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Database: UniProt
Entry: A0A0V1LSE0_9BILA
LinkDB: A0A0V1LSE0_9BILA
Original site: A0A0V1LSE0_9BILA 
ID   A0A0V1LSE0_9BILA        Unreviewed;      2733 AA.
AC   A0A0V1LSE0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   22-FEB-2023, entry version 25.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KRZ62422.1};
GN   Name=PCLO {ECO:0000313|EMBL:KRZ62422.1};
GN   ORFNames=T02_2486 {ECO:0000313|EMBL:KRZ62422.1};
OS   Trichinella nativa.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ62422.1, ECO:0000313|Proteomes:UP000054721};
RN   [1] {ECO:0000313|EMBL:KRZ62422.1, ECO:0000313|Proteomes:UP000054721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS10 {ECO:0000313|EMBL:KRZ62422.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KRZ62422.1}.
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DR   EMBL; JYDW01000009; KRZ62422.1; -; Genomic_DNA.
DR   Proteomes; UP000054721; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0006887; P:exocytosis; IEA:InterPro.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR039032; Rim-like.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR12157:SF21; RAB3 INTERACTING MOLECULE, ISOFORM F; 1.
DR   PANTHER; PTHR12157; REGULATING SYNAPTIC MEMBRANE EXOCYTOSIS PROTEIN; 1.
DR   Pfam; PF00168; C2; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054721}.
FT   DOMAIN          2345..2434
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          2523..2649
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          145..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          245..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          665..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1084..1105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1156..1179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1362..1383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1395..1418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2255..2281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1713..1740
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        156..197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..213
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..349
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        368..437
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1156..1176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2733 AA;  302190 MW;  C2638B247486088F CRC64;
     MKCGDSKHFR MFVCVLVRRL RAEVPGIRTG AVNKDAAHWL VRIDRFTNVY RLLEWEFDWL
     PPFPPAGSVE AAVIERFILP RQKKTRIKNL DEMFGKVFGG ITHAVSHTAS QLRTQVLAPQ
     FNATVDPLAG LSEVERAHIL AVQRRAADED SKLSQQPMVL PRSTASTVDA TASLPLPSLA
     PSTLPSRPSS ASSTETEGAD DTSDDDDDDS GPIPDLDQIG LSEVTPADMR LDGLAEIGQE
     RLLTSQESIE EQPTIVVHSP STNSNGAVDE SDANELEREE EEDERQQQHA EEEHEEDSLD
     ELEHYSSPES DTQDVVEPVV QIPGDQQNLQ LAATDAGDES PSSSGDEWNC EYAGESFTAP
     IRKSIEIDEP TTTPQSNERP IYQTEPAASS PPPAADTTAS SLFNYDQTDP TEWTNVEPLL
     LTQEIELSSN ETDQSVMNKA PGVEMDEEAS SQTFYGDESS NPFLDGASFA DDQAISELVP
     VEEPDEEVDE EKLNNDNEQQ LVIDASADEQ LSTALAEPIP SSDDDRFGVD EKIISQAEKT
     FATVADHADS FGISNIAAAA SSVVIERQTS RSLTETTSRS VKQPFDMPAA SQAKLQSANK
     IASAALDGFG GKSLKNFGGL FSRPKVDFSS FATSVKKSTE AALKKATDSV ASSFSSSSVV
     SMSQDSFNSN NQPCTVPPKS PSSSAINTDN ASVNSNKSSD QWSALEVDKA DNNNNNSSAV
     MKSTAAAVVG KKGIQPSPVV SNTFRVSCNS DSTEDTGYSS RCSPEDEFYR VGSDGAQFLI
     TYDSSRKLGV DTVKAPLSPR RRINPFIEDG IFSQRLITSV IVEQADDQLT KSFHVSGQKR
     QLDIVEKVEP GEQEKFHLIA EQSFWSSEPL QSQQLFGEID GPQEISQAGK DSTPKIEEVE
     TLPLPDESTP LKYPPQQSIA NSGADEIAKL FAVEDSAPDS SACTQMYDSS EVSSEQFDED
     AQKRITEIES EFLLQNNQSA DSVEDWQMCP LCQMAEVHVR PDGVSINGQP CGNCGLTVCS
     KCGHVVEQNG YGYVAYAIQI LPKLMVAGIV MVMPDRDAYA FCVYWFTTKS QAISEDDNSK
     LTFEKSQEVD SDISDQASDS SDSYPDVVIE VPSSPVKQLD FDQEFSTSNS KQCYKVFRDI
     EKHFMNNFDQ CDDTKHEGKV DHHDQQTGHS DKGNFETDPF RTVPISVGQS PTFEKLTEQA
     SPSDAQLSIG EEIFGKIVPP EQSCPSTNSN NAQEDSIDYA QAMRYYNTQP FYIHRPGPVY
     TILEDDEEVM ELNQDAISAS RPSTLSSSSS KSQLTSFSSP LANSYVGLDR PAQQMQTSSN
     ASTEQLTSTV SSDVLVQHFF ATSTTSTTTT SITASKSHAL QSNSTFTPKP VRIAPPPPPP
     SQYSISRDAK IEKSIHQETS NKPTGGRRHS ADVPLSTDVN DSVVSGSLNG TAFKPVHSSS
     STLTILAGQK KSDTPSSSTV AVSFALPVVR TVDMDASDPS SRLPLYSAAS TLCTTSTTAS
     ATTPITTNET DDDEAVVECS GTGPFVSRLK RSPAMLLNCI KNETDLRAGS LQTALQSTPT
     SALTACSSTS YPSSRLIDSA IPTPTKVVSS TSCGDTLQSG KTFLNERLFF AQASPGEMGR
     RKLPNIPKIA SNRHQQDVDE PLCNISWSAG PVCSSTTTVN GSGITGITGG SSYNNVISMP
     SSWKNIGHTL RPQHSTPLAT NCRRLLPPTL ARVLLKQELR EALTKRLDKL EAAEIEANQR
     EFVVGRYMAT GVYPQSAGVD SAPSVVRCGL SPEMVRGCVV HFDRSRYLSS IRQRESSKAE
     FSNSYGQSSR YGSYGGEEQW NSSRFVRKKE SFVKKDDSVV LLFVKFCGSS SLQTKRNDFT
     VQTSDVLERY KDASTQTVQQ SSETTNSGNF VRFKPKDDLL LSKHKNVGVS TSEGPTCRTI
     STSTDEIDED RLMARRRSEG NKKWRNLNSK SFTYFSADDD FASRESRRSK IRREIARRRE
     KFSSYEDLFN LPPHRADSTY RYMDDGMELN NYITPSLYSS NRFSGHYGSL PRIDRLYDYS
     PMSRNALYDD EPSSFSASYP LRPYQKYDRL YRSDTAPFVD GQDSAFHRGN YGTLTWRDQK
     PWFIDGQRSL SSSLPYLNNL YESLDSQPEC SFRGYSRGRR FGEAGTEQVN TPRSSSMLSH
     YANYLHNDFL RRSSALDDGY GNLCEDRSTA KCMPYADSST EFNCRPSSVM EPIASRLPYD
     KYDEPLNDCL SLHRCRTDAP METYPSTRDY CSMTAQQPTF NSRRRRSRRQ QDQEPLYSGV
     KSAQYDADLK TQSYNPYLTD SSLQNASVEN HHRQRASSQI LLEEGKSTFR QASSPSSANI
     KRLLLVRDVR DRSGHGIGMR VIGGKILPGS DGELVAYVAA VYKGGLVDLM EEVKEGDQIL
     EWNGIKLTGK TYEEVQSIID NTEGEFEIVL RSDANLNQVY RLEEGPSSSL DKGYESDCCL
     SNLAHPRLAK LALQRKTGLD QTNDRHCQGL DFGKASPCFS TTPRSRSPFT ANQQQNSLLA
     QDLANEGLLK LRVCFDHTSD TLFVTVLCAA RLPNVDAKKR RPPNPFVKIY ILPERIVQNK
     RRTKFIARSN NPVWNQTVVY KDLNLEQALS KMLEFTVWSY DRFKQNTFLG KVIINLSAAN
     RWWKHDYTVI PFEVCISMVK MQLFIHLIAA LLFLFARGED DAVVEPTFAD LKNLIDLYAR
     EMEAMNAFGT SRRLKTIPLR DPRFITRKLF KND
//
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