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STRP1_BOVIN
ID   STRP1_BOVIN             Reviewed;         837 AA.
AC   Q0P5J8;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Striatin-interacting protein 1;
DE   AltName: Full=Protein FAM40A;
GN   Name=STRIP1; Synonyms=FAM40A;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal skin;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of striatin-interacting phosphatase and kinase
CC       (STRIPAK) complex. Interacts with CDC42BPB. Interacts with CTTNBP2NL.
CC       {ECO:0000250|UniProtKB:Q5VSL9, ECO:0000250|UniProtKB:Q8C079}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Enriched on the
CC       plasma membrane. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the STRIP family. {ECO:0000305}.
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DR   EMBL; BC119950; AAI19951.1; -; mRNA.
DR   RefSeq; NP_001068964.1; NM_001075496.1.
DR   AlphaFoldDB; Q0P5J8; -.
DR   SMR; Q0P5J8; -.
DR   STRING; 9913.ENSBTAP00000027922; -.
DR   PaxDb; Q0P5J8; -.
DR   PRIDE; Q0P5J8; -.
DR   GeneID; 511120; -.
DR   KEGG; bta:511120; -.
DR   CTD; 85369; -.
DR   eggNOG; KOG3680; Eukaryota.
DR   HOGENOM; CLU_011008_1_0_1; -.
DR   InParanoid; Q0P5J8; -.
DR   OrthoDB; 1095402at2759; -.
DR   TreeFam; TF314205; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
DR   InterPro; IPR040185; Far11/STRP.
DR   InterPro; IPR021819; Far11/STRP_C.
DR   InterPro; IPR012486; Far11/STRP_N.
DR   PANTHER; PTHR13239; PTHR13239; 1.
DR   Pfam; PF11882; DUF3402; 2.
DR   Pfam; PF07923; N1221; 1.
DR   SMART; SM01293; DUF3402; 1.
DR   SMART; SM01292; N1221; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..837
FT                   /note="Striatin-interacting protein 1"
FT                   /id="PRO_0000345020"
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"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VSL9"
FT   MOD_RES         59
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VSL9"
FT   MOD_RES         335
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VSL9"
FT   MOD_RES         339
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C079"
FT   MOD_RES         788
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VSL9"
SQ   SEQUENCE   837 AA;  95687 MW;  F4390C01C918987D CRC64;
     MEPAAGTPGP LIMNNKQPQP PPPPPPATAQ PPPGAPRTAG GLLPGGKARE FNRNQRKDSE
     GYSESPDLEF EYADTDKWAA ELSELYSYTE GPEFLMNRKC FEEDFRMHVT DKKWTELDTN
     QHRTHAMRLL DGLEVTAREK RLKVARAILY VAQGTFGECS SEAEVQSWMR YNTFLLLEVG
     TFNALVELLN MEIDNSAACS SAVRKPAISL ADSTDLRVLL NIMYLIVETV HQECEGDKAE
     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
 
 
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