ID A0A287ALV3_PIG Unreviewed; 1125 AA.
AC A0A287ALV3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Rho GTPase-activating protein 7 {ECO:0000256|ARBA:ARBA00014465};
DE AltName: Full=Rho-type GTPase-activating protein 7 {ECO:0000256|ARBA:ARBA00030675};
DE AltName: Full=START domain-containing protein 12 {ECO:0000256|ARBA:ARBA00032733};
DE AltName: Full=StAR-related lipid transfer protein 12 {ECO:0000256|ARBA:ARBA00030542};
GN Name=DLC1 {ECO:0000313|Ensembl:ENSSSCP00000044892.1,
GN ECO:0000313|VGNC:VGNC:96191};
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:ENSSSCP00000044892.1, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000044892.1, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000044892.1,
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:HDB30257.1}
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:ENSSSCP00000044892.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000256|ARBA:ARBA00004246}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
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 EMBL; DQIR01174780; HDB30257.1; -; Transcribed_RNA.
DR Ensembl; ENSSSCT00000052902.2; ENSSSCP00000044892.1; ENSSSCG00000006970.5.
DR VGNC; VGNC:96191; DLC1.
DR GeneTree; ENSGT00950000183061; -.
DR OMA; AMSHESM; -.
DR Proteomes; UP000008227; Chromosome 17.
DR Bgee; ENSSSCG00000006970; Expressed in heart left ventricle and 39 other cell types or tissues.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd04375; RhoGAP_DLC1; 1.
DR CDD; cd09591; SAM_DLC1; 1.
DR CDD; cd08908; START_STARD12-like; 1.
DR Gene3D; 1.10.287.2070; -; 1.
DR Gene3D; 3.30.530.20; -; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR PANTHER; PTHR12659:SF2; RHO GTPASE-ACTIVATING PROTEIN 7; 1.
DR PANTHER; PTHR12659; RHO-TYPE GTPASE ACTIVATING PROTEIN; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF07647; SAM_2; 1.
DR Pfam; PF01852; START; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00234; START; 1.
DR SUPFAM; SSF55961; Bet v1-like; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50848; START; 1.
PE 4: Predicted;
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT DOMAIN 675..881
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 911..1096
FT /note="START"
FT /evidence="ECO:0000259|PROSITE:PS50848"
FT REGION 155..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1125 AA; 127042 MW; 07E67D50765C67F8 CRC64;
MGDPEAHVMA RPLRAPLRRS FSDHIRDSTA RALDVIWKNT RDRRLAEIEA KEACDWLRAA
GFPQYAQLYE DLLFPIDISL VKREHDFLDR DAIEALCRRL NTLNKCAVMK LEISPHRKRS
EDSDEDEPCA ISGKWTFQRD SKRWSRLEEF DVFSPKEDPI PGSPDNSHLK NAPSHESMLT
DLSERQEVAS VRSLSSTSSL ATHTPHCGDT ATTRTNSVIS VCSSGTFVGN DDSFCSLPSP
KELSSFSFSM KGHEKSTKSK THSLLKRMES LKLKGSHHGK HKAPSKLGLI ISGPILQEGM
DEEKLKQLNC MEISALNGNH INVPMVRKRS VSNSTQTSSS SSQSETSSNV STPSPVTRTR
SLSACNKRGG MYLEGFDPFN QSTFNNVMEQ NFKNRESYPE DTVFYIPEDH KPGTFPKALS
NGSFSPSGNN SSVNWRTGSF HGPGHISLRR ENSSDSPKEL KRRNSSSSMT SRLSIYDNVP
GSILYSSSGD LADLENEDIF PELDDILYHV KGMQRIVNQW SEKFSDEGDS DSALDSVSPC
PSSPKQIHLD VDNDRATPSD LDSTGNSLNE PEEPSDIPER RDSGVGASLT RSNRHRLRWH
SFQSSHRPSL NSVSLQINCQ SVAQMNLLQK YSLLKLTALL EKHTPSNKHG FSWAVPKFMK
RIKVPDYKDR NVFGVPLTVN VQRTGQPLPQ SIQQAMRYLR NHCLDQVGLF RKSGVKSRIQ
ALRQMNESAL DCVNYEGQSA YDVADMLKQY FRDLPEPLMT NKLSETFLQI YQYVPKDQRL
QAIKAAIMLL PDENREVLQT LLYFLSDVTA AVKENQMTPT NLAVCLAPSL FHLNTLKREN
SSPRVMQRKQ SLGKPDQKDL NENLAATQGL AHMIAECKKL FQVPEEMSRC RNSYTEQELK
PLTLEALGRL CNDESASYQH FLQDCVDSLF KEVKEKFKGW VSYSTSEQAE LSYKKVSEGP
PLRLWRATIE VPAMPEEILK RLLKEQHLWD VDLLDSKVIE ILDSQTEIYQ YVQNSMAPHP
ARDYVVLRTW RTNLPKGACA LLLTSVDHDR APVVGVRVNV LLSRYLIEPC GSGKSKLTYM
CRADLRGHMP EWYTKSFGHL CAAEVVKIRD SFSNQNTETK DTKSR
//
