ID   STRP1_PONAB             Reviewed;         837 AA.
AC   Q5R7S4; Q5NVH6;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 2.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Striatin-interacting protein 1;
DE   AltName: Full=Protein FAM40A;
GN   Name=STRIP1; Synonyms=FAM40A;
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] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 46-837 (ISOFORM 2).
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=2;
CC         IsoId=Q5R7S4-1; Sequence=Displayed;
CC       Name=1;
CC         IsoId=Q5R7S4-2; Sequence=VSP_014943;
CC   -!- SIMILARITY: Belongs to the STRIP family. {ECO:0000305}.
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; CR860035; CAH92186.1; -; Unassigned_RNA.
DR   EMBL; CR926057; CAI29687.1; -; mRNA.
DR   AlphaFoldDB; Q5R7S4; -.
DR   SMR; Q5R7S4; -.
DR   STRING; 9601.ENSPPYP00000001226; -.
DR   eggNOG; KOG3680; Eukaryota.
DR   InParanoid; Q5R7S4; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; ISS:UniProtKB.
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; Alternative splicing; Cytoplasm; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..837
FT                   /note="Striatin-interacting protein 1"
FT                   /id="PRO_0000187020"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..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"
FT   VAR_SEQ         179..196
FT                   /note="VGTFNALVELLNMEIDNG -> NS (in isoform 1)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_014943"
FT   CONFLICT        343
FT                   /note="S -> L (in Ref. 1; CAH92186)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        445
FT                   /note="M -> I (in Ref. 1; CAH92186)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   837 AA;  95471 MW;  F8D181B00CBF7888 CRC64;
     MEPAAGGPGP LIVNNKQPQP PPPPPPATAQ PPPGAPRAAA GLLPGGKARE FNRNQRKDSE
     GYSESPDLEF EYADTDKWAA ELSELYSYTE GPEFLMNRKC FEEDFRIHVT DKKWTELDTN
     QHRTHAMRLL DGLEVTAREK RLKVARAILY VAQGTFGECS SEAEVQSWMR YNIFLLLEVG
     TFNALVELLN MEIDNGAACS SAVRKPAISL ADSTDLRVLL NIMYLIVETV HQECEGDKAE
     WSTMRQTFRA ELGSPLYNNE PFAIMLFGMV TKFCSGHAPH FPMKKVLLLL WKTVLCTLGG
     FEELQSMKAE KRSILGLPPL PEDSIKVIRN MRAASPPASA SDSIEQQQKR GRREHKALIK
     QDNLDAFNER DPYKADDSRE EEEENDDDNS LEGETFPLER DEVMPPPLQH PQTDRLTCPK
     GLPWAPKVRE KDIEMFLESS RSKFMGYTLG SDTNTVVGLP RPIHESIKTL KQHKYTSIAE
     VQAQMEEEYL RSPLSGGEEE VEQVPAETLY QGLLPSLPQY MIALLKILLA AAPTSKAKTD
     SINILADVLP EEMPTTVLQS MKLGVDVNRH KEVIVKAISA VLLLLLKHFK LNHVYQFEYM
     AQHLVFANCI PLILKFFNQN IMSYITAKNS ISVLDYPHCV VHELPELTAE SLEAGDSNQF
     CWRNLFSCIN LLRILNKLTK WKHSRTMMLV VFKSAPILKR ALKVKQAMMQ LYVLKLLKVQ
     TKYLGRQWRK SNMKTMSAIY QKVRHRLNDD WAYGNDLDAR PWDFQAEECA LRANIERFNA
     RRYDRAHSNP DFLPVDNCLQ SVLGQRVDLP EDFQMNYDLW LEREVFSKPI SWEELLQ