SHOT1_PONAB
ID SHOT1_PONAB Reviewed; 456 AA.
AC Q5RA03;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Shootin-1 {ECO:0000250|UniProtKB:A0MZ67};
DE AltName: Full=Shootin1 {ECO:0000250|UniProtKB:A0MZ67};
GN Name=SHTN1 {ECO:0000250|UniProtKB:A0MZ66};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the generation of internal asymmetric signals
CC required for neuronal polarization and neurite outgrowth. Mediates
CC netrin-1-induced F-actin-substrate coupling or 'clutch engagement'
CC within the axon growth cone through activation of CDC42, RAC1 and PAK1-
CC dependent signaling pathway, thereby converting the F-actin retrograde
CC flow into traction forces, concomitantly with filopodium extension and
CC axon outgrowth. Plays a role in cytoskeletal organization by regulating
CC the subcellular localization of phosphoinositide 3-kinase (PI3K)
CC activity at the axonal growth cone. Also plays a role in regenerative
CC neurite outgrowth. In the developing cortex, cooperates with KIF20B to
CC promote both the transition from the multipolar to the bipolar stage
CC and the radial migration of cortical neurons from the ventricular zone
CC toward the superficial layer of the neocortex. Involved in the
CC accumulation of phosphatidylinositol 3,4,5-trisphosphate (PIP3) in the
CC growth cone of primary hippocampal neurons.
CC {ECO:0000250|UniProtKB:A0MZ67, ECO:0000250|UniProtKB:Q8K2Q9}.
CC -!- SUBUNIT: Interacts with L1CAM; this interaction occurs in axonal growth
CC cones. Interacts with actin filament retrograde flow; this interaction
CC is enhanced in a netrin-1- and PAK1-dependent manner and promotes F-
CC actin-substrate coupling and concomitant formation of traction forces
CC at axonal growth cones. Interacts with RUFY3. Interacts with PFN2.
CC Interacts (via N-terminus) with KIF20B; this interaction is direct and
CC promotes the association of SHTN1 to microtubules in primary neurons.
CC Associates with microtubule. {ECO:0000250|UniProtKB:A0MZ67,
CC ECO:0000250|UniProtKB:Q8K2Q9}.
CC -!- SUBCELLULAR LOCATION: Perikaryon {ECO:0000250|UniProtKB:Q8K2Q9}. Cell
CC projection, axon {ECO:0000250|UniProtKB:Q8K2Q9}. Cell projection,
CC growth cone {ECO:0000250|UniProtKB:Q8K2Q9}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q8K2Q9}. Cell projection, filopodium
CC {ECO:0000250|UniProtKB:A0MZ67}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:A0MZ67}. Note=Localizes in multiple growth cones
CC at neurite tips before the neuronal symmetry-breaking step. Accumulates
CC in growth cones of a single nascent axon in a neurite length-dependent
CC manner during the neuronal symmetry-breaking step; when absent from the
CC nascent axon's siblings, probably due to competitive transport,
CC prevents the formation of surplus axons. Transported anterogradely from
CC the soma to the axon growth cone in an actin and myosin-dependent
CC manner and passively diffuses back to the cell bodies. Colocalized with
CC L1CAM in close apposition with actin filaments in filopodia and
CC lamellipodia of axonal growth cones in hippocampal neurons. Exhibits
CC retrograde movements in filopodia and lamellopodia of axonal growth
CC cones. Colocalized with KIF20B along microtubules to the tip of the
CC growing cone in primary hippocampal neurons. Recruited to the growth
CC cone of developing axon in a KIF20B- and microtubule-dependent manner.
CC {ECO:0000250|UniProtKB:A0MZ67, ECO:0000250|UniProtKB:Q8K2Q9}.
CC -!- DOMAIN: The N-terminus region is necessary for interaction with actin
CC retrograde filament flow and accumulation in neuronal growth cones.
CC {ECO:0000250|UniProtKB:A0MZ67}.
CC -!- PTM: Phosphorylated on Ser-101 and Ser-249 by PAK1 through a CDC42- and
CC RAC1-dependent signaling pathway, which enhances its association with
CC F-actin retrograde flow in filopodia and lamellipodia of axonal growth
CC cones. Phosphorylation on Ser-101 and Ser-249 is increased by netrin-1.
CC {ECO:0000250|UniProtKB:A0MZ67}.
CC -!- SIMILARITY: Belongs to the shootin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH91407.1; Type=Miscellaneous discrepancy; Note=Wrong translation of mRNA.; Evidence={ECO:0000305};
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DR EMBL; CR859226; CAH91407.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001125828.1; NM_001132356.1.
DR AlphaFoldDB; Q5RA03; -.
DR SMR; Q5RA03; -.
DR STRING; 9601.ENSPPYP00000003137; -.
DR GeneID; 100172756; -.
DR KEGG; pon:100172756; -.
DR CTD; 57698; -.
DR eggNOG; ENOG502QVVT; Eukaryota.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0044295; C:axonal growth cone; ISS:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005875; C:microtubule associated complex; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0061573; P:actin filament bundle retrograde transport; ISS:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR GO; GO:0032488; P:Cdc42 protein signal transduction; ISS:UniProtKB.
DR GO; GO:0060327; P:cytoplasmic actin-based contraction involved in cell motility; ISS:UniProtKB.
DR GO; GO:0061163; P:endoplasmic reticulum polarization; ISS:UniProtKB.
DR GO; GO:0038007; P:netrin-activated signaling pathway; ISS:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB.
DR GO; GO:2001224; P:positive regulation of neuron migration; ISS:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB.
DR GO; GO:0006930; P:substrate-dependent cell migration, cell extension; ISS:UniProtKB.
DR InterPro; IPR024849; Shootin-1.
DR PANTHER; PTHR46606; PTHR46606; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Developmental protein; Phosphoprotein; Reference proteome.
FT CHAIN 1..456
FT /note="Shootin-1"
FT /id="PRO_0000295742"
FT REGION 343..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 7..353
FT /evidence="ECO:0000255"
FT COMPBIAS 350..371
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2Q9"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2Q9"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A0MZ66"
FT MOD_RES 101
FT /note="Phosphoserine; by PAK1"
FT /evidence="ECO:0000250|UniProtKB:A0MZ67"
FT MOD_RES 249
FT /note="Phosphoserine; by PAK1"
FT /evidence="ECO:0000250|UniProtKB:A0MZ67"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A0MZ66"
SQ SEQUENCE 456 AA; 52595 MW; 2C4300F2477DBAF2 CRC64;
MNSSDEEKQL QLITSLKEQA IGEYEDLRAE NQKTKEKCDK IRQERDEAVK KLEEFQKISH
MVIEEVNFMQ NHLEIEKTCR ESAEALATKL NKENKTLKRI SMLYMAKLGP DVITEEINID
DEDSTTDTDG AAETCVSVQC QKQIKELRDQ IVSVQEEKKI LAIELENLKS KLVEVIEEVN
KVKQEKAVLN SEVLEQRKVL EKCNRVSMLA VEEYEEMQVN LELEKDLRKK AESFAQEMFI
EQNKLKRQSH LLLQSSVPDQ QLSKALDENA KLTQQLEEER IQHQQKVKEL KEQLENETLH
KEIHNLKQQL ELLEEDKKEL ELKYQNSEEK ARNLKHSVDE LQKRVNQSEN SVPPPPPPPP
PLPPPPPNPI RSFMSMIRKR SHPSGSGAKK EKATQPETPE EVTDLKRQAV EEMMDRIKKG
VHLRPVNQTA RPKTKPESSK GCESAVDELK GILASQ
