ID F1S614_PIG Unreviewed; 837 AA.
AC F1S614;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Striatin-interacting protein 1 {ECO:0000256|ARBA:ARBA00039625};
DE AltName: Full=Protein FAM40A {ECO:0000256|ARBA:ARBA00041446};
GN Name=STRIP1 {ECO:0000313|Ensembl:ENSSSCP00000007267.3,
GN ECO:0000313|VGNC:VGNC:93576};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000007267.3, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000007267.3, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000007267.3,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HDA51509.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000007267.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Plays a role in the regulation of cell morphology and
CC cytoskeletal organization. Required in the cortical actin filament
CC dynamics and cell shape. {ECO:0000256|ARBA:ARBA00037760}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the STRIP family.
CC {ECO:0000256|ARBA:ARBA00007062}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQIR01096033; HDA51509.1; -; Transcribed_RNA.
DR EMBL; DQIR01137176; HDA92652.1; -; Transcribed_RNA.
DR EMBL; DQIR01206782; HDB62259.1; -; Transcribed_RNA.
DR RefSeq; XP_003125904.3; XM_003125856.5.
DR STRING; 9823.ENSSSCP00000007267; -.
DR PaxDb; 9823-ENSSSCP00000007267; -.
DR Ensembl; ENSSSCT00000007463.5; ENSSSCP00000007267.3; ENSSSCG00000006813.5.
DR GeneID; 100510902; -.
DR KEGG; ssc:100510902; -.
DR CTD; 85369; -.
DR VGNC; VGNC:93576; STRIP1.
DR eggNOG; KOG3680; Eukaryota.
DR GeneTree; ENSGT00400000022095; -.
DR HOGENOM; CLU_011008_1_0_1; -.
DR OMA; FKQHYEL; -.
DR OrthoDB; 5491701at2759; -.
DR TreeFam; TF314205; -.
DR Proteomes; UP000008227; Chromosome 4.
DR Bgee; ENSSSCG00000006813; Expressed in oocyte and 42 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IEA:Ensembl.
DR InterPro; IPR040185; Far11/STRP.
DR InterPro; IPR021819; Far11/STRP_C.
DR InterPro; IPR012486; Far11/STRP_N.
DR PANTHER; PTHR13239; PROTEIN REQUIRED FOR HYPHAL ANASTOMOSIS HAM-2; 1.
DR PANTHER; PTHR13239:SF7; STRIATIN-INTERACTING PROTEIN 1; 1.
DR Pfam; PF11882; DUF3402; 2.
DR Pfam; PF07923; N1221; 1.
DR SMART; SM01293; DUF3402; 1.
DR SMART; SM01292; N1221; 1.
PE 1: Evidence at protein level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1S614};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT DOMAIN 65..363
FT /note="Far11/STRP N-terminal"
FT /evidence="ECO:0000259|SMART:SM01292"
FT DOMAIN 460..817
FT /note="Far11/STRP C-terminal"
FT /evidence="ECO:0000259|SMART:SM01293"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..33
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..392
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 837 AA; 95638 MW; D8D0DD5C2223BB28 CRC64;
MEPALGGPGP LIMNNKQPQP PPPPPPAVAQ PPPGAPRAGG GLLPGGKARE FNRNQRKDSE
GYSESPDLEF EYADTDKWAA ELSELYSYTE GPEFLMNRKC FEEDFRMHVT DKKWTELDTN
QHRTHAMRLL DGLEVTAREK RLKVARAILY VAQGTFGECS SEAEVQSWMR YNVFLLLEVG
TFNALVELLN MEIDNSAACS SAVRKPAISL ADSTDLRVLL NIMYLIVETV HEECEGDKAE
WRTMRQTFRA ELGSPLYNNE PFAIMLFGMV TKFCSGHAPH FPMKKVLLLL WKTVLCTLGG
FEELQSMKAE KRAILGLPPL PEDSIKVIRN MRAASPPASA SDLIEQQQKR GRREHKALIK
QDNLDAFNER DPYKADDSRE EEEENDDDNS LEGETFPLER DEVMPPPLQH PQTDRLTCPK
GLPWAPKVRE KDIEMFLESS RSKFIGYTLG SDTNTVVGLP RPIHESIKTL KQHKYTSIAE
VQAQMEEEYL RSPLSGGEEE VEQVPAETLY QGLLPSLPQY MIALLKILLA AAPTSKAKTD
SINILADVLP EEMPTTVLQS MKLGVDVNRH KEVIVKAISA VLLLLLKHFK LNHVYQFEYM
AQHLVFANCI PLILKFFNQN IMSYITAKNS ISVLDYPHCV VHELPELTAE SLEAGDNNQF
CWRNLFSCIN LLRILNKLTK WKHSRTMMLV VFKSAPILKR ALKVKQAMMQ LYVLKLLKVQ
TKYLGRQWRK SNMKTMSAIY QKVRHRLNDD WAYGNDLDAR PWDFQAEECA LRANIERFNA
RRYDRAHSNP DFLPVDNCLQ SVLGQRVDLP EDFQMNYDLW LEREVFSKPI SWEELLQ
//
