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Database: UniProt
Entry: A0A3B3SGS2_9TELE
LinkDB: A0A3B3SGS2_9TELE
Original site: A0A3B3SGS2_9TELE 
ID   A0A3B3SGS2_9TELE        Unreviewed;       372 AA.
AC   A0A3B3SGS2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Parvin alpha {ECO:0000313|Ensembl:ENSPKIP00000029470.1};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000029470.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000029470.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the parvin family.
CC       {ECO:0000256|ARBA:ARBA00005666}.
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DR   AlphaFoldDB; A0A3B3SGS2; -.
DR   STRING; 1676925.ENSPKIP00000029470; -.
DR   Ensembl; ENSPKIT00000010267.1; ENSPKIP00000029470.1; ENSPKIG00000010704.1.
DR   GeneTree; ENSGT00950000183194; -.
DR   OrthoDB; 1328998at2759; -.
DR   Proteomes; UP000261540; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   CDD; cd21337; CH_PARVA_rpt2; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR028433; Parvin.
DR   PANTHER; PTHR12114:SF6; ALPHA-PARVIN; 1.
DR   PANTHER; PTHR12114; PARVIN; 1.
DR   Pfam; PF00307; CH; 2.
DR   PIRSF; PIRSF039131; Parvin; 1.
DR   SMART; SM00033; CH; 2.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   PROSITE; PS50021; CH; 2.
PE   3: Inferred from homology;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        293..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          95..202
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          262..369
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   372 AA;  42314 MW;  3768CD5A09A4CD91 CRC64;
     MATSPQKSPS SPKSPTPKSP PSRKKDDSFL GKLGGTLARR KKAKEVSELQ EEGMNAINLP
     LSPIPFELDP EDTLLEENEV RTMVDPNSRN DPKLQELMKV LIDWINDVLV GERIIVKDLA
     EDLYDGQVLQ KLFEKLEGEK LNVAEVTQSE IAQKQKLQTV LEKINDTLKI STRNIKWNVD
     SIHAKSTVAI LHLLVALSQH FRAPIRLPDH VSIQVVVVQK REGILQSRQV QEEITGNTEA
     LSGRHERDAF DTLFDHAPDK LNVVKKTLIT FVNKHLNKLN LEVSELDTQF ADGVYLVLLM
     GLLEGYFVPL YNFFLTPENF EQKVHNVSFS FELMQDGGLE RPKPRPEDIV NCDLKSTLRV
     LYNLFTKYRN VE
//
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