SYTL3_MOUSE
ID SYTL3_MOUSE Reviewed; 607 AA.
AC Q99N48; Q3KQQ0; Q8C506; Q99N47; Q99N49; Q99N54; Q99N79;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Synaptotagmin-like protein 3;
DE AltName: Full=Exophilin-6;
GN Name=Sytl3; Synonyms=Slp3;
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 [MRNA] (ISOFORM 3), INTERACTION WITH PHOSPHOLIPIDS,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH NRXN1.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=11243866; DOI=10.1006/bbrc.2001.4512;
RA Fukuda M., Mikoshiba K.;
RT "Synaptotagmin-like protein 1-3: a novel family of C-terminal-type tandem
RT C2 proteins.";
RL Biochem. Biophys. Res. Commun. 281:1226-1233(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=11327731; DOI=10.1006/bbrc.2001.4803;
RA Fukuda M., Saegusa C., Mikoshiba K.;
RT "Novel splicing isoforms of synaptotagmin-like proteins 2 and 3:
RT identification of the Slp homology domain.";
RL Biochem. Biophys. Res. Commun. 283:513-519(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary gland, and Salivary gland;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [5]
RP MUTAGENESIS OF 336-GLU-GLU-337 AND 359-LYS--LYS-361, AND INTERACTION WITH
RP PHOSPHOLIPIDS.
RX PubMed=12049610; DOI=10.1042/bj20020484;
RA Fukuda M.;
RT "The C2A domain of synaptotagmin-like protein 3 (Slp3) is an atypical
RT calcium-dependent phospholipid-binding machine: comparison with the C2A
RT domain of synaptotagmin I.";
RL Biochem. J. 366:681-687(2002).
RN [6]
RP INTERACTION WITH RAB27A.
RX PubMed=11773082; DOI=10.1074/jbc.m112414200;
RA Kuroda T.S., Fukuda M., Ariga H., Mikoshiba K.;
RT "The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2
RT functions as a novel Rab27A binding domain.";
RL J. Biol. Chem. 277:9212-9218(2002).
CC -!- FUNCTION: May act as Rab effector protein and play a role in vesicle
CC trafficking. Binds phospholipids in the presence of calcium ions.
CC -!- SUBUNIT: Monomer. Binds NRXN1. Binds RAB27A that has been activated by
CC GTP-binding via its N-terminus.
CC -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Slp3-a;
CC IsoId=Q99N48-1; Sequence=Displayed;
CC Name=2; Synonyms=Slp3-a + 3S-I;
CC IsoId=Q99N48-2; Sequence=VSP_007895;
CC Name=3; Synonyms=Slp3-b, Slp3-a delta 3S-II;
CC IsoId=Q99N48-3; Sequence=VSP_007896;
CC Name=4; Synonyms=Slp3-b + 3S-III;
CC IsoId=Q99N48-4; Sequence=VSP_007897;
CC Name=5;
CC IsoId=Q99N48-5; Sequence=VSP_007898, VSP_007899;
CC -!- TISSUE SPECIFICITY: Highly expressed in spleen and lung. Detected at
CC lower levels in heart and testis. {ECO:0000269|PubMed:11327731}.
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DR EMBL; AB050743; BAB32653.1; -; mRNA.
DR EMBL; AB057758; BAB41086.1; -; mRNA.
DR EMBL; AB057764; BAB41092.1; -; mRNA.
DR EMBL; AB057765; BAB41093.1; -; mRNA.
DR EMBL; AB057766; BAB41094.1; -; mRNA.
DR EMBL; BC022608; AAH22608.1; -; mRNA.
DR EMBL; BC106102; AAI06103.1; -; mRNA.
DR EMBL; AK079850; BAC37766.1; -; mRNA.
DR CCDS; CCDS28372.2; -. [Q99N48-1]
DR CCDS; CCDS28374.3; -. [Q99N48-2]
DR RefSeq; NP_113572.1; NM_031395.2. [Q99N48-1]
DR RefSeq; NP_899226.2; NM_183370.2. [Q99N48-2]
DR RefSeq; XP_006523322.1; XM_006523259.2. [Q99N48-1]
DR RefSeq; XP_006523324.1; XM_006523261.3. [Q99N48-2]
DR RefSeq; XP_006523326.1; XM_006523263.1. [Q99N48-2]
DR RefSeq; XP_006523327.1; XM_006523264.1. [Q99N48-2]
DR RefSeq; XP_011244483.1; XM_011246181.2. [Q99N48-1]
DR RefSeq; XP_017173221.1; XM_017317732.1.
DR AlphaFoldDB; Q99N48; -.
DR SMR; Q99N48; -.
DR IntAct; Q99N48; 2.
DR STRING; 10090.ENSMUSP00000125469; -.
DR iPTMnet; Q99N48; -.
DR PhosphoSitePlus; Q99N48; -.
DR EPD; Q99N48; -.
DR jPOST; Q99N48; -.
DR PaxDb; Q99N48; -.
DR PRIDE; Q99N48; -.
DR ProteomicsDB; 254848; -. [Q99N48-1]
DR ProteomicsDB; 254849; -. [Q99N48-2]
DR ProteomicsDB; 254850; -. [Q99N48-3]
DR ProteomicsDB; 254851; -. [Q99N48-4]
DR ProteomicsDB; 254852; -. [Q99N48-5]
DR Antibodypedia; 33442; 111 antibodies from 20 providers.
DR DNASU; 83672; -.
DR Ensembl; ENSMUST00000097430; ENSMUSP00000095041; ENSMUSG00000041831. [Q99N48-1]
DR GeneID; 83672; -.
DR KEGG; mmu:83672; -.
DR UCSC; uc008ahq.2; mouse. [Q99N48-1]
DR CTD; 94120; -.
DR MGI; MGI:1933367; Sytl3.
DR VEuPathDB; HostDB:ENSMUSG00000041831; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000160610; -.
DR HOGENOM; CLU_002711_0_0_1; -.
DR InParanoid; Q99N48; -.
DR OMA; RKKKCNP; -.
DR PhylomeDB; Q99N48; -.
DR BioGRID-ORCS; 83672; 9 hits in 72 CRISPR screens.
DR ChiTaRS; Sytl3; mouse.
DR PRO; PR:Q99N48; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q99N48; protein.
DR Bgee; ENSMUSG00000041831; Expressed in lumbar dorsal root ganglion and 65 other tissues.
DR ExpressionAtlas; Q99N48; baseline and differential.
DR Genevisible; Q99N48; MM.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
DR GO; GO:0042043; F:neurexin family protein binding; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IDA:MGI.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IDA:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR CDD; cd04020; C2B_SLP_1-2-3-4; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR041282; FYVE_2.
DR InterPro; IPR010911; Rab_BD.
DR InterPro; IPR043567; SYTL1-5_C2B.
DR InterPro; IPR028704; SYTL3.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45716:SF1; PTHR45716:SF1; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF02318; FYVE_2; 1.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50916; RABBD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; Reference proteome; Repeat.
FT CHAIN 1..607
FT /note="Synaptotagmin-like protein 3"
FT /id="PRO_0000190215"
FT DOMAIN 4..123
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT DOMAIN 305..430
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 458..590
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 221..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..296
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11327731"
FT /id="VSP_007897"
FT VAR_SEQ 1..214
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11243866,
FT ECO:0000303|PubMed:11327731"
FT /id="VSP_007896"
FT VAR_SEQ 1..195
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11327731,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007895"
FT VAR_SEQ 111..114
FT /note="NVKI -> ANGR (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007898"
FT VAR_SEQ 115..607
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007899"
FT MUTAGEN 336..337
FT /note="EE->QQ: Binds phospholipids only in the absence of
FT divalent cations."
FT /evidence="ECO:0000269|PubMed:12049610"
FT MUTAGEN 359..361
FT /note="KRK->QQQ: Binds phospholipids only in the absence of
FT divalent cations."
FT /evidence="ECO:0000269|PubMed:12049610"
FT CONFLICT 229
FT /note="Q -> R (in Ref. 1; BAB32653)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 607 AA; 68568 MW; F9F404D2D77A6351 CRC64;
MAHEVDLESF KELERDIILR VLYRDQTVQS TEEERVRKLK SHLQHLRWKG AKSSSQEYKE
KCCARCQRAL GLLLNRGAVC QGCSHRVCSE CRVFLRRTRA WKCTVCFEDR NVKIKTGEWF
FEERARKFPT AGRRETAGAK LLQSYQRLSK ISVVPPTPPP FSESQCSSSS RLQELGHFRG
FNKSVENLFL SVTTQMRKLS KSQNDMTSEK HLLAMDPRQC VGHTERRSQS DTAVNVTSRK
ASTPDILKAF HQEDPKHPPD PVLKQDTPPS SPTHSAVFSG GLRHGSLISI NSTCTEMGNF
DNANVTGEIE FAIHYCVKSC SLEICIKTCK NLAYGEEKKR KCNPYVKTYL LPDRSSQGKR
KTRVQKNTLD PTFEETLKYQ VDPGQLMTRR LQVSVWHLGT LARRVFLGEV ILPLAMWDFK
DSTAQNARWY PLRAKAEKYE ENIPQNNGEL AVRAKLVLPA GPRKPQEAQE GQLALNGQLC
LVVLGAKNLP VRSDGTLNSF VKGCLTLPNQ QKLRVKSPVL KKQACPQWKH SFVFNGVSSS
QLRQSTLELT VWDQAIFGMN DRLLGEARLG SKGGAAGCPD SGSQSKLQWH RVLSSPNLWT
DMTLVLH
