ID A0A0V1M5F7_9BILA Unreviewed; 1025 AA.
AC A0A0V1M5F7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Actin-related protein 3 {ECO:0000256|ARBA:ARBA00023892};
GN Name=arx-1 {ECO:0000313|EMBL:KRZ67099.1};
GN ORFNames=T10_4332 {ECO:0000313|EMBL:KRZ67099.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ67099.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ67099.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ67099.1};
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:KRZ67099.1}.
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DR EMBL; JYDO01000210; KRZ67099.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1M5F7; -.
DR Proteomes; UP000054843; 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; 1.
DR Pfam; PF00041; fn3; 1.
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:UP000054843};
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 457..483
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 575..593
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 605..626
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 685..705
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 717..737
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 743..766
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 825..922
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 923..1018
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
SQ SEQUENCE 1025 AA; 118299 MW; 13353E57CA0D256B CRC64;
MLYQQLQNVR SQIPKNFTKN ESFKILAMLL SSAVVIDNGT GYSKIGFAGN THPNFIIPTV
IACRSQSYNI PNTGRMPIDM DFFIGDEALN ATNYSIRYPV RHGVVEDWNL MERFLEHSIF
KYLRIEPEDH NFLMTESPLN TPENREYLAE VMFESFNVPG LYIAVQVAFL AVAASWVGCP
QENRSLTAFV IDIGDGITHC VPVIDGYTLA SCSRFMPIAG REVTFFIQNL LRERETGIPP
EQSMETARNI KEKYCYVSPN IMKEFSKYDE NLSKFIKKYE GQHAVTKKPF NVEVGYERFL
GPEIFFCPEF ANADYKRSLS EEVDLAIQQC PIDVRRALYG NIVLSGGSTM FKDFDRRIER
DVRRLVNQRL QITEKLCDHR ITSEFAMSVH TKKEYDEIGP SICRRNAHNR LVMEERPSVD
TSQHCQQQDE DDTLILDKTL QIGSHNKTTS TSQWKHYFYL ILPHASLIIV SFLYTLIGAF
VFMKLEQPHI RHLYNQKMIQ MKADKDLLLE RLIEMSRAKS SMDEGQTEFR NFVRSIYSMH
KWNRWRNTEN DRYARIVLQP NEISLNELIH PGQEWNFAAA LFFVLTTLTT IGYGDVTPLT
KEGRIFCICY CIVGIPLFLV TTANTAKFLS SGVYYLYVRY ILIKEKLLKT SGCWWSKRVE
YVHNDDRDNE KILLSDLKKI QYVRLSAPAI LLIVFGYCIL GAALMQQIEP WAFIDSLYFT
TISILTVGFG DIVPTAFHSL YIPVVYILFG LVITTMAVDT VGVQYVQRIH QFGRSMTNAD
YIHLLRRMKM RKFESDEINT LPQTDMMAKI PTDSSPSSKR RSITDPLSVQ VINVTPYSIK
LKWDEGLEQR PDEEYILKYR AKGTFSLADH KQKRQYSLSL SDREYEINNL RSFTVYSITI
SRTYKKQEAT KRNLVVITEP ESSPQDLAIA EVNQDSILLS WKPPFKNKHL VKAYAIYCTT
DVELPYEGWR KILVPPNVFT CTINDINDIS NCFFSMCSVY DTYHSPLSKP VSVVLSNTSK
ITEID
//
