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Database: UniProt
Entry: A0A0V1N2Q6_9BILA
LinkDB: A0A0V1N2Q6_9BILA
Original site: A0A0V1N2Q6_9BILA 
ID   A0A0V1N2Q6_9BILA        Unreviewed;      1444 AA.
AC   A0A0V1N2Q6;
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:KRZ78218.1};
DE   Flags: Fragment;
GN   Name=unc-10 {ECO:0000313|EMBL:KRZ78218.1};
GN   ORFNames=T10_8713 {ECO:0000313|EMBL:KRZ78218.1};
OS   Trichinella papuae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ78218.1, ECO:0000313|Proteomes:UP000054843};
RN   [1] {ECO:0000313|EMBL:KRZ78218.1, ECO:0000313|Proteomes:UP000054843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ78218.1};
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:KRZ78218.1}.
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DR   EMBL; JYDO01000013; KRZ78218.1; -; Genomic_DNA.
DR   STRING; 268474.A0A0V1N2Q6; -.
DR   Proteomes; UP000054843; 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:UP000054843};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          11..159
FT                   /note="RabBD"
FT                   /evidence="ECO:0000259|PROSITE:PS50916"
FT   DOMAIN          610..684
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          793..914
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          1320..1438
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          159..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          534..574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1040..1102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1162..1185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1262..1289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          17..70
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        159..191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..249
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..269
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..336
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..359
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..464
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..562
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1060..1084
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1171..1185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRZ78218.1"
SQ   SEQUENCE   1444 AA;  161711 MW;  B4CA8F68FB4B38C0 CRC64;
     LSQVNMADAT MPDLSHLTEE ERQIIEQVLQ RQRAEESQEM QLRRKYEKQL EEIEKQIEER
     KEVARKLVGT MDDAICQICQ KTKFADGIGH KCYYCQLRSC ARCGGRLNIK VKTDQTKSGT
     LPPKPSTGQS IQQKTIWSCS LCQQRQQILA KTGKWFHHAD NSNKTTQSTN ESPSAEPDQS
     TSSTALTVPQ KNLVEPRQVK ATPVDQNSTS QKIPELQPQA TFEPTAKNNI VHADSSSSPD
     VLANSKSLKR QSTIEDRCDA TKTDEYRLNQ RSTSKMSTSS EGSPSLYPQT EISPIQSKLA
     VKEGSVSVSE PAEPYSKSNH QQQSNRLSIQ SVVNRDQKVS HSEDDAIVQQ SQLKTKTAER
     AACKSSERVA KKSYGNADNL THREGLTEQK GELSKSERSS SSNWQLAYTD SHAENSSKYS
     NTSAIKNTKQ ISLAGIKQSN VYPSSSKSTE LRKSESVRSA SGTSHGHRIQ KHRIQQQTDP
     QTVDDQATEW HEHKSIPIRR ALSEIGDYNL STTSDQFFNQ DPISDCLPRA ARDSIQATKR
     QESLSSSDED FPSTSECQSY EDLESESYSE RGRQTKTKQR HHMFLLPEAS NQQFPLKWQS
     SPDGTFIYRK VTLHRTAGTS LGLKVTGGRS TSSGRLGAFI TKVKRGSVAD TVGHLVPGDE
     VFQWNGSLLA NASFDEVCEV INQSKFCNRI ELVIARTIMQ TPFMDEDNYA ASGEVPKHFS
     EQRQLPYRSQ TFGTFPSQAL NLQAASGTLL PDNQTPIVMI TAPLVDMLQL NSNQQQQNRT
     ISGYSTARIS GQIFGQINVS LLYVPDITQL IITVIEAVDL PPRSDGSARN PYVKMFLLPD
     RSEKSRRQSK TMAETCNPVW RQSLVYKEVT FTDLNGKAIE ITVWDYDQYT SNDFLGEVLI
     DLSKANLDNT PFWYTLIDMD EEASLKKKLR HVRPTSASYS KGLPARYDHS HRDLRLSAHS
     NATLPTITSH NVRQKYHDET WATACSSGYR SDSGVAFGSQ EPRHRLSLSH HKPYDNAEMT
     HWEEADPSTS HMSGYYSDYT SHRRSRSGRR YAKNVQSVFP LELRPNSPTE ESGNETSSPS
     HVISGSLRRL PHPPPSLRDG CDRKIELKYS SKKSSSDQVE DRANIVTGDY LSDGSETSIS
     MPSTRSERLI GSQMIVKNIT RERSLDEEHM PRSSPSVNNN SSSHHYSTHV KQESAEAGGF
     YETTTENNYK TCNATVEQIP TTDKRKKSLM TRLIPGRVTA AQLAQEQKRV VFRRSDEVGV
     PVNLSPQTSL DITKQSSRES TDSNESSLVP VAHEPGSIGE FVDGLGPGQV VGRQAVASPC
     LGEIQISLYE RRSNLEVRII RARHLNRKPG SKFYPSPYVK VYLCDEKSVV AKAKTGLAAR
     TPEPRFDQLL IFTEAYHNRL LQVILVGDYG RIERKSVIGL AMIRLSNLDL TKPIEGWYKL
     YHSG
//
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