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Database: UniProt
Entry: A0A287APY3_PIG
LinkDB: A0A287APY3_PIG
Original site: A0A287APY3_PIG 
ID   A0A287APY3_PIG          Unreviewed;       459 AA.
AC   A0A287APY3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Chimaerin {ECO:0000256|PIRNR:PIRNR038015};
DE   AltName: Full=Chimerin {ECO:0000256|PIRNR:PIRNR038015};
GN   Name=CHN1 {ECO:0000313|Ensembl:ENSSSCP00000045937.1,
GN   ECO:0000313|VGNC:VGNC:103921};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000045937.1, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000045937.1, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000045937.1,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:HDB81988.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30723633; DOI=.7717/peerj.6374;
RA   Gilbert D.G.;
RT   "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL   PeerJ 7:E6374-E6374(2019).
RN   [3] {ECO:0000313|Ensembl:ENSSSCP00000045937.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: GTPase-activating protein for p21-rac.
CC       {ECO:0000256|PIRNR:PIRNR038015}.
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DR   EMBL; DQIR01226511; HDB81988.1; -; Transcribed_RNA.
DR   STRING; 9823.ENSSSCP00000045937; -.
DR   Ensembl; ENSSSCT00000040421.3; ENSSSCP00000045937.1; ENSSSCG00000022345.4.
DR   VGNC; VGNC:103921; CHN1.
DR   GeneTree; ENSGT01030000234635; -.
DR   OrthoDB; 5395569at2759; -.
DR   Reactome; R-SSC-9013148; CDC42 GTPase cycle.
DR   Reactome; R-SSC-9013149; RAC1 GTPase cycle.
DR   Proteomes; UP000008227; Chromosome 15.
DR   Bgee; ENSSSCG00000022345; Expressed in occipital cortex and 44 other cell types or tissues.
DR   GO; GO:0046875; F:ephrin receptor binding; IBA:GO_Central.
DR   GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0008045; P:motor neuron axon guidance; IEA:Ensembl.
DR   GO; GO:0050770; P:regulation of axonogenesis; IEA:Ensembl.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:UniProtKB-UniRule.
DR   CDD; cd20856; C1_alphaCHN; 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; CHIMERIN FAMILY MEMBER; 1.
DR   PANTHER; PTHR46075:SF1; N-CHIMAERIN; 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   1: Evidence at protein level;
KW   GTPase activation {ECO:0000256|PIRNR:PIRNR038015};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR038015};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:A0A287APY3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW   SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          49..117
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          205..255
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          268..459
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
SQ   SEQUENCE   459 AA;  53169 MW;  9669BE162A232368 CRC64;
     MALTLFDTDE YRPPVWKSYL YQLQQEAPHP RRITCTNEVE NRPKYYGREF HGMISREAAD
     QLLSVAEGSY LIRESQRQPG TYTLALRFGS QTRNFRLYYD GKHFVGEKRF ESIHDLVTDG
     LITLYIETKA AEYIAKMTIN PIYEHIGYTT LNREPAYQKH MPVLKETHDE RDSTGQDGVS
     EKRLTSLVRR ATLKENEQIP KYEKVHNFKV HTFRGPHWCE YCANFMWGLI AQGVKCADCG
     LNVHKQCSKM VPNDCKPDLK HVKKVYSCDL TTLVKAHITK RPMVVDMCIR EIESRGLNSE
     GLYRVSGFSD LIEDVKMAFD RDGEKADISV NMYEDINIIT GALKLYFRDL PIPLITYDAY
     PKFIESAKIM DPDEQLETLH EALKLLPPAH CETLRYLMAH LKRVTLHEKE NLMNAENLGI
     VFGPTLMRSP ELDAMAALND IRYQRLVVEL LIKNEDILF
//
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