ID A0A1S3L0G2_SALSA Unreviewed; 1580 AA.
AC A0A1S3L0G2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Protein unc-13 homolog B-like isoform X4 {ECO:0000313|RefSeq:XP_013984044.1};
GN Name=LOC106563215 {ECO:0000313|RefSeq:XP_013984044.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013984044.1};
RN [1] {ECO:0000313|RefSeq:XP_013984044.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013984044.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_013984044.1; XM_014128569.1.
DR GeneID; 106563215; -.
DR OrthoDB; 5395569at2759; -.
DR Proteomes; UP000087266; Chromosome ssa11.
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 CDD; cd08395; C2C_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:SF8; PROTEIN UNC-13 HOMOLOG B; 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:UP000087266};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..97
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 466..516
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 572..696
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1006..1149
FT /note="MHD1"
FT /evidence="ECO:0000259|PROSITE:PS51258"
FT DOMAIN 1254..1394
FT /note="MHD2"
FT /evidence="ECO:0000259|PROSITE:PS51259"
FT DOMAIN 1408..1535
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 166..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1580 AA; 179369 MW; 3CD8462AAC654A82 CRC64;
MSLLCVRVKK AKLQGSPGKF NSYVTLKVQN VKSTSITVRG DQPCWEQDFM FEINCLDLGL
IVEVWNKGLI WDTMLGTAWI PLKSIRQSEE EGSGDWTFLD AEVLMKADEI YGTKNQTHHQ
VLLDSRFELP FDIPDDEAQY WTGKLDCINT MRIYDEDEVQ RRLMPPTASQ CSLDDHDSAV
DDRDSDYRSE TSNSLPPRYH TTSQPNSSMH QYPMGPQLQN HLDSCTDSMH SFDMDYRDHR
GSSPVESSRF GSSGNLSQTS SQISETGQES APGSGLEESF HSYHSTGFRP SINVQQPTNG
HIPSNGHSVL GKKLGRPCLD VGKNLHGSLK KLDHSVEKRS NKHLRSFHDN GPPLPFSPSR
IHWLKAINKV RDQLQEGRDD EPNSRQAWIK PGGGSGLFGI DSMPDLRKRK PIPLVSDVAM
SLVQARKAGI TSSMAARSSV KDEELKNHVY KKTLQALIYP ISCTTPHNFE VWTATTPTYC
YECEGLLWGI ARQGMRCSEC GVKCHEKCQE LLNADCLQRA AEKSSKHGAE DRTQNIIMAM
KDRMKIRERN KPEIFDMIRD VFVISKAIHA QQMKTIKQSV LDGTSKWSAK ITITVLCAQG
LQAKDKTGSS DPYVTVQVGK TKKRTKTIYG NLNPVWEENF HFECHNSSDR IKVRVWDEDD
DIKSRVKQRL KRESDDFLGQ SIIEVRTLSG EMDVWYNLEK RTDKSAVSGA IRLQISVEIK
GEEKVAPYHV QYTCLHENLF HHSTDILGQG VVRIPDAKGD DAWKVYFDEV SQEIVDEFAM
RYGIESIYQA MTNFACLSSK YMCPGVPAVM STLLANINAF YAHTTASTNV SASDRFSASN
FGKERFVKLL DQLHNSLRID LSTYRNNFPA SSKDRLQDLK STVDLLTSIT FFRMKVQELQ
SPPRASQVVR DCVKACLNST YDYIFNNCQE LYSRQYQLLD THKEDLSLEE QGPSIKNLDF
WPKLITLIVS IVEEDRNSYT PVLSQFPQEL NVGKVCAEVM WMLFSQDMKY AMEEHEKNRL
CKSADYMNLH FKVKWLYNEY VKDLPNFNRV VPDYPSWFLQ FVLQWLDENE YVSMEFMHGA
LERDKKDGFQ QTSEHALFSC SVVDVFTQLN QSFEIIKKLD CPDPKVMAHY SRRFAKTIAK
VLLQYSAILT KSFPSYSDKE KITCVLMNNV QQLRIQLEKM FESMGAKRLD PDASELLNEL
QVKLNNVLDE LSITFGNSFQ VHIDDCMRQM ASLLYQIKGP VNANSRNMVE ADSDNMLRPL
MDFLDSKLTL FATACEKTVL KRVLKELWRI VMSSLEKTIV LPQGNGTFGS QILSAAKELG
QLSKLKDHMA GEAKSLTPKQ CAVIDIALDT IKQYFHAGGN GLKKAFLEKS SELTSLRHAL
SLYTQTTDTL IKTFVTTQHA QGSGVDKPVG EISIQIDLFT HPGTGEHKVT VKVVGANDLK
WQTSGMFRPF VEITMIGPHL SDKKRKFQTK SKNNSWAPKF NETFHFVLGN EDGFECYELQ
MCVKDYCFGR ADRVLGMAVM QLRDVAEKGS VACWCPLGQS VTMDETGLTA MRILSQRSND
EVAKEFVKLK SEMRSAEEGR
//
