ESYT3_MOUSE
ID ESYT3_MOUSE Reviewed; 891 AA.
AC Q5DTI8; Q0VF61; Q8C3B9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Extended synaptotagmin-3;
DE Short=E-Syt3;
GN Name=Esyt3; Synonyms=D9Ertd280e, Fam62c, Kiaa4186;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Tethers the endoplasmic reticulum to the cell membrane and
CC promotes the formation of appositions between the endoplasmic reticulum
CC and the cell membrane. Binds glycerophospholipids in a barrel-like
CC domain and may play a role in cellular lipid transport (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A0FGR9};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:A0FGR9}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:A0FGR9}; Multi-pass membrane
CC protein {ECO:0000255}. Note=Localizes to endoplasmic reticulum-plasma
CC membrane contact sites (EPCS). Recruited to the cell membrane via the
CC third C2 domain (By similarity). {ECO:0000250|UniProtKB:A0FGR9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5DTI8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5DTI8-2; Sequence=VSP_030426;
CC -!- DOMAIN: The SMP-LTD domain is a barrel-like domain that binds
CC glycerophospholipids in its interior (By similarity).
CC {ECO:0000250|UniProtKB:A0FGR8}.
CC -!- SIMILARITY: Belongs to the extended synaptotagmin family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC39655.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD90311.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK220532; BAD90311.1; ALT_INIT; mRNA.
DR EMBL; AK086367; BAC39655.1; ALT_FRAME; mRNA.
DR EMBL; BC118967; AAI18968.1; -; mRNA.
DR CCDS; CCDS40739.1; -. [Q5DTI8-1]
DR RefSeq; NP_808443.2; NM_177775.3. [Q5DTI8-1]
DR RefSeq; XP_006511284.1; XM_006511221.3. [Q5DTI8-1]
DR AlphaFoldDB; Q5DTI8; -.
DR SMR; Q5DTI8; -.
DR BioGRID; 234879; 1.
DR IntAct; Q5DTI8; 1.
DR STRING; 10090.ENSMUSP00000038757; -.
DR iPTMnet; Q5DTI8; -.
DR PhosphoSitePlus; Q5DTI8; -.
DR MaxQB; Q5DTI8; -.
DR PaxDb; Q5DTI8; -.
DR PRIDE; Q5DTI8; -.
DR ProteomicsDB; 267659; -. [Q5DTI8-1]
DR ProteomicsDB; 267660; -. [Q5DTI8-2]
DR Antibodypedia; 33435; 63 antibodies from 15 providers.
DR DNASU; 272636; -.
DR Ensembl; ENSMUST00000042158; ENSMUSP00000038757; ENSMUSG00000037681. [Q5DTI8-1]
DR GeneID; 272636; -.
DR KEGG; mmu:272636; -.
DR UCSC; uc009reb.1; mouse. [Q5DTI8-1]
DR CTD; 83850; -.
DR MGI; MGI:1098699; Esyt3.
DR VEuPathDB; HostDB:ENSMUSG00000037681; -.
DR eggNOG; KOG1012; Eukaryota.
DR GeneTree; ENSGT00940000161072; -.
DR HOGENOM; CLU_012047_1_0_1; -.
DR InParanoid; Q5DTI8; -.
DR OMA; AKGFCEP; -.
DR OrthoDB; 52746at2759; -.
DR PhylomeDB; Q5DTI8; -.
DR TreeFam; TF324255; -.
DR Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
DR BioGRID-ORCS; 272636; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Esyt3; mouse.
DR PRO; PR:Q5DTI8; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q5DTI8; protein.
DR Bgee; ENSMUSG00000037681; Expressed in arcuate nucleus of hypothalamus and 128 other tissues.
DR ExpressionAtlas; Q5DTI8; baseline and differential.
DR Genevisible; Q5DTI8; MM.
DR GO; GO:0140268; C:endoplasmic reticulum-plasma membrane contact site; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0031227; C:intrinsic component of endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0044232; C:organelle membrane contact site; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR GO; GO:0008429; F:phosphatidylethanolamine binding; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0061817; P:endoplasmic reticulum-plasma membrane tethering; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd08391; C2A_C2C_Synaptotagmin_like; 1.
DR CDD; cd04050; C2B_Synaptotagmin-like; 1.
DR CDD; cd04030; C2C_KIAA1228; 1.
DR Gene3D; 2.60.40.150; -; 3.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037752; C2C_KIAA1228.
DR InterPro; IPR037733; Ext_Synaptotagmin_C2A.
DR InterPro; IPR037749; Ext_Synaptotagmin_C2B.
DR InterPro; IPR031468; SMP_LBD.
DR InterPro; IPR039010; Synaptotagmin_SMP.
DR Pfam; PF00168; C2; 3.
DR Pfam; PF17047; SMP_LBD; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR SMART; SM00239; C2; 3.
DR SUPFAM; SSF49562; SSF49562; 3.
DR PROSITE; PS50004; C2; 3.
DR PROSITE; PS51847; SMP; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Cell membrane; Endoplasmic reticulum;
KW Lipid transport; Lipid-binding; Membrane; Metal-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..891
FT /note="Extended synaptotagmin-3"
FT /id="PRO_0000314900"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..891
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 118..295
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01194"
FT DOMAIN 292..412
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 430..570
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 759..881
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..813
FT /note="Required for phosphatidylinositol 4,5-bisphosphate-
FT dependent location at the cell membrane"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 387
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..367
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030426"
SQ SEQUENCE 891 AA; 100068 MW; B4F1AC8531024234 CRC64;
MQPEEPCAPS APGGPDVPER GQRSRDPGPR LSGQLLPELY SFVARVLFYL APVYLAGYLG
LSVTWLLLGA LLWMWWRRNR RGKLGRLEAA FEFLEHEREF ISRELRGQHL PAWIHFPDVE
RVEWANKIII QIWPYLSMIM ENKIREKLEP KIREKSIHLR TFTFTKLYFG QKCPKVNGVK
VHTDKRNRRK VTLDLQICYI GDCEISVELQ KIRGGVSGVQ LQGTLRVILE PLLVDKPFIG
AVTVFFLQKP HLQINWTGLT NLLDMPGINE LSDSLLEDLI AAHLVLPNRV TVPVKKGLDV
TNLRVPLPCG VIRVHLLEAK KLAQKDNFLG LGGKSDPYAK VSIGLQHCRS RTIYKNLNPT
WNEVFEFMVY EVPGQDLEVD LYDEDTDKDD FLGSLQICLG DVMKNRVVDE WFALNDTTSG
RLHLRLEWLS LLTDQEALTE NDSGLSTAIL VVFLENACNL PRNPFDYLNG EYRAKKLSRF
VKNKASRDPS SYVKLTVGKK TFTSKTCPHS KDPVWSQVFS FFVHSVAAEQ LCLKVLDDEL
ECALGVLEFP LCRILPCADL TLEQCFQLDH SGLDSLISMR LVLRFLRVEG RELGSPYTGP
DALKKGPLFI KKVATNQGCK APPLNEGLAD VTSTSNPASY IKGASKSIDN ISAATTDPEP
MPEPQGPGPE PKGKDSARGL CESPGKKKNP ATTFLTVPGL HSPGPIKSPR PMSRPAFPFA
WPLTRVAPSM SSLNSLASSC FDLTDVSLNT EAGDSRQGRL GEIQLTVRYV CLRHCLRVLV
NGCRNLTPCT SSGADPYVRI YLLPERRWAS RKKTSVKQKT LEPLFDETFE FFVPMGEVQK
RSLDVAVKNS RPLGSHRRKE LGKVLIDLSK QDLIKGFSQW YELTADGQPR S
