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}.
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 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
//