ID A0A091J6N5_CALAN Unreviewed; 1597 AA.
AC A0A091J6N5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 35.
DE SubName: Full=Regulating synaptic membrane exocytosis protein 1 {ECO:0000313|EMBL:KFP07386.1};
DE Flags: Fragment;
GN ORFNames=N300_07828 {ECO:0000313|EMBL:KFP07386.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFP07386.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFP07386.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP07386.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KL218657; KFP07386.1; -; Genomic_DNA.
DR STRING; 9244.A0A091J6N5; -.
DR Proteomes; UP000054308; 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:InterPro.
DR CDD; cd04031; C2A_RIM1alpha; 1.
DR CDD; cd04028; C2B_RIM1alpha; 1.
DR CDD; cd00992; PDZ_signaling; 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; 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:SF18; REGULATING SYNAPTIC MEMBRANE EXOCYTOSIS PROTEIN 1; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF02318; FYVE_2; 1.
DR Pfam; PF00595; PDZ; 1.
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; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054308};
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 15..71
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 509..595
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 646..769
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1443..1561
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 80..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1203..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1238..1301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1316..1400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..870
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..913
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1077
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1346..1378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP07386.1"
FT NON_TER 1597
FT /evidence="ECO:0000313|EMBL:KFP07386.1"
SQ SEQUENCE 1597 AA; 178967 MW; 6DF8463F7501C92A CRC64;
RKIGEEARRY QGEHKDDAPT CGICHKTKFA DGCGHLCSYC RTKFCARCGG RVSLRSNNVM
WVCNLCRKQQ EILTKSGAWF FGSGPQPSPS QDGTLSDTAT GGSSDAPREK KARLQERSRS
QTPLSTAAAS AQEISSSSVQ PDRRKGAEVS QPAMGLDQKP VSSRSRSEPP RERKKTILVS
DQNGKGLKSE RKRVPKSPLP KEGPADDRER KERHEGRRLE KGKSQDYSDF PEKLEEGKVP
DDEKQRKEDE YHTRYRSDPN LARYPVKPHP EEQQMRMHAK VSKARHERRH SDVALPHTEM
EEAEVPENKL GKRSQLQGTQ DRKSLVETQR SYSIDRTGDV RISVSKQLTN HSPPTPRHSP
VPIEHVEYKN HDSFKKQSRL DPSSAILMRK AKREKMETML RNDSLSSDQS ESVRPSPPKP
HRAKRGGKKR QMSVSSSEEE GASTPEYTSC EDVEIESESV SEKGDLDYYW LDPATWHSRE
TSPISSHPVT WQPSKEGDRL IGRVILNKRT TMPKESGALL GLKVVGGKMT ELGRLGAFIT
KVKKGSLADV VGHLRAGDEV LEWNGKPLPG ATNEEVYNII LESKSEPQVE IIVSRPIGDI
PRIPETSHPP LESSSSSFES QKMERPSISV ISPTSPGVLR DAPQVLPGQL SVKLWYDKVG
HQLIVNVLQA TDLPPRVDGR PRNPYVKMYF LPDRSDKSKR RTKTVKKSLE PKWNQTFIYS
HVHRRDFRER MLEITVWDQP RVQEEESEFL GEILIELETA LLDDEPHWYK LQTHDESSLP
LPQPSPFMPR RHVHGGESTS KKLQRSRPIS DSDISDYDVD DGIGVVPPVG YRSSTREGKS
TTLTVPEQQR TTHHRSRSVS PHRGDDQGRP RSRLPNVPLQ RSLDEIHQMR RSRSPTRHHD
ASRTPVDYRS RDMDSQYLSD QESELLMLPR AKRGRSAECL HTIRSSVSHY KTLPPKMPLL
TNGTHWNLYS STLPACAKTK SVIRQDISLL HDCLNSRIPK FGDDLLVSEL QPSLDRARSA
STNCLRPDTS LHSPERERGR LSPSLERRRP TSPRIHIQHA SPEDDRQSRK VERYSSQKQT
RKVSATETER GLPPCLSRRG LPTPRTTEQP GIRGKHHTRS RSSEHSSVRP LCTVHHLQPG
GSAPPSPLLT RIHQQGSPTQ SPPADTSFSS RRGRQLPQVP VRSGSIEQAS LVVEERTRQL
KMKVHRYNQT SGSGSSQEHE REQYTKYNIQ TDQYRSCDNV SAKSSDSDVS DVSAISRTSS
ASRLSSTSFM SEQSERPRGR ISTFTPKMQG RRMGTPGRIT KSTSVSGEIY KLEHNDGSQS
DTAVGMVGTG GKKRRSSLSA KVVAIVSRRS RSTSQLSQTE AGSKKLKSTI QRSTETGMAA
EMRSRMVRQP SRESTDGSIN SYSSEGNLIF PGVRLGADSQ FSDFLDGLGP AQLVGRQTLA
TPAMGDIQIG MVDKKGQLEV EVIRARGLTQ KPGSKSTPAP YVKVYLLENG ACIAKKKTRI
ARKTLDPLYQ QTLVFDESPQ GKVLQVIVWG DYGRMDHKCF MGVAQILLEE LDLSSVVIGW
YKLFPPSSLV DPTLTPLTRR ASQSSLESST GPPCIRS
//
