ID A0A0V1PFB4_9BILA Unreviewed; 1434 AA.
AC A0A0V1PFB4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 03-MAY-2023, entry version 33.
DE SubName: Full=Rab-3-interacting molecule unc-10 {ECO:0000313|EMBL:KRZ94906.1};
GN Name=unc-10 {ECO:0000313|EMBL:KRZ94906.1};
GN ORFNames=T08_16258 {ECO:0000313|EMBL:KRZ94906.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ94906.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ94906.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ94906.1};
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 -!- 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:KRZ94906.1}.
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DR EMBL; JYDM01000015; KRZ94906.1; -; Genomic_DNA.
DR STRING; 92180.A0A0V1PFB4; -.
DR Proteomes; UP000054924; 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 GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR CDD; cd04031; C2A_RIM1alpha; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd22265; UDM1_RNF168; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
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; IPR041282; FYVE_2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR010911; Rab_BD.
DR InterPro; IPR039032; Rim-like.
DR InterPro; IPR001565; Synaptotagmin.
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; 2.
DR Pfam; PF02318; FYVE_2; 1.
DR Pfam; PF00595; PDZ; 1.
DR PRINTS; PR00399; SYNAPTOTAGMN.
DR SMART; SM00239; C2; 2.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50916; RABBD; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 6..154
FT /note="RabBD"
FT /evidence="ECO:0000259|PROSITE:PS50916"
FT DOMAIN 603..677
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 786..907
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1310..1428
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 161..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1155..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1252..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 12..65
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 161..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1434 AA; 160940 MW; A7D6996D625087EC CRC64;
MADATMPDLS HLTEEERQII EQVLQRQRAE ESQEMQLRRK YEKQLEEIEK QIEERKEVAR
KLVGTMDDAI CQICQKTKFA DGIGHKCYYC QLRSCARCGG RLHIKVKTDQ SKSGTLPPKA
STGQSIQQKT IWSCSLCQQR QQILAKTGKW FHHADNSNKT TLSTNEIPSA EPDQSTSSTA
LTVPQKDLVE PRQVKATPVD QNSTCQKIPE LQPQAIFEPT AKNNIAHADS PSSPDVLANS
KSLKRQSTIE DRCDATKTDE YRLNQRSTSK MSTSLEGSPS LYPQTETSLI QSKIAVKEGS
VTVSEPAETY SKNNRQQQSN KLSIKSAANR DQKLSHSEDD ATVQQSQLKT TTAERAAYKT
SERVAKKSYA DNLTNQEGLT EQRGELSKSE RPSSSNWQLA YTDSHAEDSS KYGNTSAIKN
TKEISSVGIK QPNVYLSSSK SAELRKSESV RSASGTSHSH RMQKHRIQQQ TDPETVDDQA
TEWHEHKSIP IRRALSEIGD YNLSTTSDQF FNQDPISDCL SRAAHDSIQT TERQGSLSSS
DEDFPSTSEC QSYEDLESES YSERGRQTKT KQRHHMFMLP ETSNQQFPLQ WQSSPDGSFI
YRKVTLHRTA GTSLGLKVTG GRSTSSGRLG AFITKVKRGS VADTVGHLVP GDEVFQWNGS
LLANASFDEV CEVINQSKFC NRIELVIART IMQSPFVDED NYAASGEVPK HFFEQRQLPY
RSQTFGTFPS QALNLQAASG TLLPDNQTPI VMITAPLVDM LQLNSNQQQQ NRTISGYSTA
RISGQIFGQI NVSLLYVPDI TQLIITVIEA VDLPPRSDGS ARNPYVKMFL LPDRSEKSRR
QSKTMAETCN PVWRQSLVYK EVTFTDLNRK AIEITVWDYD QYTSNDFLGE VLIDLSKANL
DNTPFWYTLI DMDEEASLKK KLRHVRPISA SYSKGLPARY DHRDRDLRFS AYSNATLPTI
TSRNVRQKYH DETWATACSS GYRSDSGVAF GSQEPRHRLS LSHHKPYDNA EFGHWEEADP
STSHMSGYYS DYTSHRRTRS GRRYAKNVQS VFPLELRPNS PTEESGNETS SPSHVIGASL
RRLPHPPPSL TDGCDRKIEL KYSSKKSSSD QVEDRANIVT GDYLSDGSET SISMPSTRSE
RLIGSQMIVK NITRERSLDE EHMPRSVNNN SSSHHYSTHV KQESAEAGGF YETTTENNYK
SCNATVEQIP TTDKRKKSLM TRLIPGRVTA AQLAQEQKRV VFRRSDEVGV PVNLSPQTSL
DITKQSSRES TDSNESSLVP VAHEPGSIGE FVDGLGPGQV VGRQAVASPC LGEIQISLYE
RRSNLEVRII RARHLNRKPG SKFYPSPYVK VYLCDEKSVV AKAKTGLAAR TPEPRFDQLL
IFTEAYHNRL LQVILVGDYG RIERKSVIGL AMIRLSNLDL KKPIEGWYKL YHSG
//
