SYTL1_MOUSE
ID SYTL1_MOUSE Reviewed; 567 AA.
AC Q99N80; Q99J26;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2003, sequence version 2.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Synaptotagmin-like protein 1;
DE AltName: Full=Exophilin-7;
GN Name=Sytl1; Synonyms=Slp1;
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], 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 [LARGE SCALE MRNA].
RC TISSUE=Mammary cancer;
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 [3]
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).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB27A, AND TISSUE
RP SPECIFICITY.
RX PubMed=18266782; DOI=10.1111/j.1600-0854.2008.00714.x;
RA Holt O., Kanno E., Bossi G., Booth S., Daniele T., Santoro A., Arico M.,
RA Saegusa C., Fukuda M., Griffiths G.M.;
RT "Slp1 and Slp2-a localize to the plasma membrane of CTL and contribute to
RT secretion from the immunological synapse.";
RL Traffic 9:446-457(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Binds phosphatidylinositol 3,4,5-trisphosphate (By
CC similarity). May play a role in vesicle trafficking. Acts as a RAB27A
CC effector protein and may play a role in cytotoxic granule exocytosis in
CC lymphocytes. {ECO:0000250, ECO:0000269|PubMed:18266782}.
CC -!- SUBUNIT: Monomer. Binds NCF2 and NRXN1 (By similarity). Binds RAB27A
CC that has been activated by GTP-binding via its N-terminus.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000269|PubMed:18266782}; Peripheral membrane protein
CC {ECO:0000269|PubMed:18266782}. Cell membrane
CC {ECO:0000269|PubMed:18266782}.
CC -!- TISSUE SPECIFICITY: Highly expressed in lung. Detected at lower levels
CC in spleen, liver and kidney, and at very low levels in heart, brain and
CC skeletal muscle. Expressed in cytotoxic T-lymphocytes (CTL).
CC {ECO:0000269|PubMed:18266782}.
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DR EMBL; AB050741; BAB32651.1; -; mRNA.
DR EMBL; BC005623; AAH05623.1; -; mRNA.
DR AlphaFoldDB; Q99N80; -.
DR SMR; Q99N80; -.
DR IntAct; Q99N80; 2.
DR STRING; 10090.ENSMUSP00000030674; -.
DR iPTMnet; Q99N80; -.
DR PhosphoSitePlus; Q99N80; -.
DR EPD; Q99N80; -.
DR MaxQB; Q99N80; -.
DR PaxDb; Q99N80; -.
DR PRIDE; Q99N80; -.
DR ProteomicsDB; 263197; -.
DR MGI; MGI:1933365; Sytl1.
DR eggNOG; KOG1028; Eukaryota.
DR InParanoid; Q99N80; -.
DR Reactome; R-MMU-8854214; TBC/RABGAPs.
DR PRO; PR:Q99N80; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q99N80; protein.
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:0042470; C:melanosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042043; F:neurexin family protein binding; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IDA:UniProtKB.
DR CDD; cd04020; C2B_SLP_1-2-3-4; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR010911; Rab_BD.
DR InterPro; IPR028378; Sytl1.
DR InterPro; IPR043567; SYTL1-5_C2B.
DR PANTHER; PTHR45716:SF3; PTHR45716:SF3; 1.
DR Pfam; PF00168; C2; 2.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50916; RABBD; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Exocytosis; Membrane; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..567
FT /note="Synaptotagmin-like protein 1"
FT /id="PRO_0000190212"
FT DOMAIN 31..87
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT DOMAIN 271..390
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 403..532
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 103..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYJ3"
FT CONFLICT 178
FT /note="H -> Q (in Ref. 1; BAB32651)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 567 AA; 62362 MW; 13ACC780131F65FB CRC64;
MPQRGHPSQE RLWALPSLPM AHGPGSEVEG LLDLSFLTEE EQEAISDVLK RDAHLRQLEE
GRVSKLRASL EDPWQLKILT GDWFQEARSQ RHHHAHFGSD LVRASIRRKK SPKGDQALGS
DGEAEAAGED TIEGEPESRV SIEVAAPERS TETQGPDLSS PYVPSKASEG QEEEPQDHEC
ELEAPGEGGV QVAEADPELD PEQKAEQESQ PTPAQSKATS KILENGEEAP GLGPSLDRML
SSSSSVSSLN SSTLSGSLMS LSGEEAGTVQ VRGSVLFSLH YEPGTSELRV QVIQCQGLAA
ARRRRSDPYV KSYLLPDKQS KRKTSVKKRN LNPIFNETLR HSVQQADLPG RVLSLSVWHR
ESLGRNIFLG EVEVPLDTWN WDSEATWLPL QPRVPPSPDE LPSRGLLSLS LKYVPAGSEG
GGQPQSGELH FWVKEAQSLV PLRPGSLDTY IQCSVLPDDS RASRQRTRVV RRSLSPVFNH
TMVYDGFGPA DLRQACAELS LWDHGALASR QLGGTRLSLG TGSSYGLQVP WMDSTPEEKQ
LWQTLLERPC EWVDGLLPLR TNLVPRA
