP_042302"
FT VARIANT 518
FT /note="N -> S (in salt-sensitive hypertension)"
FT /evidence="ECO:0000269|PubMed:11984003"
FT VARIANT 562
FT /note="C -> R (in salt-sensitive hypertension)"
FT /evidence="ECO:0000269|PubMed:11984003"
FT CONFLICT 317
FT /note="S -> A (in Ref. 1; ABG66707)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="Q -> KLQ (in Ref. 3; AAA03623)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="V -> L (in Ref. 1; ABG66707 and 3; AAA03623)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="Missing (in Ref. 1; ABG66707 and 3; AAA03623)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 881 AA; 98324 MW; A7F36BD7667DF7ED CRC64;
MDAAGASCSS SEAVARELLL AALQDLSQEQ LKRFRHKLRD APLDGRSIPW GRLEHSDAVD
LTDKLIEFYA PEPAVDVTRK ILKKADIRDV SLRLKEQQLQ RLGSSSALLT VSEYKKKYRE
HVLRQHAKVK ERNARSVKIN KRFTKLLIAP GSGAGEDELL GTSGEPEPER ARRSDTHTFN
RLFRGNDDEG PRPLTVVLQG PAGIGKTMAA KKILYDWAGG KLYHSQVDFA FFMPCGELLE
RPGTRSLADL ILEQCPDRTA PVRRILAQPH RLLFILDGAD ELPTLAAPEA TPCRDPFEAT
SGLRVLSGLL SQELLPSARL LVTSRNATLG RLQGRLCSPQ CAEVRGFSDK DKKKYFFKFF
RDERKAERAY RFVKENETLY ALCFVPFVCW IVCTVLLQQM ELGRDLSRTS KTTTSVYLLF
ITSMLKSAGT NGPRVQGELR MLCRLAREGI LKHQAQFSEK DLERLKLQGS QVQTMFLSKK
ELPGVLETVV TYQFIDQSFQ EFLAALSYLL DAEGAPGNSA GSVQMLVNSD AGLRGHLALT
TRFLFGLLST ERIRDIGNHF GCVVPGRVKQ DTLRWVQGQS QPKVATVGAE KKDELKDEEA
EEEEEEEEEE EEELNFGLEL LYCLYETQED DFVRQALSSL PEMVLERVRL TRMDLEVLSY
CVQCCPDGQA LRLVSCGLVA AKEKKKKKKS FMNRLKGSQS TGKQPPASLL RPLCEAMITQ
QCGLSILTLS HCKLPDAVCR DLSEALKVAP SLRELGLLQN RLTEAGLRLL SQGLAWPKCK
VQTLRIQMPG LQEVIHYLVI VLQQSPVLTT LDLSGCQLPG TVVEPLCSAL KHPKCGLKTL
SLTSVELTEN PLRELQAVKT LKPDLAIIHS KLGTHPQPLK G
