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Database: UniProt
Entry: G1SI61_RABIT
LinkDB: G1SI61_RABIT
Original site: G1SI61_RABIT 
ID   G1SI61_RABIT            Unreviewed;      1665 AA.
AC   G1SI61;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Rho GTPase activating protein 21 {ECO:0000313|Ensembl:ENSOCUP00000002360.4};
GN   Name=ARHGAP21 {ECO:0000313|Ensembl:ENSOCUP00000002360.4};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000002360.4, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000002360.4, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000002360.4,
RC   ECO:0000313|Proteomes:UP000001811};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSOCUP00000002360.4}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000002360.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC       Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Cytoplasmic
CC       vesicle membrane {ECO:0000256|ARBA:ARBA00004284}; Peripheral membrane
CC       protein {ECO:0000256|ARBA:ARBA00004284}. Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004395}.
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DR   EMBL; AAGW02059374; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02059375; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02059376; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02059377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02059378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02059379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PaxDb; 9986-ENSOCUP00000002360; -.
DR   Ensembl; ENSOCUT00000002723.4; ENSOCUP00000002360.4; ENSOCUG00000002720.4.
DR   eggNOG; KOG4407; Eukaryota.
DR   GeneTree; ENSGT00940000155406; -.
DR   HOGENOM; CLU_001776_1_0_1; -.
DR   TreeFam; TF329345; -.
DR   Proteomes; UP000001811; Chromosome 16.
DR   Bgee; ENSOCUG00000002720; Expressed in frontal cortex and 16 other cell types or tissues.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   CDD; cd01253; PH_ARHGAP21-like; 1.
DR   CDD; cd04395; RhoGAP_ARHGAP21; 1.
DR   Gene3D; 1.20.5.220; -; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR23175; PDZ DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR23175:SF16; RHO GTPASE-ACTIVATING PROTEIN 21; 1.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001811}.
FT   DOMAIN          52..161
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          897..1006
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          1110..1302
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          205..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          412..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          494..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          653..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          840..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1053..1089
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1311..1360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1379..1538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1559..1578
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1606..1665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        866..880
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1061..1085
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1312..1329
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1339..1360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1388..1419
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1451..1477
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1559..1576
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1618..1632
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1665 AA;  180843 MW;  3FDB328F60C3E13A CRC64;
     MMATRRTGLP EGDGDKLKAC ETPVSKNKDG KEQSETVSPS EDEAFSWPGP KTVTLKRTPQ
     GFGFTLRHFI VYPPESAVQL SYKDEENGNR GGKQGKRLEP MDTIFVKQVK EGGPAFEAGL
     CTGDRIIKVN GESVIGKTYS QVIALIQNSD TALELSVMPK DEDILQVAYS QDAYLKGNEA
     YSGNARNIPE PPPVCYPWLP SAPPAAAAQP AEASPADAPL SKQQTSTPGP TPPGRAYRME
     IQVPPSPTDV AKSNTAVCVC NESVRSVIVP SEKAVDVLPG RGSHTGPSHR TEEVRYGANE
     HTSLKAVSRA TSPPSSVPAA HRIHHAAGSR SLDPSGGLLK SGNYAGHSEG IPSDRAHAVD
     SPSIAVNHYS PNSHQRIDWK NYKTYKEYID NRRLHIGCRT IQERLDSLRA ASRSTADYSQ
     VAPGRAASQV RRRSTSHDRV PPAAQIRQRS VSQERLEDPV LTRYCPRSAS QGALTSPPVG
     LSQHRTRSWD YLEGQGEPAE RQTPDSNGER AQASRWGGFA ERDDRRGVRE APKAFRGAHL
     SVAPGAVSVE SRRVTGRGAP GAPQFKKPPL DLKALQPSRT VPTACGAPLA RGVAQDRSPL
     VKVRSHSLKA PSAHAAAKPA VSQNSLVCTK DQRPVIHAHE NSVLSQQTWF RPESAPDHQA
     DPAKPPSVSG APAKPAAQTS ENGAAAECEL SVSLRDVDIR AAEAGAPQPH PADGTEAVVL
     REKPPSGRQT PQPLRHQSYI LAVNDQEAGS DSTCWLPNDA RREVHIKRLE ERKASSASPP
     GDSLASIPFI DEPTSPSIDH DIAHISASAV ISASTSQVPC RATVPPSLTT SAPLIRRQLS
     HDHDSIGPPS LDAQPTSKTE RSKSYDEVSG VASITDSQKS SEDSGSRKDS SSEVFSDAAK
     EGWLHFRPLV TDKGKRVGGS IRPWKQMYVV LRGHSLYLYK DKREQTAPCE EEQPISVNAC
     LIDISYSETK RKNVFRLTTS DRECLFQAED RDDMLAWIKT IQDSSNLNEE DTGVTNRDLI
     SRRIKEYNSL MSKAEQLPKT PRQSLSLRQT LLGAKSEPKT QSPHSPKEEP ERKLLGKDDT
     SPPKDRGMWI RGIPQIGRRK KPAATGTFGV RLDDCPPAHT NRYIPLIVDI CCKLVEERGL
     EYTGIYRVPG NNAAISSMQE ELNKGMADID IQDDKWRDLN VISSLLKSFF RKLPEPLFTN
     DKYADFIEAN RKEDPLDRLK TLKRLIHDLP EHHYETLKFL SAHLKTVAEN SEKNKMEPRN
     LAIVFGPTLV RTSEDNMTHM VTHMPDQYKI VETLIQHHDW FFTEEGAEEP LTTVRQESTV
     ESQPVPNIDH LLSNIGRTGA SPGDASDSAT SDSTKSKVTC SGEQYSRELL VTSIFAAASR
     KRKKPKEKAQ PSSSEDELDS VFSKKEPGAQ GREHGRAGEA AGRTPGAPRS ASPSPEAAPW
     AAGRLSPEAR SVAESRGEEA DDERSELVSE GRPPESDSEG DFPACAAPGR RDSEGSEASG
     PRPAAARAHQ LIEGDTLARR KAAPTGSDGD GDAPALARNI LDGTVTSLRT QAEADFRRGV
     RRRHTLGGHR DASFWKEPEL SAVTRLQPRC PAQDLSITHW LARERLRTST PDLSTPGGLD
     PAPVPAPRPA PPDQVNGGDG FPGASCAAAS QPPALSGAAQ PHPCL
//
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