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Database: UniProt
Entry: A0A3P8VHY2_CYNSE
LinkDB: A0A3P8VHY2_CYNSE
Original site: A0A3P8VHY2_CYNSE 
ID   A0A3P8VHY2_CYNSE        Unreviewed;      1163 AA.
AC   A0A3P8VHY2;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
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:ENSCSEP00000013937.1};
OS   Cynoglossus semilaevis (Tongue sole).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC   Cynoglossinae; Cynoglossus.
OX   NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000013937.1, ECO:0000313|Proteomes:UP000265120};
RN   [1] {ECO:0000313|Ensembl:ENSCSEP00000013937.1, ECO:0000313|Proteomes:UP000265120}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24487278;
RA   Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA   Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA   Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA   Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA   Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA   Zhao Y., Schartl M., Tang Q., Wang J.;
RT   "Whole-genome sequence of a flatfish provides insights into ZW sex
RT   chromosome evolution and adaptation to a benthic lifestyle.";
RL   Nat. Genet. 46:253-260(2014).
RN   [2] {ECO:0000313|Ensembl:ENSCSEP00000013937.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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}.
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DR   RefSeq; XP_008315337.1; XM_008317115.2.
DR   AlphaFoldDB; A0A3P8VHY2; -.
DR   Ensembl; ENSCSET00000014099.1; ENSCSEP00000013937.1; ENSCSEG00000008933.1.
DR   GeneID; 103383815; -.
DR   CTD; 10395; -.
DR   GeneTree; ENSGT00950000183061; -.
DR   OrthoDB; 2883046at2759; -.
DR   Proteomes; UP000265120; Chromosome 9.
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:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd04375; RhoGAP_DLC1; 1.
DR   CDD; cd08869; START_RhoGAP; 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   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265120};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          717..927
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   DOMAIN          999..1138
FT                   /note="START"
FT                   /evidence="ECO:0000259|PROSITE:PS50848"
FT   REGION          120..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          238..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          319..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          470..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          556..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..208
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..383
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..578
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        581..609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..647
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1163 AA;  129421 MW;  71796DA8F288F3E2 CRC64;
     MILTQIEAKE ACTWLRAAGF PQYAQLYEDA LFPIDISSVT RDHDFLDRDA IEALCRRLNT
     LNKCALMRLE ISPQRKRSED SDEDELCAIS GRWTFQRDSK RWSRMEELDV FSTLSMDDKE
     ASSFPKDHVP QKGKHVLHEG NSSESVLTDL SEQPEVVSIH SSGSGGRGEE KGHGATLVNE
     SAPAGATRAS SVTSMCSSSG TGGSGCANED SLSDGLPPSP LESLGQFTFD MKTGIVGLGG
     NMERGSESSK STRSRAKSFL KRMESLRLRS SSTSKRKKKG SITGGKIEIS GPVIKEGLDD
     DKLRRLNCVD IPSISFHQNL NHHRNPTQTM TLNRNRSVSY STQTSNGSTG STGSSQSEAS
     SGSAVSTPSP VTRARSHSTA AGSSKRGGMY LEGFDPLSIL QQTSDRQPKP PPNSSNAFNC
     PATNGMTVHE QNHKNNYSYQ SNGGELGEEE EEEDEGMLYF YLPEGHKPGT FPKALEDGSS
     RNNNGIDNGN LVVLRGRQSR RQRRGSSGSV DSRLSFYDNV PYTEREEEVE EEGDEGKLEE
     VLKHVSGLKR FNAWSEAVVG EEEEEEEEDE EEEGDSDSAL DSASPCPSSP LQNRLEETEN
     GSDQDSTGNP LGEGEEGMRE RRDSGVGASL TRTSRPQKLR WPSFQNSHRP SLASAQLQIS
     CQSVLQMNLL QKLSLLQLTA LLEKHTPANK HGFSWAVPKF MKRIKVRDYK DRNVFGVPLQ
     VIVQRTGQPL PQGIQQAMRF LRNQCLDQVG LFRKSGVKSR IQALRQMNEA SGADGGGVSY
     EGQSAYDVAD MLKQYFRDLP EPLLTSKLSE TFLQIYQYMP KELRLQAARA AVLLLPDENR
     EALRTLLCFL SDVTASVAEN QMTPTNLAVC LAPSLFHLNT LRRKESSSPR VMNRKQILGK
     PDQKDLNENL AATHGVAHMI QECRKLFRIP EEMNRCRNSY MEQALLPRCI KDLCDEQAGN
     GGYRTYLRNH LDALLKEAKD KFRGYDSCST PEQAELACRK VHDGFPLRQW KVTIEVPASP
     EEVLTRVLRE QGHWDEDLLE SRVVESLDDK MEVYQYVRNT MAPHPTRDHV VLRSWVTDLP
     KGACALVCTS VDHEGAPVVG VRANVLTSRY FIEPCGSNKS RLTHISRIDC RGRFPEWYNK
     LYGHLCAAEV VRIRESFSAP LDK
//
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