ID A0A091DB53_FUKDA Unreviewed; 1322 AA.
AC A0A091DB53;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Regulating synaptic membrane exocytosis protein 2 {ECO:0000313|EMBL:KFO20056.1};
GN ORFNames=H920_18562 {ECO:0000313|EMBL:KFO20056.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO20056.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO20056.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO20056.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN124863; KFO20056.1; -; Genomic_DNA.
DR STRING; 885580.ENSFDAP00000021718; -.
DR eggNOG; KOG2060; Eukaryota.
DR eggNOG; KOG3799; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
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:UniProtKB-KW.
DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
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; IPR041282; FYVE_2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
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; REGULATING SYNAPTIC MEMBRANE EXOCYTOSIS PROTEIN; 1.
DR PANTHER; PTHR12157:SF15; REGULATING SYNAPTIC MEMBRANE EXOCYTOSIS PROTEIN 2; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF02318; FYVE_2; 1.
DR Pfam; PF17820; PDZ_6; 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.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Neurotransmitter transport {ECO:0000256|ARBA:ARBA00022775};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Transport {ECO:0000256|ARBA:ARBA00022775};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 81..137
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 632..718
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 769..892
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 150..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..937
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1008
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1046
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1095
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1322 AA; 150007 MW; 3C4C76D28B78D626 CRC64;
MNKKTFNLHC YSFGYSVTLF AYLNRWFPFS GITELVNNVL QPQQKQQNEK EPQTKLHQQF
EMYKEQVKKM GEESQQQQEQ KGDAPTCGIC HKTKFADGCG HNCSYCQTKF CARCGGRVSL
RSNKVMWVCN LCRKQQEILT KSGAWFYNSG SHIPQQPDQR APRGVRNEEA PQEKKAKLQE
QAQFQGRPGD LSVPAVERSR SRGLTRQESI KDGAGVRHQT ASDTSSDRKR SPSVSRDQKR
RYDQREESEE YPQYAPPDSA MPRSPSDYAE RRPQREPQFY EESDHLSYRG SNRRSHRHSK
EYIVEDEDVE SRDEHDRQRR EEEYQARYRS DPNLARYPVK PQPYEEQMRI HAEVSRARHE
RRHSDVSLAN AELEDSRVSL LRMDRPSRQR SVSERRAAME NQKSYSMERT REAQGQSSYP
PRTTNRSPPT PRRSPVPIDR PDLRRTDSLR KQHHLDPSSA VRKTKREKME TMLRNDSLSS
DQSESVRPPP PKPHKSKKGG KIRQVSLSSS EEELASTPEY TSCDDVEIES ESVSEKGDSQ
KGKRKISEQA VLSDSNTRSE RQKKMMYFGG HSLEEDLDWS EPQIKDSGVD TCSSTTLNEE
HSHRDKHPVT WQPSKDGDRL IGRILLNKRL KDGSVPRDSG AMLGLKVVGG KMTESGRLCA
FITKVKKGSL ADTVGHLRPG DEVLEWNGRL LQGATFEEVY NIILESKPEP QVELVVSRPI
GDIPRIPDST HAQLESSSSS FESQKMDRPS ISVTSPMSPG MLRDVPQFLS GQLSIKLWFD
KVGHQLIVTI LGAKDLPSRE DGRPRNPYVK IYFLPDRSDK NKRRTKTVKK TLEPKWNQTF
IYSPVHRREF RERMLEITLW DQARVREEES EFLGEILIEL ETALLDDEPH WYKLQTHDVS
SLPLPHPSPY LPRRQLHEDS PTRRLQRSKR ISDSEISDYD CDDGIGVVSD YRHNDQDLQS
STLSVPEQVM SSSHCAPSGS PHRVDALGRT RSWSPSVPPP QSRNVEQGLR GTRMAPGHYN
TVGRMERHRV VDDHYSPERD SHFLTLPRSR HSQSNGHRHR DCEAADRQPY HRSRPTEPRP
LLERTTTRSR STERPDSNLM RSMPSLMTGR SAPPSPALSR SHPRTGSAQT SPSSTPAAAR
RGRQLPQLPP KGTLERRWDP HRGADNISTK SSDSDVSDIS AVSRTSSASR FSSTSYMSVQ
SERPRGNKKR SVFTSKMQSR QTGVPGKSVT KSTSVSGDLC PLDKNDGSQS DTAVGALGAG
GKKRRSSIGA KVVAIVGLSR KSRSASQLGQ TAWREEEPPG LEVTPSLLLT ARLPLQSVAA
LT
//
