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Q9R0Q1 (SYTL4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Synaptotagmin-like protein 4
Alternative name(s):
Exophilin-2
Granuphilin
Gene names
Name:Sytl4
Synonyms:Slp4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length673 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Modulates exocytosis of dense-core granules and secretion of hormones in the pancreas and the pituitary. Interacts with vesicles containing negatively charged phospholipids in a Ca2+-independent manner. Ref.8

Subunit structure

Part of a ternary complex containing STX1A and RAB27A. Can bind both dominant negative and dominant active mutants of RAB27A. Binds STXBP1, RAB3A, RAB8A and RAB27B. Interacts with MYO5A. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8 Ref.10

Subcellular location

Membrane; Peripheral membrane protein. Cytoplasmic vesiclesecretory vesicle membrane; Peripheral membrane protein. Note: Detected close to the plasma membrane and on secretory granules. In pancreas, interacts with insulin-containing vesicles. Ref.1

Tissue specificity

Detected in the pancreatic islet, in particular in insulin-positive beta cells, and in pituitary. Ref.1

Sequence similarities

Contains 2 C2 domains.

Contains 1 FYVE-type zinc finger.

Contains 1 RabBD (Rab-binding) domain.

Ontologies

Keywords
   Cellular componentCytoplasmic vesicle
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processexocytosis

Inferred from direct assay Ref.8. Source: MGI

intracellular protein transport

Inferred from electronic annotation. Source: InterPro

multivesicular body sorting pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of insulin secretion

Inferred from mutant phenotype PubMed 16890542. Source: MGI

positive regulation of exocytosis

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein secretion

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcentrosome

Inferred from electronic annotation. Source: Ensembl

endosome

Inferred from electronic annotation. Source: Ensembl

extrinsic component of membrane

Inferred from direct assay PubMed 11243866. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: Ensembl

secretory granule

Inferred from direct assay Ref.1. Source: MGI

transport vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionneurexin family protein binding

Inferred from direct assay PubMed 11243866. Source: UniProtKB

phospholipid binding

Inferred from direct assay Ref.1. Source: MGI

zinc ion binding

Non-traceable author statement PubMed 11327731. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9R0Q1-1)

Also known as: Granuphilin-a;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9R0Q1-2)

Also known as: Granuphilin-b;

The sequence of this isoform differs from the canonical sequence as follows:
     486-502: ISTESSPGLPAHKGELV → GSVMAKWWTGWIRLVKK
     503-673: Missing.
Isoform 3 (identifier: Q9R0Q1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     486-673: ISTESSPGLP...SSMVKQKLGV → VVCFKGRSQLASQVNCL
Note: May be due to an intron retention. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 673673Synaptotagmin-like protein 4
PRO_0000190217

Regions

Domain4 – 122119RabBD
Domain360 – 464105C2 1
Domain515 – 619105C2 2
Zinc finger63 – 10543FYVE-type
Compositional bias306 – 3138Poly-Glu

Amino acid modifications

Modified residue2051Phosphoserine By similarity
Modified residue2181Phosphoserine Ref.9

Natural variations

Alternative sequence486 – 673188ISTES…QKLGV → VVCFKGRSQLASQVNCL in isoform 3.
VSP_007902
Alternative sequence486 – 50217ISTES…KGELV → GSVMAKWWTGWIRLVKK in isoform 2.
VSP_007900
Alternative sequence503 – 673171Missing in isoform 2.
VSP_007901

Experimental info

Mutagenesis141E → A: Abolishes interaction with RAB27A. Ref.8
Mutagenesis181I → A: Abolishes interaction with RAB27A. Ref.8
Mutagenesis211V → A: Abolishes interaction with RAB27A. Ref.8
Mutagenesis321D → A: Abolishes interaction with RAB27A. Ref.8
Mutagenesis431L → A: Strongly reduces interaction with STX1A. Ref.7
Mutagenesis1181W → S: Strongly reduces interaction with RAB27A. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Granuphilin-a) [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 2AC218E2A4BE4C8D

FASTA67376,021
        10         20         30         40         50         60 
MSEILDLSFL SEMERDLILG VLQRDEELRK ADEKRIRRLK NELLEIKRKG AKRGSQHYSD 

        70         80         90        100        110        120 
RTCARCQEGL GRLIPKSSTC VGCNHLVCRE CRVLESNGSW RCKVCSKEIE LKKATGDWFY 

       130        140        150        160        170        180 
DQKVNRFDYR TGSEIIRMSL RQKPAVNKRE TAGQSLLQQT QMGDIWPGRR IIQEQQQREQ 

       190        200        210        220        230        240 
SVLFEVPKTR SGKSALEAES ESLDSYTADS DSTSRRDSLD KSGLFPEWKK MSAPKSQVEK 

       250        260        270        280        290        300 
EIPPGNQNAV CGDEGDMVFK KNTKKVLRPS EYTKSVIDLR PEDVAQESGI LGDRSKSVPG 

       310        320        330        340        350        360 
LSVDMEEEEE EEEDIDHLVK LHRQKLARGS MQSGSSMSTL GSIMSIYSEA GDFGNISVTG 

       370        380        390        400        410        420 
KIAFSLKFEQ KTQTLVIHVK ECHQLAYADE AKKRSNPYVK TYLLPDKSRQ GKRKTSIKRD 

       430        440        450        460        470        480 
TINPLYDETF RYEISESLLA QRTLQFSVWH HGRFGRNTFL GEAEVHMDSW KLDKKLDHCL 

       490        500        510        520        530        540 
PLHGKISTES SPGLPAHKGE LVVSLKYIPA SKLPVGGDRK KSKGGEGGEL QVWIKEAKNL 

       550        560        570        580        590        600 
TAAKSGGTSD SFVKGYLLPM RNKASKRKTP VMKKTLSPHY NHTFVYNGVR LEDLQHMCLE 

       610        620        630        640        650        660 
LTVWDREPLA SNDFLGGVRL GVGTGISNGE VVDWMDSTGE EVSLWQKMRQ YPGSWAEGTL 

       670 
QLRSSMVKQK LGV 

« Hide

Isoform 2 (Granuphilin-b) [UniParc].

Checksum: 6353F899E39192A4
Show »

FASTA50257,479
Isoform 3 [UniParc].

Checksum: 7EC60E5235FF9B0E
Show »

FASTA50257,285

References

« Hide 'large scale' references
[1]"Novel rabphilin-3-like protein associates with insulin-containing granules in pancreatic beta cells."
Wang J., Takeuchi T., Yokota H., Izumi T.
J. Biol. Chem. 274:28542-28548(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH PHOSPHOLIPIDS.
Tissue: Pancreas.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Pituitary.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Mammary tumor.
[5]"Involvement of Rab27b in the regulated secretion of pituitary hormones."
Zhao S., Torii S., Yokota-Hashimoto H., Takeuchi T., Izumi T.
Endocrinology 143:1817-1824(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB27A AND RAB27B.
[6]"The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domain."
Kuroda T.S., Fukuda M., Ariga H., Mikoshiba K.
J. Biol. Chem. 277:9212-9218(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB27A.
[7]"Granuphilin modulates the exocytosis of secretory granules through interaction with syntaxin 1a."
Torii S., Zhao S., Yi Z., Takeuchi T., Izumi T.
Mol. Cell. Biol. 22:5518-5526(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LEU-43 AND TRP-118, INTERACTION WITH RAB27A AND STX1A.
[8]"Slp4-a/granuphilin-a inhibits dense-core vesicle exocytosis through interaction with the GDP-bound form of Rab27A in PC12 cells."
Fukuda M.
J. Biol. Chem. 278:15390-15396(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLU-14; ILE-18; VAL-21 AND ASP-32, INTERACTION WITH RAB27A; STXBP1; RAB3A AND RAB8A.
[9]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[10]"Structural basis of cargo recognitions for class V myosins."
Wei Z., Liu X., Yu C., Zhang M.
Proc. Natl. Acad. Sci. U.S.A. 110:11314-11319(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYO5A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB025258 mRNA. Translation: BAA84656.1.
AB025259 mRNA. Translation: BAA84657.1.
AK030401 mRNA. Translation: BAC26945.1.
AL691421 Genomic DNA. Translation: CAM17840.1.
AL691421 Genomic DNA. Translation: CAM17841.1.
BC026819 mRNA. Translation: AAH26819.1.
RefSeqNP_038785.1. NM_013757.1.
XP_006528614.1. XM_006528551.1.
XP_006528615.1. XM_006528552.1.
XP_006528616.1. XM_006528553.1.
UniGeneMm.38674.

3D structure databases

ProteinModelPortalQ9R0Q1.
SMRQ9R0Q1. Positions 10-120, 356-654.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-31497N.
IntActQ9R0Q1. 3 interactions.

PTM databases

PhosphoSiteQ9R0Q1.

Proteomic databases

PaxDbQ9R0Q1.
PRIDEQ9R0Q1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033608; ENSMUSP00000033608; ENSMUSG00000031255. [Q9R0Q1-1]
ENSMUST00000113294; ENSMUSP00000108919; ENSMUSG00000031255. [Q9R0Q1-3]
ENSMUST00000113297; ENSMUSP00000108922; ENSMUSG00000031255. [Q9R0Q1-2]
GeneID27359.
KEGGmmu:27359.
UCSCuc009ufe.1. mouse. [Q9R0Q1-1]
uc009uff.1. mouse. [Q9R0Q1-2]
uc009ufh.2. mouse. [Q9R0Q1-3]

Organism-specific databases

CTD94121.
MGIMGI:1351606. Sytl4.

Phylogenomic databases

eggNOGNOG293068.
GeneTreeENSGT00750000117593.
HOGENOMHOG000231332.
HOVERGENHBG054255.
InParanoidQ9R0Q1.
KOK17598.
OMAYDETLRY.
OrthoDBEOG7JMGDC.
PhylomeDBQ9R0Q1.
TreeFamTF341184.

Gene expression databases

ArrayExpressQ9R0Q1.
BgeeQ9R0Q1.
CleanExMM_SYTL4.
GenevestigatorQ9R0Q1.

Family and domain databases

Gene3D2.60.40.150. 2 hits.
3.30.40.10. 1 hit.
InterProIPR000008. C2_dom.
IPR028694. SYTL4.
IPR010911. Znf_FYVE-typ.
IPR011011. Znf_FYVE_PHD.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERPTHR10024:SF9. PTHR10024:SF9. 1 hit.
PfamPF00168. C2. 2 hits.
PF02318. FYVE_2. 1 hit.
[Graphical view]
SMARTSM00239. C2. 2 hits.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 2 hits.
SSF57903. SSF57903. 1 hit.
PROSITEPS50004. C2. 2 hits.
PS50916. RABBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio305228.
PROQ9R0Q1.
SOURCESearch...

Entry information

Entry nameSYTL4_MOUSE
AccessionPrimary (citable) accession number: Q9R0Q1
Secondary accession number(s): B1AVI8 expand/collapse secondary AC list , B1AVI9, Q8R321, Q9R0Q0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot