ID A0A0V0TI98_9BILA Unreviewed; 1049 AA.
AC A0A0V0TI98;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Actin-related protein 3 {ECO:0000256|ARBA:ARBA00023892};
GN Name=arx-1 {ECO:0000313|EMBL:KRX38751.1};
GN ORFNames=T05_1336 {ECO:0000313|EMBL:KRX38751.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX38751.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX38751.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX38751.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the actin family. ARP3 subfamily.
CC {ECO:0000256|ARBA:ARBA00006681}.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.8) family. {ECO:0000256|ARBA:ARBA00006666,
CC ECO:0000256|RuleBase:RU003857}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX38751.1}.
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DR EMBL; JYDJ01000256; KRX38751.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0TI98; -.
DR Proteomes; UP000055048; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:UniProt.
DR CDD; cd00063; FN3; 2.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR003092; 2pore_dom_K_chnl_TASK.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR11937; ACTIN; 1.
DR PANTHER; PTHR11937:SF31; ACTIN-RELATED PROTEIN 3; 1.
DR Pfam; PF00022; Actin; 2.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PRINTS; PR01333; 2POREKCHANEL.
DR PRINTS; PR01095; TASKCHANNEL.
DR SMART; SM00268; ACTIN; 1.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 2.
DR PROSITE; PS50853; FN3; 2.
PE 3: Inferred from homology;
KW Ion channel {ECO:0000256|RuleBase:RU003857};
KW Ion transport {ECO:0000256|RuleBase:RU003857};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium channel {ECO:0000256|ARBA:ARBA00022826};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003857};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003857}.
FT TRANSMEM 481..507
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 599..617
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 629..650
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 709..729
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 741..761
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 767..790
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 849..946
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 947..1042
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
SQ SEQUENCE 1049 AA; 121400 MW; 2141F6C8ED091EC7 CRC64;
MPSQQPQNIK SQIRWYEDEM CQEWLRYSKI GFAGNTHPNF IIPTVIACRS QSYNIPNTGR
MPIDMDFFIG DEALNATNYS IRYPVRHGVV EDWNLMERFL EHSIFKYLRI EPEDHNFLMT
ESPLNTPENR EYLAEVMFES FNVPGLYIAV QVAFLAVAAS WVGCPQENRS LTAFVIDIGD
GITHCVPVID GYTLASCSRF MPIAGREVTF FIQNLLREQF SKYDENLSKF IKKYEGQHAV
TKKPFHVDVG YERFLGPEIF FCPEFANADY KRSLSEEVDL AIQQCPIDVR RALYGNIVLS
GGSTMFKDFD RRIERDVRRL VNQRLQITEQ LCDHRITPKP VTVRVLSHRL QRNAVWFGGS
VLASSSEFAM SVHTKKEYDE IGPSICRRNA HNRLVMEERP SVDTSQHCQQ QDEDDTLILD
KTLQIGSHHK TTSTSQWKHI LRIKEEHYYY VKKNITSCKV CKNLLTNIKN MLKMLNRSNA
YFYLILPHAS LIIVSFLYTL IGAFVFMKLE QPHIRHLYNQ KMIQMKADKD LLLERLIEMS
RAKSSMDEGQ TEFRNFVRSI YSMHKWNRWR NTENDRYARI VLQPNEISLN ELIHPGQEWN
FAAALFFVLT TLTTIGYGDV TPLTKEGRIF CICYCIVGIP LFLVTTANTA KFLSSGVYYL
YVRYILIKEK LLKTSGCWRS KRVEYLHNDD RGNEKILLSD LKKIQYVRLS APAILLIVFG
YCILGAALMQ QIEPWAFIDS LYFTTISILT VGFGDIVPNA FHSLYIPVVY ILFGLVITTM
AVDTVGVQYV QRIHQFGRSM TNADYIHLLR RMKMRKFESD EINTLPQMDM IAKIPTDSSP
SSKRRSITDP LLVQVINVTP YSIKLRWDEG LEKCPDEEYI LKYRAKGTFS LADHKQKRQY
SLSLSDREYE INNLRSFTVY SITISRTYKK QEATKRNLVV ITEPESSPQD LAIAEVNQDS
ILLSWKPPFK NKHLVKAYAI YCTTDVELPY EGWRKILVPP NVFTCTINDI NDISNCFFSM
CSVYDTYHSP LSKPVSVVLS STSKITEAD
//
