SRC8_CHICK
ID SRC8_CHICK Reviewed; 563 AA.
AC Q01406;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Src substrate protein p85;
DE AltName: Full=Cortactin;
DE AltName: Full=p80;
GN Name=CTTN1; Synonyms=EMS1, P85.25;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=1922035; DOI=10.1128/mcb.11.10.5113-5124.1991;
RA Wu H., Reynolds A.B., Kanner S.B., Vines R.R., Parsons J.T.;
RT "Identification and characterization of a novel cytoskeleton-associated
RT pp60src substrate.";
RL Mol. Cell. Biol. 11:5113-5124(1991).
CC -!- FUNCTION: Contributes to the organization of the actin cytoskeleton and
CC cell shape (By similarity). Plays a role in the formation of
CC lamellipodia and in cell migration (By similarity). Plays a role in the
CC regulation of neuron morphology, axon growth and formation of neuronal
CC growth cones, and may play a role in the regulation of neuronal spine
CC density (By similarity). Plays a role in focal adhesion assembly and
CC turnover (By similarity). Plays a role in intracellular protein
CC transport and endocytosis, and in modulating the levels of potassium
CC channels present at the cell membrane (By similarity). Plays a role in
CC endocytosis via clathrin-coated pits (By similarity).
CC {ECO:0000250|UniProtKB:Q14247, ECO:0000250|UniProtKB:Q66HL2}.
CC -!- INTERACTION:
CC Q01406; Q8AYS8: KCNMA1; NbExp=2; IntAct=EBI-2530463, EBI-1635766;
CC Q01406; P39054: Dnm2; Xeno; NbExp=2; IntAct=EBI-2530463, EBI-642337;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1922035}.
CC Endoplasmic reticulum {ECO:0000305|PubMed:1922035}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:1922035}. Cell projection,
CC lamellipodium {ECO:0000250}. Cell projection, ruffle {ECO:0000250}.
CC Cell projection, dendritic spine {ECO:0000250}. Cell projection,
CC dendrite {ECO:0000250}. Cell projection {ECO:0000250|UniProtKB:Q66HL2}.
CC Cell junction {ECO:0000250|UniProtKB:Q66HL2}. Membrane, clathrin-coated
CC pit {ECO:0000250|UniProtKB:Q66HL2}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:Q66HL2}. Cell projection, podosome
CC {ECO:0000269|PubMed:1922035}. Note=Colocalizes transiently with
CC PTK2/FAK1 at focal adhesions (By similarity). Associated with membrane
CC ruffles and lamellipodia. In normal cells, probably in association with
CC the plasma membrane and possibly the endoplasmic reticulum
CC (PubMed:1922035). p80/85 colocalizes with F-actin in peripheral
CC extensions of normal cells and rosettes (podosomes) of src-transformed
CC cells. p80/85 probably associates with components of the cytoskeleton.
CC In response to neuronal activation by glutamate, redistributes from
CC dendritic spines to the dendritic shaft (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q66HL2, ECO:0000269|PubMed:1922035}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=p85;
CC IsoId=Q01406-1; Sequence=Displayed;
CC Name=p80;
CC IsoId=Q01406-2; Sequence=VSP_018797;
CC -!- DOMAIN: The SH3 motif may mediate binding to the cytoskeleton.
CC {ECO:0000305}.
CC -!- PTM: In normal cells, appears to be phosphorylated on serine and
CC threonine; in cells expressing activated forms of pp60-src, they become
CC heavily phosphorylated on tyrosine in vitro. Tyrosine phosphorylation
CC in transformed cells may contribute to cellular growth regulation and
CC transformation. {ECO:0000269|PubMed:1922035}.
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DR EMBL; M73705; AAA49031.1; -; mRNA.
DR PIR; A41530; A41530.
DR RefSeq; NP_990799.1; NM_205468.1. [Q01406-1]
DR AlphaFoldDB; Q01406; -.
DR BMRB; Q01406; -.
DR SMR; Q01406; -.
DR BioGRID; 676704; 1.
DR IntAct; Q01406; 2.
DR STRING; 9031.ENSGALP00000012463; -.
DR iPTMnet; Q01406; -.
DR PaxDb; Q01406; -.
DR PRIDE; Q01406; -.
DR GeneID; 396455; -.
DR KEGG; gga:396455; -.
DR CTD; 2017; -.
DR VEuPathDB; HostDB:geneid_396455; -.
DR eggNOG; ENOG502QS6C; Eukaryota.
DR InParanoid; Q01406; -.
DR OrthoDB; 1243441at2759; -.
DR PhylomeDB; Q01406; -.
DR PRO; PR:Q01406; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR GO; GO:0005905; C:clathrin-coated pit; ISS:UniProtKB.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0030863; C:cortical cytoskeleton; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0030427; C:site of polarized growth; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; IEA:InterPro.
DR GO; GO:0048870; P:cell motility; ISS:UniProtKB.
DR GO; GO:0048041; P:focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0097581; P:lamellipodium organization; ISS:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISS:UniProtKB.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:0030516; P:regulation of axon extension; ISS:UniProtKB.
DR CDD; cd11959; SH3_Cortactin; 1.
DR InterPro; IPR015503; Cortactin.
DR InterPro; IPR035716; Cortactin_SH3.
DR InterPro; IPR003134; Hs1_Cortactin.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10829:SF15; PTHR10829:SF15; 3.
DR Pfam; PF02218; HS1_rep; 7.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51090; CORTACTIN; 7.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Cell junction; Cell membrane; Cell projection;
KW Coated pit; Coiled coil; Cytoplasm; Cytoskeleton; Endocytosis;
KW Endoplasmic reticulum; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain; Synapse.
FT CHAIN 1..563
FT /note="Src substrate protein p85"
FT /id="PRO_0000022411"
FT REPEAT 89..125
FT /note="Cortactin 1"
FT REPEAT 126..162
FT /note="Cortactin 2"
FT REPEAT 163..199
FT /note="Cortactin 3"
FT REPEAT 200..236
FT /note="Cortactin 4"
FT REPEAT 237..273
FT /note="Cortactin 5"
FT REPEAT 274..310
FT /note="Cortactin 6"
FT REPEAT 311..333
FT /note="Cortactin 7; truncated"
FT DOMAIN 505..563
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 331..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 349..410
FT /evidence="ECO:0000255"
FT COMPBIAS 335..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..10
FT /note="Missing (in isoform p80)"
FT /evidence="ECO:0000305"
FT /id="VSP_018797"
SQ SEQUENCE 563 AA; 63329 MW; 22A824A08B8D654C CRC64;
MTVLLLVVLQ MWKATAGHSI AVSQDDGADD WETDPDFVND VSEKEQRWGA KTVKGSGHQE
HINIHQLREN VFQEHQTIKE KELETGPKAS HGYGGKFGVE QDRMDKSAVG HEYQSKLSKH
CSQVDSVKGF GGKFGVQTDR VDQSAVGFEY QGKTEKHASQ KDYSSGFGGK YGVQADRVDK
SAVGFDYQGK TEKHESQKDY SKGFGGKYGV DKDKVDKSAV GFEYQGKTEK HESQKDYVKG
FGGKFGVQTD RQDKCALGWD HQEKVQLHES QKDYKSGFGG KFGVQTERQD PSAVGFDYKE
KLAKHESQQD YSKGFGGKYG VQKDRMDKNA ATFEDIEKPT STYQKTKPVE RVANKTSSIR
ANLENLAKEK EQEDRRKAEA ERAQRMAREK QEQEEARRKL EEQAKAKKQT PPPSPTTQPA
EPKTPSSPVY QDAVSYDAES AYKNSSTTYS AEHEPESGYK TTGSDYQEAV SQREAEYEPE
TVYEVAGAGD HYQAEENTYD EYENELGITA IALYDYQAAG DDEISFDPDD IITNIEMIDD
GWWRGVCKGR YGLFPANYVE LRQ
