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Q9R0Q1

- SYTL4_MOUSE

UniProt

Q9R0Q1 - SYTL4_MOUSE

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Protein

Synaptotagmin-like protein 4

Gene
Sytl4, Slp4
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri63 – 10543FYVE-typeAdd
BLAST

GO - Molecular functioni

  1. neurexin family protein binding Source: UniProtKB
  2. phospholipid binding Source: MGI
  3. protein binding Source: UniProtKB
  4. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. exocytosis Source: MGI
  2. intracellular protein transport Source: InterPro
  3. multivesicular body sorting pathway Source: Ensembl
  4. negative regulation of insulin secretion Source: MGI
  5. positive regulation of exocytosis Source: Ensembl
  6. positive regulation of protein secretion Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptotagmin-like protein 4
Alternative name(s):
Exophilin-2
Granuphilin
Gene namesi
Name:Sytl4
Synonyms:Slp4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:1351606. Sytl4.

Subcellular locationi

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.1 Publication

GO - Cellular componenti

  1. centrosome Source: Ensembl
  2. endosome Source: Ensembl
  3. extrinsic component of membrane Source: UniProtKB
  4. nucleus Source: Ensembl
  5. secretory granule Source: MGI
  6. transport vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi14 – 141E → A: Abolishes interaction with RAB27A. 1 Publication
Mutagenesisi18 – 181I → A: Abolishes interaction with RAB27A. 1 Publication
Mutagenesisi21 – 211V → A: Abolishes interaction with RAB27A. 1 Publication
Mutagenesisi32 – 321D → A: Abolishes interaction with RAB27A. 1 Publication
Mutagenesisi43 – 431L → A: Strongly reduces interaction with STX1A. 1 Publication
Mutagenesisi118 – 1181W → S: Strongly reduces interaction with RAB27A. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 673673Synaptotagmin-like protein 4PRO_0000190217Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei205 – 2051Phosphoserine By similarity
Modified residuei218 – 2181Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9R0Q1.
PRIDEiQ9R0Q1.

PTM databases

PhosphoSiteiQ9R0Q1.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiQ9R0Q1.
BgeeiQ9R0Q1.
CleanExiMM_SYTL4.
GenevestigatoriQ9R0Q1.

Interactioni

Subunit structurei

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.6 Publications

Protein-protein interaction databases

DIPiDIP-31497N.
IntActiQ9R0Q1. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9R0Q1.
SMRiQ9R0Q1. Positions 10-120, 356-654.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 122119RabBDAdd
BLAST
Domaini360 – 464105C2 1Add
BLAST
Domaini515 – 619105C2 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi306 – 3138Poly-Glu

Sequence similaritiesi

Contains 2 C2 domains.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri63 – 10543FYVE-typeAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG293068.
GeneTreeiENSGT00750000117593.
HOGENOMiHOG000231332.
HOVERGENiHBG054255.
InParanoidiQ9R0Q1.
KOiK17598.
OMAiDWFYDQR.
OrthoDBiEOG7JMGDC.
PhylomeDBiQ9R0Q1.
TreeFamiTF341184.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
3.30.40.10. 1 hit.
InterProiIPR000008. C2_dom.
IPR028694. SYTL4.
IPR010911. Znf_FYVE-typ.
IPR011011. Znf_FYVE_PHD.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR10024:SF9. PTHR10024:SF9. 1 hit.
PfamiPF00168. C2. 2 hits.
PF02318. FYVE_2. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 2 hits.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 2 hits.
SSF57903. SSF57903. 1 hit.
PROSITEiPS50004. C2. 2 hits.
PS50916. RABBD. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9R0Q1-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MSEILDLSFL SEMERDLILG VLQRDEELRK ADEKRIRRLK NELLEIKRKG    50
AKRGSQHYSD RTCARCQEGL GRLIPKSSTC VGCNHLVCRE CRVLESNGSW 100
RCKVCSKEIE LKKATGDWFY DQKVNRFDYR TGSEIIRMSL RQKPAVNKRE 150
TAGQSLLQQT QMGDIWPGRR IIQEQQQREQ SVLFEVPKTR SGKSALEAES 200
ESLDSYTADS DSTSRRDSLD KSGLFPEWKK MSAPKSQVEK EIPPGNQNAV 250
CGDEGDMVFK KNTKKVLRPS EYTKSVIDLR PEDVAQESGI LGDRSKSVPG 300
LSVDMEEEEE EEEDIDHLVK LHRQKLARGS MQSGSSMSTL GSIMSIYSEA 350
GDFGNISVTG KIAFSLKFEQ KTQTLVIHVK ECHQLAYADE AKKRSNPYVK 400
TYLLPDKSRQ GKRKTSIKRD TINPLYDETF RYEISESLLA QRTLQFSVWH 450
HGRFGRNTFL GEAEVHMDSW KLDKKLDHCL PLHGKISTES SPGLPAHKGE 500
LVVSLKYIPA SKLPVGGDRK KSKGGEGGEL QVWIKEAKNL TAAKSGGTSD 550
SFVKGYLLPM RNKASKRKTP VMKKTLSPHY NHTFVYNGVR LEDLQHMCLE 600
LTVWDREPLA SNDFLGGVRL GVGTGISNGE VVDWMDSTGE EVSLWQKMRQ 650
YPGSWAEGTL QLRSSMVKQK LGV 673
Length:673
Mass (Da):76,021
Last modified:May 1, 2000 - v1
Checksum:i2AC218E2A4BE4C8D
GO
Isoform 2 (identifier: Q9R0Q1-2) [UniParc]FASTAAdd to Basket

Also known as: Granuphilin-b

The sequence of this isoform differs from the canonical sequence as follows:
     486-502: ISTESSPGLPAHKGELV → GSVMAKWWTGWIRLVKK
     503-673: Missing.

Show »
Length:502
Mass (Da):57,479
Checksum:i6353F899E39192A4
GO
Isoform 3 (identifier: Q9R0Q1-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:502
Mass (Da):57,285
Checksum:i7EC60E5235FF9B0E
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei486 – 673188ISTES…QKLGV → VVCFKGRSQLASQVNCL in isoform 3. VSP_007902Add
BLAST
Alternative sequencei486 – 50217ISTES…KGELV → GSVMAKWWTGWIRLVKK in isoform 2. VSP_007900Add
BLAST
Alternative sequencei503 – 673171Missing in isoform 2. VSP_007901Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS30388.1. [Q9R0Q1-1]
CCDS72429.1. [Q9R0Q1-2]
RefSeqiNP_001277646.1. NM_001290717.1. [Q9R0Q1-2]
NP_001277647.1. NM_001290718.1. [Q9R0Q1-2]
NP_001277648.1. NM_001290719.1. [Q9R0Q1-3]
NP_038785.1. NM_013757.2. [Q9R0Q1-1]
XP_006528614.1. XM_006528551.1. [Q9R0Q1-1]
UniGeneiMm.38674.

Genome annotation databases

EnsembliENSMUST00000033608; ENSMUSP00000033608; ENSMUSG00000031255. [Q9R0Q1-1]
ENSMUST00000113294; ENSMUSP00000108919; ENSMUSG00000031255. [Q9R0Q1-3]
ENSMUST00000113297; ENSMUSP00000108922; ENSMUSG00000031255. [Q9R0Q1-2]
GeneIDi27359.
KEGGimmu:27359.
UCSCiuc009ufe.1. mouse. [Q9R0Q1-1]
uc009uff.1. mouse. [Q9R0Q1-2]
uc009ufh.2. mouse. [Q9R0Q1-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS30388.1. [Q9R0Q1-1 ]
CCDS72429.1. [Q9R0Q1-2 ]
RefSeqi NP_001277646.1. NM_001290717.1. [Q9R0Q1-2 ]
NP_001277647.1. NM_001290718.1. [Q9R0Q1-2 ]
NP_001277648.1. NM_001290719.1. [Q9R0Q1-3 ]
NP_038785.1. NM_013757.2. [Q9R0Q1-1 ]
XP_006528614.1. XM_006528551.1. [Q9R0Q1-1 ]
UniGenei Mm.38674.

3D structure databases

ProteinModelPortali Q9R0Q1.
SMRi Q9R0Q1. Positions 10-120, 356-654.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-31497N.
IntActi Q9R0Q1. 3 interactions.

PTM databases

PhosphoSitei Q9R0Q1.

Proteomic databases

PaxDbi Q9R0Q1.
PRIDEi Q9R0Q1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000033608 ; ENSMUSP00000033608 ; ENSMUSG00000031255 . [Q9R0Q1-1 ]
ENSMUST00000113294 ; ENSMUSP00000108919 ; ENSMUSG00000031255 . [Q9R0Q1-3 ]
ENSMUST00000113297 ; ENSMUSP00000108922 ; ENSMUSG00000031255 . [Q9R0Q1-2 ]
GeneIDi 27359.
KEGGi mmu:27359.
UCSCi uc009ufe.1. mouse. [Q9R0Q1-1 ]
uc009uff.1. mouse. [Q9R0Q1-2 ]
uc009ufh.2. mouse. [Q9R0Q1-3 ]

Organism-specific databases

CTDi 94121.
MGIi MGI:1351606. Sytl4.

Phylogenomic databases

eggNOGi NOG293068.
GeneTreei ENSGT00750000117593.
HOGENOMi HOG000231332.
HOVERGENi HBG054255.
InParanoidi Q9R0Q1.
KOi K17598.
OMAi DWFYDQR.
OrthoDBi EOG7JMGDC.
PhylomeDBi Q9R0Q1.
TreeFami TF341184.

Miscellaneous databases

NextBioi 305228.
PROi Q9R0Q1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9R0Q1.
Bgeei Q9R0Q1.
CleanExi MM_SYTL4.
Genevestigatori Q9R0Q1.

Family and domain databases

Gene3Di 2.60.40.150. 2 hits.
3.30.40.10. 1 hit.
InterProi IPR000008. C2_dom.
IPR028694. SYTL4.
IPR010911. Znf_FYVE-typ.
IPR011011. Znf_FYVE_PHD.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
PANTHERi PTHR10024:SF9. PTHR10024:SF9. 1 hit.
Pfami PF00168. C2. 2 hits.
PF02318. FYVE_2. 1 hit.
[Graphical view ]
SMARTi SM00239. C2. 2 hits.
SM00184. RING. 1 hit.
[Graphical view ]
SUPFAMi SSF49562. SSF49562. 2 hits.
SSF57903. SSF57903. 1 hit.
PROSITEi PS50004. C2. 2 hits.
PS50916. RABBD. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiSYTL4_MOUSE
AccessioniPrimary (citable) accession number: Q9R0Q1
Secondary accession number(s): B1AVI8
, B1AVI9, Q8R321, Q9R0Q0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi