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Protein

Shootin-1

Gene

Shtn1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the generation of internal asymmetric signals required for neuronal polarization and neurite outgrowth (PubMed:17030985, PubMed:17439943, PubMed:18519736, PubMed:20664640). Mediates netrin-1-induced F-actin-substrate coupling or 'clutch engagement' within the axon growth cone through activation of CDC42, RAC1 and PAK1-dependent signaling pathway, thereby converting the F-actin retrograde flow into traction forces, concomitantly with filopodium extension and axon outgrowth (PubMed:18519736, PubMed:23453953). Plays a role in cytoskeletal organization by regulating the subcellular localization of phosphoinositide 3-kinase (PI3K) activity at the axonal growth cone (PubMed:17030985). Plays also a role in regenerative neurite outgrowth (PubMed:20664640). In the developing cortex, cooperates with KIF20B to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. Involved in the accumulation of phosphatidylinositol 3,4,5-trisphosphate (PIP3) in the growth cone of primary hippocampal neurons (By similarity).By similarity5 Publications

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • cell adhesion molecule binding Source: UniProtKB

GO - Biological processi

  • actin filament bundle retrograde transport Source: UniProtKB
  • axonogenesis Source: HGNC
  • Cdc42 protein signal transduction Source: UniProtKB
  • cytoplasmic actin-based contraction involved in cell motility Source: UniProtKB
  • endoplasmic reticulum polarization Source: UniProtKB
  • netrin-activated signaling pathway Source: UniProtKB
  • positive regulation of axon extension Source: UniProtKB
  • positive regulation of neuron migration Source: UniProtKB
  • Ras protein signal transduction Source: UniProtKB
  • regulation of establishment of cell polarity Source: UniProtKB
  • substrate-dependent cell migration, cell extension Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Names & Taxonomyi

Protein namesi
Recommended name:
Shootin-1Imported
Alternative name(s):
Shootin11 Publication
Gene namesi
Name:Shtn1Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1311558. Shtn1.

Subcellular locationi

GO - Cellular componenti

  • axon Source: UniProtKB
  • axonal growth cone Source: UniProtKB
  • cell leading edge Source: UniProtKB
  • cytosol Source: Reactome
  • filopodium Source: UniProtKB
  • growth cone Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • microtubule associated complex Source: UniProtKB
  • microtubule cytoskeleton Source: UniProtKB
  • perikaryon Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi101 – 1011S → A: Inhibits F-actin retrograde flow at the peripheral region of growth cones; when associated with A-249. 1 Publication
Mutagenesisi101 – 1011S → D: Does not inhibit F-actin retrograde flow at the peripheral region of growth cones; when associated with D-249. 1 Publication
Mutagenesisi249 – 2491S → A: Inhibits F-actin retrograde flow at the peripheral region of growth cones; when associated with A-101. 1 Publication
Mutagenesisi249 – 2491S → D: Does not inhibit F-actin retrograde flow at the peripheral region of growth cones; when associated with D-101. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 633633Shootin-1PRO_0000295743Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei3 – 31PhosphoserineBy similarity
Modified residuei4 – 41PhosphoserineBy similarity
Modified residuei101 – 1011Phosphoserine; by PAK11 Publication
Modified residuei249 – 2491Phosphoserine; by PAK11 Publication
Modified residuei375 – 3751PhosphoserineBy similarity
Modified residuei494 – 4941PhosphoserineBy similarity
Modified residuei496 – 4961PhosphothreonineBy similarity
Modified residuei506 – 5061PhosphoserineCombined sources
Modified residuei515 – 5151PhosphoserineBy similarity
Modified residuei537 – 5371PhosphothreonineBy similarity

Post-translational modificationi

Phosphorylated on Ser-101 and Ser-249 by PAK1 through a CDC42- and RAC1-dependent signaling pathway, which enhances its association with F-actin retrograde flow in filopodia and lamellipodia of axonal growth cones (PubMed:23453953). Phosphorylation on Ser-101 and Ser-249 is increased by netrin-1 (PubMed:23453953).1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiA0MZ67.
PRIDEiA0MZ67.

PTM databases

PhosphoSiteiA0MZ67.

Expressioni

Tissue specificityi

Brain-specific (at protein level) (PubMed:17030985). Expressed in hippocampal neurons (PubMed:18519736).2 Publications

Developmental stagei

Expressed in hippocampal neurons at 18 dpc (PubMed:23408951). Expressed at high level both in hippocampal neurons and in brain, during the period of axon formation and elongation. Accumulates in axonal growth cones during the stage 2/3 transition. Accumulates asymmetrically in a single neurite before polarization, while it is depleted in its sibling neurites, through competitive transport to multiple neurites. Transported anterogradely to the growth cones and diffused back to the soma (at protein level) (PubMed:17030985).2 Publications

Inductioni

Up-regulated by axonal regeneration (PubMed:20664640).1 Publication

Interactioni

Subunit structurei

Interacts with PFN2. Interacts (via N-terminus) with KIF20B; this interaction is direct and promotes the association of SHTN1 to microtubules in primary neurons. Associates with microtubule (By similarity). Interacts with L1CAM; this interaction occurs in axonal growth cones (PubMed:18519736). Interacts with actin filament retrograde flow; this interaction is enhanced in a netrin-1- and PAK1-dependent manner and promotes F-actin-substrate coupling and concomitant formation of traction forces at axonal growth cones (PubMed:18519736, PubMed:23453953). Interacts with RUFY3 (PubMed:17030985).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Pik3r1Q637872EBI-1392040,EBI-518443

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • cell adhesion molecule binding Source: UniProtKB

Protein-protein interaction databases

IntActiA0MZ67. 1 interaction.
STRINGi10116.ENSRNOP00000061843.

Structurei

3D structure databases

ProteinModelPortaliA0MZ67.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili7 – 353347Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi353 – 36917Pro-richAdd
BLAST

Domaini

The N-terminus region is necessary for interaction with actin retrograde filament flow and accumulation in neuronal growth cones (PubMed:18519736).1 Publication

Sequence similaritiesi

Belongs to the shootin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFIH. Eukaryota.
ENOG4111HDU. LUCA.
HOGENOMiHOG000154318.
HOVERGENiHBG108488.
InParanoidiA0MZ67.
PhylomeDBiA0MZ67.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: A0MZ67-1) [UniParc]FASTAAdd to basket

Also known as: Shootin2

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

        10         20         30         40         50
MNSSDEEKQL QLITSLKEQA IGEYEDLRAE NQKTKETCDK IRQERDEAVK
60 70 80 90 100
KLEEFQKISH MVIEEVNFMQ NHLEIEKTCR ESAEALATKL NKENKTLKRI
110 120 130 140 150
SMLYMAKLGP DVITEEINID DDDPGTDTDA AAETCVSVQC QKQIKELRDQ
160 170 180 190 200
IVSVQEEKKV LAIELESLKS KLGEVMEEVN KVKQEKAVLN SEVLEQRKVL
210 220 230 240 250
EKCNRVSVLA VEEYEELQVN LELEKDLRKK AESFAQEMFI EQNKLKRQSH
260 270 280 290 300
LLLQSSLPDQ QLLKALDENA KLIQQLEEER IQHQQKVKEL EERLENEALH
310 320 330 340 350
KEIHNLRQQL ELLEDDKREL EQKYQSSEEK ARNLKHSVDE LQKRVNQSEN
360 370 380 390 400
SVPPPPPPPP PLPPPPPNPI RSLMSMIRKR SHPSGGSTKK EKATQPETAE
410 420 430 440 450
EVTDLKRQAV EEMMDRIKKG VHLRPVNQTA RPKAKPDSLK GSESAVDELK
460 470 480 490 500
GILGTLNKST SSRSLKSLGP ENSETELERI LRRRKLTAEA DSSSPTGILA
510 520 530 540 550
TSESKSMPVL GSVSSVTKSA LNKKTLEAEF NNPCPLTPEP GEGPRKLEGC
560 570 580 590 600
TNSKVTFQPP SKGGYRRKCV GSENQSEPVV VLDPVSTHEP QTKDQAAEKD
610 620 630
PTQCKEEERG ETQPEFKEDS SGGKTGETDS SNC
Length:633
Mass (Da):71,446
Last modified:December 12, 2006 - v1
Checksum:i7E982A943E7E98C5
GO
Isoform 2 (identifier: A0MZ67-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     454-456: GTL → ASQ
     457-633: Missing.

Show »
Length:456
Mass (Da):52,436
Checksum:i2F8CD963708BBCC9
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei454 – 4563GTL → ASQ in isoform 2. 1 PublicationVSP_027056
Alternative sequencei457 – 633177Missing in isoform 2. 1 PublicationVSP_027057Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF055485 mRNA. Translation: ABK56020.1.
EF055488 mRNA. Translation: ABK56023.1.
RefSeqiNP_001073173.2. NM_001079705.4. [A0MZ67-1]
NP_001290466.1. NM_001303537.1. [A0MZ67-2]
UniGeneiRn.16095.

Genome annotation databases

GeneIDi292139.
KEGGirno:292139.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF055485 mRNA. Translation: ABK56020.1.
EF055488 mRNA. Translation: ABK56023.1.
RefSeqiNP_001073173.2. NM_001079705.4. [A0MZ67-1]
NP_001290466.1. NM_001303537.1. [A0MZ67-2]
UniGeneiRn.16095.

3D structure databases

ProteinModelPortaliA0MZ67.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiA0MZ67. 1 interaction.
STRINGi10116.ENSRNOP00000061843.

PTM databases

PhosphoSiteiA0MZ67.

Proteomic databases

PaxDbiA0MZ67.
PRIDEiA0MZ67.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi292139.
KEGGirno:292139.

Organism-specific databases

CTDi57698.
RGDi1311558. Shtn1.

Phylogenomic databases

eggNOGiENOG410IFIH. Eukaryota.
ENOG4111HDU. LUCA.
HOGENOMiHOG000154318.
HOVERGENiHBG108488.
InParanoidiA0MZ67.
PhylomeDBiA0MZ67.

Miscellaneous databases

NextBioi633831.
PROiA0MZ67.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Shootin1: a protein involved in the organization of an asymmetric signal for neuronal polarization."
    Toriyama M., Shimada T., Kim K.B., Mitsuba M., Nomura E., Katsuta K., Sakumura Y., Roepstorff P., Inagaki N.
    J. Cell Biol. 175:147-157(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RUFY3, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: Sprague-Dawley.
  2. "Shootin2: a splicing variant of shootin1."
    Katsuta K., Toriyama M., Shimada T., Inagaki N.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: Wistar.
  3. "Singar1, a novel RUN domain-containing protein, suppresses formation of surplus axons for neuronal polarity."
    Mori T., Wada T., Suzuki T., Kubota Y., Inagaki N.
    J. Biol. Chem. 282:19884-19893(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Shootin1 interacts with actin retrograde flow and L1-CAM to promote axon outgrowth."
    Shimada T., Toriyama M., Uemura K., Kamiguchi H., Sugiura T., Watanabe N., Inagaki N.
    J. Cell Biol. 181:817-829(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH L1CAM, INTERACTION WITH F-ACTIN, DOMAIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  5. "A diffusion-based neurite length-sensing mechanism involved in neuronal symmetry breaking."
    Toriyama M., Sakumura Y., Shimada T., Ishii S., Inagaki N.
    Mol. Syst. Biol. 6:394-394(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Conversion of a signal into forces for axon outgrowth through Pak1-mediated shootin1 phosphorylation."
    Toriyama M., Kozawa S., Sakumura Y., Inagaki N.
    Curr. Biol. 23:529-534(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH F-ACTIN, PHOSPHORYLATION AT SER-101 AND SER-249, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-101 AND SER-249.
  8. "Synchronous symmetry breaking in neurons with different neurite counts."
    Wissner-Gross Z.D., Scott M.A., Steinmeyer J.D., Yanik M.F.
    PLoS ONE 8:E54905-E54905(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiSHOT1_RAT
AccessioniPrimary (citable) accession number: A0MZ67
Secondary accession number(s): A0MZ64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: December 12, 2006
Last modified: December 9, 2015
This is version 66 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.