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 24-JAN-2024, entry version 188. 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 a voltage-sensor and CC is 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) CC (TC 1.A.1.2) subfamily. Kv1.5/KCNA5 sub-subfamily. {ECO:0000305}. 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; 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 GlyCosmos; Q61762; 1 site, No reported glycans. DR GlyGen; Q61762; 1 site. DR iPTMnet; Q61762; -. DR PhosphoSitePlus; Q61762; -. DR SwissPalm; Q61762; -. DR MaxQB; Q61762; -. DR PaxDb; 10090-ENSMUSP00000055673; -. DR PeptideAtlas; Q61762; -. DR ProteomicsDB; 301769; -. [Q61762-1] DR ProteomicsDB; 301770; -. [Q61762-2] DR ProteomicsDB; 301771; -. [Q61762-3] DR Antibodypedia; 22318; 337 antibodies from 35 providers. DR DNASU; 16493; -. DR Ensembl; ENSMUST00000060972.5; ENSMUSP00000055673.4; ENSMUSG00000045534.5. [Q61762-1] DR GeneID; 16493; -. DR KEGG; mmu:16493; -. DR UCSC; uc009dva.2; mouse. [Q61762-1] DR AGR; MGI:96662; -. 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; 1478695at2759; -. DR PhylomeDB; Q61762; -. DR TreeFam; TF313103; -. DR Reactome; R-MMU-1296072; Voltage gated Potassium channels. DR Reactome; R-MMU-5576890; Phase 3 - rapid repolarisation. DR BioGRID-ORCS; 16493; 2 hits in 76 CRISPR screens. DR PRO; PR:Q61762; -. DR Proteomes; UP000000589; Chromosome 6. DR RNAct; Q61762; Protein. DR Bgee; ENSMUSG00000045534; Expressed in olfactory epithelium and 163 other cell types or tissues. DR GO; GO:0009986; C:cell surface; ISO:MGI. 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: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: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 Gene3D; 1.10.287.70; -; 1. DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 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; IPR027359; Volt_channel_dom_sf. DR PANTHER; PTHR11537:SF250; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY A MEMBER 5; 1. DR PANTHER; PTHR11537; VOLTAGE-GATED POTASSIUM CHANNEL; 1. DR Pfam; PF02214; BTB_2; 1. DR Pfam; PF00520; Ion_trans; 1. DR PRINTS; PR00169; KCHANNEL. DR PRINTS; PR01512; KV15CHANNEL. DR PRINTS; PR01491; KVCHANNEL. DR PRINTS; PR01496; SHAKERCHANEL. DR SMART; SM00225; BTB; 1. DR SUPFAM; SSF54695; POZ domain; 1. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1. DR Genevisible; Q61762; MM. 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 //