ID A0A2I0MM33_COLLI Unreviewed; 1079 AA.
AC A0A2I0MM33;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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};
DE Flags: Fragment;
GN Name=DLC1 {ECO:0000313|EMBL:PKK30737.1};
GN ORFNames=A306_00003544 {ECO:0000313|EMBL:PKK30737.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK30737.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK30737.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK30737.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKK30737.1}.
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DR EMBL; AKCR02000006; PKK30737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0MM33; -.
DR STRING; 8932.A0A2I0MM33; -.
DR InParanoid; A0A2I0MM33; -.
DR Proteomes; UP000053872; Unassembled WGS sequence.
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:UP000053872}.
FT DOMAIN 628..834
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 865..1050
FT /note="START"
FT /evidence="ECO:0000259|PROSITE:PS50848"
FT REGION 278..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PKK30737.1"
SQ SEQUENCE 1079 AA; 121298 MW; 0468ABE2A58249FB CRC64;
EAKEACDWLR AAGFPQYAQL YEDLLFPIDI ALVKREHDFL DRDAIEALCR RLNTLNKCAV
MKLEISPHRK RSEDSDEDEP CAISGKWTFQ RDSKRWSRLE EFDVFPPKPD LNTASSEAPH
LTNAASHESV LTDLSERQEV ASILSISSNS SHQPTLQSEA STTRTNSVVS VCSSSNFVAN
DDSFSSLPSP RELNSFSFNT KANEKNAKSK TKSLLKRMES LKIKSSQHGK SKAPSKLGLI
ISGPILQEGM DEDKLKQLNC VEISALNGNH ISLPMVRKRS VSNSTQTSSS SSQSETSSAV
STPSPITRTR SLSAYNKRVG MYLEGFDPFN QSTFSDVMEQ NFKNRGSFAE DTVFFIPEDH
KPGTFPKALS NGNFSPTESN ASVNWRTGSF HGHGHLALRR ENSGDSCKEL GMGKRRNSSS
SVSSRLSIYD NVPGSILYSS TSDLADLENE DIFPELDDIL YHVKGMQRIV NQWSEKFSDE
GDSDSALDSI SPCPSSPKQI HLDVDNDRTT PSDLDSTGNS LNETEEPAGM QDRRDSGVGA
SLTRSSRHRL RWHSFQSSHR PSLSSASLQI NCQSVAQMNL LQKYSLLKLT ALLEKYTPSN
KHGFSWAVPK FMKRIKVPDY KDRNVFGVPL QVNVQRTGQP LPQSIQQAMR YLRNHCLDQV
GLFRKSGVKS RIQALRQMNE SSTDSVNYEG QSAYDVADML KQFFRDLPEP LMTNKLSETF
LQIYQYVPKD QRLQAIKAAI MLLPDENREV LQILLYFLSD VTAAVKENQM TPTNLAVCLA
PSLFHLNTLK RENSSPRVMQ RKPSLGKPDQ KDLNENLAAT QGLAHMIAEC KKLFQIPEEM
SRGRNSYTEQ DLRPLSLEEL RGGSSTTEPS DYHCYLQDCV DDLLKEMKEK FKGWVSCSTS
EQADLAYKKV CEGPPLRLWK TTIEIPATPE DVLNRLLKEQ HLWDEDLIDS KVIESLDSQT
DIYQYVQNSM APQPARDFVV LRTWRTNFPK GACVLLATSV DHDRAPVAGV RVNVLLSRYL
IEPCGSGKSK LTYMCRIDLR GHMPDWYTKS FGHLCASEVV KIRDSFSHQS LESKEVKSR
//
