ID A0A3Q1IQL2_ANATE Unreviewed; 1512 AA.
AC A0A3Q1IQL2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSATEP00000022735.2};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000022735.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000022735.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR STRING; 64144.ENSATEP00000022735; -.
DR Ensembl; ENSATET00000023106.2; ENSATEP00000022735.2; ENSATEG00000015705.2.
DR GeneTree; ENSGT00940000161905; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0098793; C:presynapse; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019992; F:diacylglycerol binding; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR CDD; cd20859; C1_Munc13-2-like; 1.
DR CDD; cd08394; C2A_Munc13; 1.
DR CDD; cd04027; C2B_Munc13; 1.
DR Gene3D; 1.10.357.50; -; 1.
DR Gene3D; 1.20.58.1100; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 3.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR010439; MUN_dom.
DR InterPro; IPR014770; Munc13_1.
DR InterPro; IPR014772; Munc13_dom-2.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR027080; Unc-13.
DR InterPro; IPR037302; Unc-13_C2B.
DR PANTHER; PTHR10480; PROTEIN UNC-13 HOMOLOG; 1.
DR PANTHER; PTHR10480:SF1; PROTEIN UNC-13 HOMOLOG A; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00168; C2; 3.
DR Pfam; PF06292; MUN; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00239; C2; 3.
DR SMART; SM01145; DUF1041; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 3.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR PROSITE; PS50004; C2; 3.
DR PROSITE; PS51258; MHD1; 1.
DR PROSITE; PS51259; MHD2; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..98
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 419..469
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 525..649
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 955..1098
FT /note="MHD1"
FT /evidence="ECO:0000259|PROSITE:PS51258"
FT DOMAIN 1198..1337
FT /note="MHD2"
FT /evidence="ECO:0000259|PROSITE:PS51259"
FT DOMAIN 1350..1466
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 178..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1512 AA; 172385 MW; FF2685D64303DF01 CRC64;
FVPLCVSTVK KAKLDGPQEK FNTYVTLKVQ NVKSTTIAVR GNSPSWEQDF MFEINRLDLG
LTVEMWNKGL IWDTMVGTVW IPLSSIRQSN EEGPGEWLTL DSQVIMTDNE ICGTKDPTLH
LVLLDTRFEL PLDIPEDEAR YWAKKLEQLN AMRDQDIILF FCHFFMCLCL DEDPDSAVDD
RDSDYRSETS TSIPPPYYST SQPNASVHQY PISHQHRNSR SFSYPRSGNS HELDYHHQRT
VSYASSAELS RCSSQLSEED YGGEYGERDP YDENDSYHSC HSSVSYSKGS PDWDPDETQG
AYSDEGGYSK DGGEERALYE EDDGGLYEGE EEGLYEDEEM MYDDEDLMGG ALYSIDSMPD
LRKRKAIPLV RDLSLVQNSR KAGITSAMAS TTLGNEELKS HVYKKTLQAL IYPISSTTPH
NFEVWTATTP TYCYECEGLL WGIARQGMRC SECGVKCHEK CQDLLNADCL QRAAEKSSKH
GAEDRTQNII MVLKDRMKIR ERNKPEIFEL IQEVFGLDKA THATHMKQIK QSVLDGTSKW
SAKISITVVC AQGLQAKDKT GSSDPYVTVQ VGKTKKRTKT IYGNLNPVWE ESFHFECHNS
SDRIKVRVWD EDDDIKSRVK QRFKRESDDF LGQTIIEVRT LSGEMDVWYN LDKRTDKSAV
SGAIRMHISV EIKGEETVAP YHVQYTCLHE HLFQYTTEEQ NGGVVKIPDA KGDDAWKVYF
DETAQEIVDE FAMRYGVESI YQAMTHFACL SSKYMCPGVP AVMSTLLANI NAYYAHTTQS
SNNVSASDRF AASNFGKERF VKLLDQLHNS LRIDLSMYRN NFPASSPERL QDLKSTVDLL
TSITFFRMKV QELQSPPRAS QVVKDCVKAC LNSTYEYIFN NCHDLYNREY QTDPYPNYEQ
GPSIKNLDFW SKLITLIVSI IEEDKNSYTP CLNQFPQELN VGKISAEVMW NMFAQDMKYA
MEEHEKHRLC KSADYMNLHF KVKWLYNEYC KELPTFQKHV PDYPAWFEPF VIMWLDENEE
VSRDFLHGAL ERDKKDGFQV TSEHALFSCS VVDVFSQLNQ SFEIIRKLEC PDPQIVGNYM
KRFAKTIGNV LLSYADIIAK DFPNHVKKEK VPCIIINNIQ QLRVQLEKMF EAMGGKDASD
FLKELQNKLN SVMDDLSHIF AVSFQPQIED NVRQMGDILA QVKGQTVPAN GSVVQEADNV
LQPIMDFLDS NLSLFAKICE KTVLKRVLKE LWKLVMNTME KTIVLPTLTD QTMIFNAAKE
LGQLSKLKEH MGREEAKALT PKQCAVIELA LDTIKQYFHA GGVGLKKTFL EKSPDLQSLR
YALSLYTQAT DKLIRKFVLS QNAQTSGVDA VGEVVMNVDI LPQPNGEHKI SVKVVAANDL
KWKAQGFRPF VEVYIIGPHL SDKKRKFATK SKNNGFIIKN PPVGPESYEL QVCVKDYCFA
REDRTVGMAV LQVKDIANKS SVTCWLPLGR RVHMDETGLT VLRILSQRNN DDVAKEFVKL
KSDQRSAEEG HS
//
