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Database: UniProt
Entry: A0A0V1LSC5_9BILA
LinkDB: A0A0V1LSC5_9BILA
Original site: A0A0V1LSC5_9BILA 
ID   A0A0V1LSC5_9BILA        Unreviewed;      2758 AA.
AC   A0A0V1LSC5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KRZ62424.1};
GN   Name=PCLO {ECO:0000313|EMBL:KRZ62424.1};
GN   ORFNames=T02_2486 {ECO:0000313|EMBL:KRZ62424.1};
OS   Trichinella nativa.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ62424.1, ECO:0000313|Proteomes:UP000054721};
RN   [1] {ECO:0000313|EMBL:KRZ62424.1, ECO:0000313|Proteomes:UP000054721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS10 {ECO:0000313|EMBL:KRZ62424.1};
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:KRZ62424.1}.
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DR   EMBL; JYDW01000009; KRZ62424.1; -; Genomic_DNA.
DR   STRING; 6335.A0A0V1LSC5; -.
DR   Proteomes; UP000054721; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0045202; C:synapse; IEA:UniProt.
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; IPR011011; Znf_FYVE_PHD.
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; SSF57903; FYVE/PHD zinc finger; 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          2370..2459
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          2548..2674
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..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          694..731
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1095..1122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1172..1195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1387..1408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1420..1443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2280..2306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1738..1765
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        397..466
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1172..1192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2758 AA;  304814 MW;  C2EAEF3724ABE263 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 TTTPSITLTA VEGEHEEEED DDDNDQATVV SFSQSNERPI YQTEPAASSP
     PPAADTTASS LFNYDQTDPT EWTNVEPLLL TQEIELSSNE TDQSVMNKAP GVEMDEEASS
     QTFYGDESSN PFLDGASFAD DQAISELVPV EEPDEEVDEE KLNNDNEQQL VIDASADEQL
     STALAEPIPS SDDDRFGVDE KIISQAEKTF ATVADHADSF GISNIAAAAS SVVIERQTSR
     SLTETTSRSV KQPFDMPAAS QAKLQSANKI ASAALDGFGG KSLKNFGGLF SRPKVDFSSF
     ATSVKKSTEA ALKKATDSVA SSFSSSSVVS MSQDSFNSNN QPCTVPPKSP SSSAINTDNA
     SVNSNKSSDQ WSALEVDKAD NNNNNSSAVM KSTAAAVVGK KGIQPSPVVS NTFRVSCNSD
     STEDTGYSSR CSPEDEFYRV GSDGAQFLIT YDSSRKLGVD TVKAPLSPRR RINPFIEDGI
     FSQRLITSVI VEQADDQLTK SFHVSGQKRQ LDIVEKVEPG EQEKFHLIAE QSFWSSEPLQ
     SQQLFGEIDG PQEISQAGKD STPKIEEVET LPLPDESTPL KYPPQQSIAN SGADEIAKLF
     AVEDSAPDSS ACTQMYDSSE VSSEQFDEDA QKRITEIESE FLLQNNQSAD SVEDWQMCPL
     CQMAEVHVRP DGVSINGQPC GNCGLTVCSK CGHVVEQNGR KVWLCGICDS NIAETNGRWY
     CDATKSQAIS EDDNSKLTFE KSQEVDSDIS DQASDSSDSY PDVVIEVPSS PVKQLDFDQE
     FSTSNSKQCY KVFRDIEKHF MNNFDQCDDT KHEGKVDHHD QQTGHSDKGN FETDPFRTVP
     ISVGQSPTFE KLTEQASPSD AQLSIGEEIF GKIVPPEQSC PSTNSNNAQE DSIDYAQAMR
     YYNTQPFYIH RPGPVYTILE DDEEVMELNQ DGKNKTAYMA AISASRPSTL SSSSSKSQLT
     SFSSPLANSY VGLDRPAQQM QTSSNASTEQ LTSTVSSDVL VQHFFATSTT STTTTSITAS
     KSHALQSNST FTPKPVRIAP PPPPPSQYSI SRDAKIEKSI HQETSNKPTG GRRHSADVPL
     STDVNDSVVS GSLNGTAFKP VHSSSSTLTI LAGQKKSDTP SSSTVAVSFA LPVVRTVDMD
     ASDPSSRLPL YSAASTLCTT STTASATTPI TTNETDDDEA VVECSGTGPF VSRLKRSPAM
     LLNCIKNETD LRAGSLQTAL QSTPTSALTA CSSTSYPSSR LIDSAIPTPT KVVSSTSCGD
     TLQSGKTFLN ERLFFAQASP GEMGRRKLPN IPKIASNRHQ QDVDEPLCNI SWSAGPVCSS
     TTTVNGSGIT GITGGSSYNN VISMPSSWKN IGHTLRPQHS TPLATNCRRL LPPTLARVLL
     KQELREALTK RLDKLEAAEI EANQREFVVG RYMATGVYPQ SAGVDSAPSV VRCGLSPEMV
     RGCVVHFDRS RYLSSIRQRE SSKAEFSNSY GQSSRYGSYG GEEQWNSSRF VRKKESFVKK
     DDSVVLLFVK FCGSSSLQTK RNDFTVQTSD VLERYKDAST QTVQQSSETT NSGNFVRFKP
     KDDLLLSKHK NVGVSTSEGP TCRTISTSTD EIDEDRLMAR RRSEGNKKWR NLNSKSFTYF
     SADDDFASRE SRRSKIRREI ARRREKFSSY EDLFNLPPHR ADSTYRYMDD GMELNNYITP
     SLYSSNRFSG HYGSLPRIDR LYDYSPMSRN ALYDDEPSSF SASYPLRPYQ KYDRLYRSDT
     APFVDGQDSA FHRGNYGTLT WRDQKPWFID GQRSLSSSLP YLNNLYESLD SQPECSFRGY
     SRGRRFGEAG TEQVNTPRSS SMLSHYANYL HNDFLRRSSA LDDGYGNLCE DRSTAKCMPY
     ADSSTEFNCR PSSVMEPIAS RLPYDKYDEP LNDCLSLHRC RTDAPMETYP STRDYCSMTA
     QQPTFNSRRR RSRRQQDQEP LYSGVKSAQY DADLKTQSYN PYLTDSSLQN ASVENHHRQR
     ASSQILLEEG KSTFRQASSP SSANIKRLLL VRDVRDRSGH GIGMRVIGGK ILPGSDGELV
     AYVAAVYKGG LVDLMEEVKE GDQILEWNGI KLTGKTYEEV QSIIDNTEGE FEIVLRSDAN
     LNQVYRLEEG PSSSLDKGYE SDCCLSNLAH PRLAKLALQR KTGLDQTNDR HCQGLDFGKA
     SPCFSTTPRS RSPFTANQQQ NSLLAQDLAN EGLLKLRVCF DHTSDTLFVT VLCAARLPNV
     DAKKRRPPNP FVKIYILPER IVQNKRRTKF IARSNNPVWN QTVVYKDLNL EQALSKMLEF
     TVWSYDRFKQ NTFLGKVIIN LSAANRWWKH DYTVIPFEVC ISMVKMQLFI HLIAALLFLF
     ARGEDDAVVE PTFADLKNLI DLYAREMEAM NAFGTSRRLK TIPLRDPRFI TRKLFKND
//
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