KCNA5_MOUSE
ID KCNA5_MOUSE Reviewed; 602 AA.
AC Q61762; Q9Z1R6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Potassium voltage-gated channel subfamily A member 5;
DE AltName: Full=Voltage-gated potassium channel subunit Kv1.5;
DE Short=KV1-5;
GN Name=Kcna5;
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] (ISOFORMS 1; 2 AND 3), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=SWR/J; TISSUE=Heart;
RX PubMed=8226976; DOI=10.1016/s0021-9258(20)80523-7;
RA Attali B., Lesage F., Ziliani P., Guillemare E., Honore E., Waldmann R.,
RA Hugnot J.-P., Mattei M.-G., Lazdunski M., Barhanin J.;
RT "Multiple mRNA isoforms encoding the mouse cardiac Kv1-5 delayed rectifier
RT K+ channel.";
RL J. Biol. Chem. 268:24283-24289(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=129/Sv;
RX PubMed=11349004; DOI=10.1161/hh0901.090929;
RA London B., Guo W., Pan X., Lee J.S., Shusterman V., Rocco C.J.,
RA Logothetis D.A., Nerbonne J.M., Hill J.A.;
RT "Targeted replacement of KV1.5 in the mouse leads to loss of the 4-
RT aminopyridine-sensitive component of I(K,slow) and resistance to drug-
RT induced qt prolongation.";
RL Circ. Res. 88:940-946(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tanaka H., Janzen K., Winkfein R.J., Fiset C., Clark B., Giles W.R.;
RT "Cloning and functional expression of mouse heart K+ channel alpha-
RT subunits, Kv1.5, Kv4.2, and Kv4.3.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Stomach;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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).
CC -!- FUNCTION: Voltage-gated potassium channel that mediates transmembrane
CC potassium transport in excitable membranes. Forms tetrameric potassium-
CC selective channels through which potassium ions pass in accordance with
CC their electrochemical gradient. The channel alternates between opened
CC and closed conformations in response to the voltage difference across
CC the membrane (PubMed:8226976, PubMed:11349004). Can form functional
CC homotetrameric channels and heterotetrameric channels that contain
CC variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, and possibly other
CC family members as well; channel properties depend on the type of alpha
CC subunits that are part of the channel (By similarity). Channel
CC properties are modulated by cytoplasmic beta subunits that regulate the
CC subcellular location of the alpha subunits and promote rapid
CC inactivation (By similarity). Homotetrameric channels display rapid
CC activation and slow inactivation (PubMed:8226976, PubMed:11349004). May
CC play a role in regulating the secretion of insulin in normal pancreatic
CC islets (By similarity). {ECO:0000250|UniProtKB:P22460,
CC ECO:0000269|PubMed:11349004, ECO:0000269|PubMed:8226976}.
CC -!- SUBUNIT: Homotetramer and heterotetramer of potassium channel proteins.
CC Interacts with DLG1, which enhances channel currents. Forms a ternary
CC complex with DLG1 and CAV3 (By similarity). Interacts with KCNAB1 (By
CC similarity). Interacts with UBE2I (By similarity).
CC {ECO:0000250|UniProtKB:P19024, ECO:0000250|UniProtKB:P22460}.
CC -!- INTERACTION:
CC Q61762; Q4U4S6: Xirp2; NbExp=2; IntAct=EBI-26520959, EBI-10768169;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11349004,
CC ECO:0000269|PubMed:8226976}; Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q61762-1; Sequence=Displayed;
CC Name=2; Synonyms=5';
CC IsoId=Q61762-2; Sequence=VSP_000961;
CC Name=3; Synonyms=3';
CC IsoId=Q61762-3; Sequence=VSP_000962;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart and moderately in brain.
CC Low levels in thymus, skeletal muscle and spleen. Not expressed in
CC liver, lung or kidney.
CC -!- DOMAIN: The amino terminus may be important in determining the rate of
CC inactivation of the channel while the C-terminal PDZ-binding motif may
CC play a role in modulation of channel activity and/or targeting of the
CC channel to specific subcellular compartments. {ECO:0000250}.
CC -!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position. Channel opening and closing is effected by a
CC conformation change that affects the position and orientation of the
CC voltage-sensor paddle formed by S3 and S4 within the membrane. A
CC transmembrane electric field that is positive inside would push the
CC positively charged S4 segment outwards, thereby opening the pore, while
CC a field that is negative inside would pull the S4 segment inwards and
CC close the pore. Changes in the position and orientation of S4 are then
CC transmitted to the activation gate formed by the inner helix bundle via
CC the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}.
CC -!- PTM: Sumoylated on Lys-212, and Lys-525, preferentially with SUMO3.
CC Sumoylation regulates the voltage sensitivity of the channel (By
CC similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. The action potential in
CC myocytes is not prolonged by low concentrations of 4-aminopyridine,
CC contrary to the situation in wild-type. {ECO:0000269|PubMed:11349004}.
CC -!- MISCELLANEOUS: [Isoform 3]: Inactive. Inhibits expression of isoform 1
CC and isoform 2. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the potassium channel family. A (Shaker) (TC
CC 1.A.1.2) subfamily. Kv1.5/KCNA5 sub-subfamily. {ECO:0000305}.
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DR EMBL; L22218; AAA39365.1; -; mRNA.
DR EMBL; AF108659; AAD13779.1; -; mRNA.
DR EMBL; AF302768; AAG40241.1; -; Genomic_DNA.
DR EMBL; AK146843; BAE27474.1; -; mRNA.
DR EMBL; CH466523; EDK99840.1; -; Genomic_DNA.
DR EMBL; BC021787; AAH21787.1; -; mRNA.
DR CCDS; CCDS20554.1; -. [Q61762-1]
DR PIR; A49507; A49507.
DR RefSeq; NP_666095.1; NM_145983.2. [Q61762-1]
DR AlphaFoldDB; Q61762; -.
DR SMR; Q61762; -.
DR BioGRID; 200880; 1.
DR IntAct; Q61762; 1.
DR MINT; Q61762; -.
DR STRING; 10090.ENSMUSP00000055673; -.
DR GlyGen; Q61762; 1 site.
DR iPTMnet; Q61762; -.
DR PhosphoSitePlus; Q61762; -.
DR SwissPalm; Q61762; -.
DR MaxQB; Q61762; -.
DR PaxDb; Q61762; -.
DR PeptideAtlas; Q61762; -.
DR PRIDE; Q61762; -.
DR ProteomicsDB; 301769; -. [Q61762-1]
DR ProteomicsDB; 301770; -. [Q61762-2]
DR ProteomicsDB; 301771; -. [Q61762-3]
DR Antibodypedia; 22318; 292 antibodies from 34 providers.
DR DNASU; 16493; -.
DR Ensembl; ENSMUST00000060972; ENSMUSP00000055673; ENSMUSG00000045534. [Q61762-1]
DR GeneID; 16493; -.
DR KEGG; mmu:16493; -.
DR UCSC; uc009dva.2; mouse. [Q61762-1]
DR CTD; 3741; -.
DR MGI; MGI:96662; Kcna5.
DR VEuPathDB; HostDB:ENSMUSG00000045534; -.
DR eggNOG; KOG1545; Eukaryota.
DR GeneTree; ENSGT00940000161860; -.
DR HOGENOM; CLU_011722_4_0_1; -.
DR InParanoid; Q61762; -.
DR OMA; MNNTLSC; -.
DR OrthoDB; 695337at2759; -.
DR PhylomeDB; Q61762; -.
DR TreeFam; TF313103; -.
DR Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR BioGRID-ORCS; 16493; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q61762; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q61762; protein.
DR Bgee; ENSMUSG00000045534; Expressed in olfactory epithelium and 162 other tissues.
DR Genevisible; Q61762; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; IDA:MGI.
DR GO; GO:0046691; C:intracellular canaliculus; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0034705; C:potassium channel complex; ISS:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
DR GO; GO:0030018; C:Z disc; ISO:MGI.
DR GO; GO:0051393; F:alpha-actinin binding; ISO:MGI.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR GO; GO:0086089; F:voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization; ISO:MGI.
DR GO; GO:0086087; F:voltage-gated potassium channel activity involved in bundle of His cell action potential repolarization; ISO:MGI.
DR GO; GO:0086090; F:voltage-gated potassium channel activity involved in SA node cell action potential repolarization; ISO:MGI.
DR GO; GO:0086014; P:atrial cardiac muscle cell action potential; ISO:MGI.
DR GO; GO:0060081; P:membrane hyperpolarization; ISO:MGI.
DR GO; GO:0098914; P:membrane repolarization during atrial cardiac muscle cell action potential; ISO:MGI.
DR GO; GO:0086050; P:membrane repolarization during bundle of His cell action potential; ISO:MGI.
DR GO; GO:0086052; P:membrane repolarization during SA node cell action potential; ISO:MGI.
DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:2000288; P:positive regulation of myoblast proliferation; ISO:MGI.
DR GO; GO:0097623; P:potassium ion export across plasma membrane; ISO:MGI.
DR GO; GO:0055075; P:potassium ion homeostasis; ISO:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISO:MGI.
DR GO; GO:0006813; P:potassium ion transport; ISO:MGI.
DR GO; GO:0051259; P:protein complex oligomerization; ISO:MGI.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0060372; P:regulation of atrial cardiac muscle cell membrane repolarization; ISO:MGI.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:MGI.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0042391; P:regulation of membrane potential; IGI:MGI.
DR GO; GO:0043266; P:regulation of potassium ion transport; ISO:MGI.
DR GO; GO:0019229; P:regulation of vasoconstriction; IMP:MGI.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0010033; P:response to organic substance; IEA:Ensembl.
DR Gene3D; 1.20.120.350; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR InterPro; IPR003972; K_chnl_volt-dep_Kv1.
DR InterPro; IPR004052; K_chnl_volt-dep_Kv1.5.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR028325; VG_K_chnl.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01512; KV15CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01496; SHAKERCHANEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein; Ion channel;
KW Ion transport; Isopeptide bond; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Potassium; Potassium channel; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation; Voltage-gated channel.
FT CHAIN 1..602
FT /note="Potassium voltage-gated channel subfamily A member
FT 5"
FT /id="PRO_0000053986"
FT TOPO_DOM 1..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 239..260
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 261..314
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 315..336
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 337..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 348..368
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 369..384
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 385..405
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 406..420
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 421..442
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 443..456
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 457..468
FT /note="Helical; Name=Pore helix"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 469..476
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 477..483
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 484..512
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 513..602
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..420
FT /note="S4-S5 linker"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT MOTIF 469..474
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT MOTIF 600..602
FT /note="PDZ-binding"
FT MOD_RES 81
FT /note="Phosphoserine; by CK2 and PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 535
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 546
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 569
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT LIPID 337
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 212
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 525
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..200
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8226976"
FT /id="VSP_000961"
FT VAR_SEQ 515..602
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8226976"
FT /id="VSP_000962"
FT CONFLICT 8
FT /note="M -> T (in Ref. 1; AAA39365)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="G -> V (in Ref. 1; AAA39365)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="G -> A (in Ref. 1; AAA39365)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="G -> D (in Ref. 1; AAA39365)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="A -> V (in Ref. 1; AAA39365)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="T -> N (in Ref. 1; AAA39365)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="L -> S (in Ref. 1; AAA39365)"
FT /evidence="ECO:0000305"
FT CONFLICT 268..269
FT /note="DE -> VD (in Ref. 1; AAA39365)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="R -> L (in Ref. 1; AAA39365)"
FT /evidence="ECO:0000305"
FT CONFLICT 289..291
FT /note="ANG -> TNA (in Ref. 1; AAA39365)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="P -> T (in Ref. 1; AAA39365)"
FT /evidence="ECO:0000305"
FT CONFLICT 452..453
FT /note="HF -> QL (in Ref. 1; AAA39365)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="C -> H (in Ref. 1; AAA39365)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 602 AA; 66580 MW; 02926E85DC022DDA CRC64;
MEISLVPMEN GSAMTLRGGG EAGASCVQSP RGECGCPPTA GLNNQSKETS PRRRATHEDA
GQGGRPLPPM PQELPQPRRP SAEDEEGEGD PGLGTVEEDQ APQDSGSLHH QRVLINISGL
RFETQLGTLA QFPNTLLGDP VKRLRYFDPL RNEYFFDRNR PSFDGILYYY QSGGRLRRPV
NVSLDVFADE IRFYQLGDEA MERFREDEGF IKEEEKPLPR NEFQRQVWLI FEYPESSGSA
RAIAIVSVLV ILISIITFCL ETLPEFRDER ELLRHPPVPP QPPAPAPGAN GSGSGVLSSG
PTVAPLLPRT LADPFFIVET TCVIWFTFEL LVRFFACPSK AEFSRNIMNI IDIVAIFPYF
ITLGTELAEQ QPGGGGQNGQ QAMSLAILRV IRLVRVFRIF KLSRHSKGLQ ILGKTLQASM
RELGLLIFFL FIGVILFSSA VYFAEADNQG SHFSSIPDAF WWAVVTMTTV GYGDMRPITV
GGKIVGSLCA IAGVLTIALP VPVIVSNFNY FYHRETDHEE QAALKEEQGI QRRESGLDTG
GQRKVSCSKA SFCKTGGPLE STDSIRRGSC PLEKCHLKAK SNVDLRRSLY ALCLDTSRET
DL
