ID   STRP1_DANRE             Reviewed;         813 AA.
AC   Q803T2;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Striatin-interacting protein 1 homolog;
GN   Name=strip1; Synonyms=fam40a;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18307296; DOI=10.1021/pr700667w;
RA   Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA   Slijper M., Heck A.J.R.;
RT   "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT   analysis down to a single embryo.";
RL   J. Proteome Res. 7:1555-1564(2008).
CC   -!- FUNCTION: May play 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. {ECO:0000250}.
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; BC044205; AAH44205.1; -; mRNA.
DR   AlphaFoldDB; Q803T2; -.
DR   SMR; Q803T2; -.
DR   STRING; 7955.ENSDARP00000103366; -.
DR   iPTMnet; Q803T2; -.
DR   PaxDb; Q803T2; -.
DR   ZFIN; ZDB-GENE-040426-2927; strip1.
DR   eggNOG; KOG3680; Eukaryota.
DR   InParanoid; Q803T2; -.
DR   PhylomeDB; Q803T2; -.
DR   PRO; PR:Q803T2; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; 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:0060047; P:heart contraction; IMP:ZFIN.
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   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..813
FT                   /note="Striatin-interacting protein 1 homolog"
FT                   /id="PRO_0000187021"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          307..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..41
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..352
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..368
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         310
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18307296"
SQ   SEQUENCE   813 AA;  93600 MW;  B97EA4014450F20C CRC64;
     MDGVGLCANN KQKQNQMLPN KMRGEFTRNQ RKDSEGLSEA PDLEFEYSDA DKWTAELSEL
     YSYTEGPEFL LNRKCFEEDF HTHLPDQKWT ELDSVQRRAH AMRLLDGLEV IGRERRLKVA
     RAILYMAQGT FGECSSELEV QHWMRYNVFL LLDVGAFTAL VELLNMEIDN SAACSSAVRK
     PAISLADSTD LRVLLNIMYL MVETIQREEP TDSPEWRTIR ETFKSELGSP LYNHEPVSVM
     LFGMVTKFCS GHAPHFPMKK VLLLLWKTIL FTLGGFEQLQ SCKISRRAAL GLPPLPEDSI
     RVVRSMRAAS PPASASDLIE QQQRRARREH KALIKQDNLD TFNEKDPYKA DDSHEDEEEN
     DDNDNSLEAE PFPLERDEVM PPPIPHPPTE RMCFPKGLPW APKVREKDIE SFLESSRSKF
     IGYTLGNDTD TVVGLPRPIH ESIKTLKQHK YVSIAEVQIA KEEAFQKTPL SGGEEELELC
     ATELLYQGIL PSLPQYMIAL LKILLAAAPT SKAKTDSINI LADVLPEEMP TTVLQSMKLG
     VDVNRHKEII VKAISAILLL LLKHFKLNHV YQFEYMAQHL VFANCIPLIL KFFNQNIMSY
     ITAKNSISAL DFPHCVIHEL PELTAESLEA GDNNQFCWRN LFSCINLLRI LNKLTKWKHS
     RTMMLVVFKS APILKRALKV KQAMMQLYVL KLLKVQTKYL GRQWRKGNMK TMSAIYQKVR
     HRLNDDWAYG NDLDARPWDF QAEECALRAN IERFNSRRYD KNQSNPEFLP VDNCLQSVLG
     QRIDLPEDFQ MNYDLWLERE VFSKPISWEE LLQ