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Database: UniProt
Entry: A0A2Y9JE85_ENHLU
LinkDB: A0A2Y9JE85_ENHLU
Original site: A0A2Y9JE85_ENHLU 
ID   A0A2Y9JE85_ENHLU        Unreviewed;       468 AA.
AC   A0A2Y9JE85;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Chimaerin {ECO:0000256|PIRNR:PIRNR038015};
DE   AltName: Full=Chimerin {ECO:0000256|PIRNR:PIRNR038015};
GN   Name=LOC111147263 {ECO:0000313|RefSeq:XP_022358901.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022358901.1};
RN   [1] {ECO:0000313|RefSeq:XP_022358901.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022358901.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: GTPase-activating protein for p21-rac.
CC       {ECO:0000256|PIRNR:PIRNR038015}.
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DR   RefSeq; XP_022358901.1; XM_022503193.1.
DR   AlphaFoldDB; A0A2Y9JE85; -.
DR   STRING; 391180.A0A2Y9JE85; -.
DR   KEGG; elk:111147263; -.
DR   OrthoDB; 5395569at2759; -.
DR   Proteomes; UP000248482; Unplaced.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:UniProtKB-UniRule.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd20857; C1_betaCHN; 1.
DR   CDD; cd04372; RhoGAP_chimaerin; 1.
DR   CDD; cd10352; SH2_a2chimerin_b2chimerin; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR035840; Chimaerin_SH2.
DR   InterPro; IPR017356; CHN1/CHN2.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR037860; RhoGAP_chimaerin.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   PANTHER; PTHR46075:SF4; BETA-CHIMAERIN; 1.
DR   PANTHER; PTHR46075; CHIMERIN FAMILY MEMBER; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF00017; SH2; 1.
DR   PIRSF; PIRSF038015; N-chimaerin; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00252; SH2; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   4: Predicted;
KW   GTPase activation {ECO:0000256|PIRNR:PIRNR038015};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR038015};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW   SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          59..127
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          214..264
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          277..468
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   468 AA;  53742 MW;  2FFE13975E2E7F5B CRC64;
     MAASSNSSLS GSSVSSDAEE YQPPIWKSYL YQLQQEAPRP KRIICAGEVE NRPKYYGREF
     HGIISREQAD ELLGGVEGAY ILRESQRQPG CYTLALRFGN QTLNYRLFYD GKHFVGEKRF
     ESIHDLVTDG LITLYIETKA SEYISKMTTN PIYEHIGYAT LLREKVSRRL SRSKNESRKT
     SVTNEEHTAV EKISSLVRRA ALTHNDNHFN YEKTHNFKVH TFRGPHWCEY CANFMWGLIA
     QGVRCSDCGL NVHKQCSKHV PNDCQPDLKR IKKVYCCDLT TLVKAHNTQR PMVVDICIRE
     IEARGLKSEG LYRVSGFTEH IEDVKMAFDR DGEKADISAN IYPDINIITG ALKLYFRDLP
     IPVITYDTYP KFIEAAKISN ADERLEAVHD VLMLLPPAHY ETLRYLMIHL KKVTLNEKDN
     LMNAENLGIV FGPTLMRSPE DSTLTTLHDM RYQKLIVQIL IENEDVLF
//
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