ID A0A2G5SV73_9PELO Unreviewed; 1128 AA.
AC A0A2G5SV73;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 13-SEP-2023, entry version 29.
DE RecName: Full=Rab-3-interacting molecule unc-10 {ECO:0008006|Google:ProtNLM};
GN Name=Cni-unc-10 {ECO:0000313|EMBL:PIC19034.1};
GN Synonyms=Cnig_chr_X.g24718 {ECO:0000313|EMBL:PIC19034.1};
GN ORFNames=B9Z55_024718 {ECO:0000313|EMBL:PIC19034.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC19034.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) 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:PIC19034.1}.
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DR EMBL; PDUG01000006; PIC19034.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5SV73; -.
DR Proteomes; UP000230233; Chromosome x.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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; IPR000595; cNMP-bd_dom.
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; IPR017455; Znf_FYVE-rel.
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 Pfam; PF02318; FYVE_2; 1.
DR Pfam; PF00595; PDZ; 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; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50916; RABBD; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 7..133
FT /note="RabBD"
FT /evidence="ECO:0000259|PROSITE:PS50916"
FT DOMAIN 66..121
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 631..721
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 764..846
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 827..949
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 27..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1073
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1128 AA; 127623 MW; 7B599512959C6E04 CRC64;
MDDPSLMPDL SHLSAEEREI IEQVFRRQRD EEAKETQASQ AATEELSSLE KQITERKETS
RKLVGTQDDA ICQICQKTKF ADGIGHKCFY CQLRSCARCG GRAQSKNKAI WACSLCQKRQ
QILAKTGKWF QPEEQAQQKI SVSEASPSPQ PLTQTPDHNG PPTQLQPRQT EPPDKIDQNF
QPNQQQRAMH GPQQTNGPIQ NGPHQNGPSQ NGPTHNQNHQ GNHHPQNNRR QMQQQQSVNQ
NHAPMNQNQQ NFRNQAGPPN QNQNQNQRPV DNRNMRGNQM QQQQQQQNQF QGNMVGNNQP
FQQQQQQHGP QQPGPSHHQQ MGEQQQQQQQ HRMDNNRMRE NHNGHGGMFN NKQPSLERTT
STNKYNQGRV DEDSMNQQQR PTFYAGNGEN DQRQYDGQNM NSNSNSHGQN QNQNQIQNQN
QNQNLRKNQG NRVTEEDYAS SSVFESKKQR NHNSQVPSTS QGVRAVPPND DHLNRVKNRL
HRQLRSMSSS EEDIIAGGGG NTLKMSTSAV VAAGGKTAFH DDMGASNVQR LSEECNSEKD
LLRYIYGDHK NPDSSSLSSS GPVSGGNSVL KNMQTNRRRD KSLSVSPSRN DHFGGTGSIS
GGELLASRIR TILAHPVTWQ PTSDQKRLIG HMVLHRTENS AANGDLGLKI VGGRRTDTGK
LGAFITQVKP GSVADTIGRL RPGDEVVEWN GQSLQNATYE QVYDSIAASR YDTQVDMIVS
RNAILPGGDD FFNIPSSQMS SSTYSRVPST YPSQYSRQLP NPELFLDLHP ALQQQLLSHS
QSAVFPHNST LTSRNRSTSS YYYSEVPDLG VPHTRELSDQ TFGTGHIFGR IELSFVYSHH
ERQLSVALTR GFDLPPRSDG TPRNPYVKIF LLPDRSEKSR RQSAVIAETL MPVWDEVFYY
NGLTEPMLLQ RVLELTVWDY DKFGTNSFLG ETLIDLAAVP LDGEHSLMCV LVDMDDDNPL
RTRLKLRKAS YNAPVRRPQS ELNYYDQSHH YYNHISQNMD KPSHHHVLGA MNDEENDEYI
DDDELENDID LATGGAARKS RAYRREKGLH GGHGYADWTQ NNPRQSGYTS DHGYGRQTMM
GGGGGRTYNR RQQRRPRSAT ALSQMERDEM YDPTRKHREE DEYSMRET
//
