SYTL1_HUMAN
ID SYTL1_HUMAN Reviewed; 562 AA.
AC Q8IYJ3; Q5SSC9; Q96BB6; Q96GU6; Q96S89; Q96SI0;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Synaptotagmin-like protein 1;
DE AltName: Full=Exophilin-7;
DE AltName: Full=Protein JFC1;
GN Name=SYTL1; Synonyms=SLP1; ORFNames=SB146;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Li N., Wan T., Zhang M., Zhang W., Cao X.;
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell, Lung, and Ovary;
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP NCF2.
RC TISSUE=Peripheral blood leukocyte;
RX PubMed=11278853; DOI=10.1074/jbc.m011167200;
RA McAdara Berkowitz J.K., Catz S.D., Johnson J.L., Ruedi J.M., Thon V.,
RA Babior B.M.;
RT "JFC1, a novel tandem C2 domain-containing protein associated with the
RT leukocyte NADPH oxidase.";
RL J. Biol. Chem. 276:18855-18862(2001).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: May play a role in vesicle trafficking (By similarity). Binds
CC phosphatidylinositol 3,4,5-trisphosphate. Acts as a RAB27A effector
CC protein and may play a role in cytotoxic granule exocytosis in
CC lymphocytes (By similarity). {ECO:0000250, ECO:0000269|PubMed:11278853,
CC ECO:0000269|PubMed:18266782}.
CC -!- SUBUNIT: Monomer. Binds NRXN1. Binds RAB27A that has been activated by
CC GTP-binding via its N-terminus (By similarity). Binds NCF2.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q8IYJ3; P51159: RAB27A; NbExp=3; IntAct=EBI-2802861, EBI-716881;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11278853,
CC ECO:0000269|PubMed:18266782}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11278853, ECO:0000269|PubMed:18266782}; Cytoplasmic
CC side {ECO:0000269|PubMed:11278853, ECO:0000269|PubMed:18266782}.
CC Note=Peripheral membrane protein tightly bound to the cytoplasmic side
CC of cellular membranes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IYJ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IYJ3-2; Sequence=VSP_007883;
CC -!- TISSUE SPECIFICITY: Highly expressed in bone marrow and lymphoid
CC tissues. Detected at lower levels in cerebellum, occipital lobe,
CC prostate, stomach, kidney, appendix, lung and trachea. Expressed in
CC cytotoxic T-lymphocytes (CTL). {ECO:0000269|PubMed:11278853,
CC ECO:0000269|PubMed:18266782}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH15764.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY037157; AAK67636.1; -; mRNA.
DR EMBL; AK027902; BAB55444.1; -; mRNA.
DR EMBL; FO393419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009224; AAH09224.2; -; mRNA.
DR EMBL; BC015764; AAH15764.1; ALT_INIT; mRNA.
DR EMBL; BC035725; AAH35725.1; -; mRNA.
DR CCDS; CCDS298.1; -. [Q8IYJ3-2]
DR CCDS; CCDS53286.1; -. [Q8IYJ3-1]
DR RefSeq; NP_001180237.1; NM_001193308.1. [Q8IYJ3-1]
DR RefSeq; NP_116261.1; NM_032872.2. [Q8IYJ3-2]
DR AlphaFoldDB; Q8IYJ3; -.
DR SMR; Q8IYJ3; -.
DR BioGRID; 124389; 14.
DR IntAct; Q8IYJ3; 14.
DR MINT; Q8IYJ3; -.
DR STRING; 9606.ENSP00000440704; -.
DR iPTMnet; Q8IYJ3; -.
DR PhosphoSitePlus; Q8IYJ3; -.
DR BioMuta; SYTL1; -.
DR DMDM; 33301659; -.
DR EPD; Q8IYJ3; -.
DR jPOST; Q8IYJ3; -.
DR MassIVE; Q8IYJ3; -.
DR MaxQB; Q8IYJ3; -.
DR PaxDb; Q8IYJ3; -.
DR PeptideAtlas; Q8IYJ3; -.
DR PRIDE; Q8IYJ3; -.
DR ProteomicsDB; 71187; -. [Q8IYJ3-1]
DR ProteomicsDB; 71188; -. [Q8IYJ3-2]
DR TopDownProteomics; Q8IYJ3-2; -. [Q8IYJ3-2]
DR Antibodypedia; 51546; 100 antibodies from 17 providers.
DR DNASU; 84958; -.
DR Ensembl; ENST00000318074.9; ENSP00000316464.5; ENSG00000142765.18. [Q8IYJ3-2]
DR Ensembl; ENST00000543823.1; ENSP00000440704.1; ENSG00000142765.18. [Q8IYJ3-1]
DR Ensembl; ENST00000616558.5; ENSP00000481032.1; ENSG00000142765.18. [Q8IYJ3-1]
DR GeneID; 84958; -.
DR KEGG; hsa:84958; -.
DR MANE-Select; ENST00000616558.5; ENSP00000481032.1; NM_001193308.2; NP_001180237.1.
DR UCSC; uc001bnv.3; human. [Q8IYJ3-1]
DR CTD; 84958; -.
DR DisGeNET; 84958; -.
DR GeneCards; SYTL1; -.
DR HGNC; HGNC:15584; SYTL1.
DR HPA; ENSG00000142765; Tissue enhanced (esophagus, pancreas).
DR MIM; 608042; gene.
DR neXtProt; NX_Q8IYJ3; -.
DR OpenTargets; ENSG00000142765; -.
DR PharmGKB; PA134921815; -.
DR VEuPathDB; HostDB:ENSG00000142765; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000160932; -.
DR HOGENOM; CLU_002711_4_0_1; -.
DR InParanoid; Q8IYJ3; -.
DR OMA; WFSEECS; -.
DR OrthoDB; 916843at2759; -.
DR PhylomeDB; Q8IYJ3; -.
DR TreeFam; TF341184; -.
DR PathwayCommons; Q8IYJ3; -.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR SignaLink; Q8IYJ3; -.
DR BioGRID-ORCS; 84958; 22 hits in 1075 CRISPR screens.
DR ChiTaRS; SYTL1; human.
DR GeneWiki; SYTL1; -.
DR GenomeRNAi; 84958; -.
DR Pharos; Q8IYJ3; Tbio.
DR PRO; PR:Q8IYJ3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8IYJ3; protein.
DR Bgee; ENSG00000142765; Expressed in granulocyte and 134 other tissues.
DR ExpressionAtlas; Q8IYJ3; baseline and differential.
DR Genevisible; Q8IYJ3; HS.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; ISS:UniProtKB.
DR GO; GO:0031528; C:microvillus membrane; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042043; F:neurexin family protein binding; ISS: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 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 Alternative splicing; Cell membrane; Exocytosis; Membrane; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..562
FT /note="Synaptotagmin-like protein 1"
FT /id="PRO_0000190211"
FT DOMAIN 31..87
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT DOMAIN 266..385
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 398..527
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 154..165
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_007883"
FT CONFLICT 111
FT /note="S -> N (in Ref. 1; AAK67636)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="V -> A (in Ref. 4; AAH15764)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="Q -> R (in Ref. 1; AAK67636 and 4; AAH09224)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 562 AA; 61857 MW; 056BE1F16723EE19 CRC64;
MPQRGHPSQE GLWALPSLPM AHGPKPETEG LLDLSFLTEE EQEAIAGVLQ RDARLRQLEE
GRVSKLRASV ADPGQLKILT GDWFQEARSQ RHHNAHFGSD LVRASMRRKK STRGDQAPGH
DREAEAAVKE KEEGPEPRLT IDEAPQERLR ETEGPDFPSP SVPLKASDPE EASQAQEDPG
QGDQQVCAEE ADPELEPASG GEQEPRPQQA QTKAASQILE NGEEAPGPDP SLDRMLSSSS
SVSSLNSSTL SGSQMSLSGD AEAVQVRGSV HFALHYEPGA AELRVHVIQC QGLAAARRRR
SDPYVKSYLL PDKQSKRKTA VKKRNLNPVF NETLRYSVPQ AELQGRVLSL SVWHRESLGR
NIFLGEVEVP LDTWDWGSEP TWLPLQPRVP PSPDDLPSRG LLALSLKYVP AGSEGAGLPP
SGELHFWVKE ARDLLPLRAG SLDTYVQCFV LPDDSQASRQ RTRVVRRSLS PVFNHTMVYD
GFGPADLRQA CAELSLWDHG ALANRQLGGT RLSLGTGSSY GLQVPWMDST PEEKQLWQAL
LEQPCEWVDG LLPLRTNLAP RT
