ID W5UC61_ICTPU Unreviewed; 781 AA.
AC W5UC61;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Rho GTPase-activating protein 26 {ECO:0000313|EMBL:AHH39174.1, ECO:0000313|RefSeq:XP_017347884.1};
GN Name=ARHGAP26 {ECO:0000313|EMBL:AHH39174.1};
GN Synonyms=LOC108278797 {ECO:0000313|RefSeq:XP_017347884.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|EMBL:AHH39174.1};
RN [1] {ECO:0000313|EMBL:AHH39174.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Mixed {ECO:0000313|EMBL:AHH39174.1};
RX PubMed=23127152; DOI=10.1186/1471-2164-13-595;
RA Liu S., Zhang Y., Zhou Z., Waldbieser G., Sun F., Lu J., Zhang J.,
RA Jiang Y., Zhang H., Wang X., Rajendran K.V., Khoo L., Kucuktas H.,
RA Peatman E., Liu Z.;
RT "Efficient assembly and annotation of the transcriptome of catfish by RNA-
RT Seq analysis of a doubled haploid homozygote.";
RL BMC Genomics 13:595-595(2012).
RN [2] {ECO:0000313|RefSeq:XP_017347884.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017347884.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000256|ARBA:ARBA00004246}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
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DR EMBL; JT410744; AHH39174.1; -; mRNA.
DR RefSeq; XP_017347884.1; XM_017492395.3.
DR Ensembl; ENSIPUT00000017218; ENSIPUP00000016520; ENSIPUG00000010994.
DR GeneID; 108278797; -.
DR OrthoDB; 5395569at2759; -.
DR Proteomes; UP000221080; Chromosome 18.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd01249; BAR-PH_GRAF_family; 1.
DR CDD; cd07636; BAR_GRAF; 1.
DR CDD; cd11882; SH3_GRAF-like; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 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 Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR035483; GRAF_BAR.
DR InterPro; IPR047234; GRAF_fam.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR047225; PH_GRAF.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR12552; OLIGOPHRENIN 1; 1.
DR PANTHER; PTHR12552:SF4; RHO GTPASE-ACTIVATING PROTEIN 26; 1.
DR Pfam; PF16746; BAR_3; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 265..370
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 384..568
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 723..781
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 571..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 781 AA; 89312 MW; 064E3827B90DF7FC CRC64;
MGLPALEFSD CYLDSPQFRE RLKSHELELD NTNKFIKELL KDGKALIQAL KNLSTAQRKF
AESLNEFKFQ CIGDAETDDE ICIARSLQEF AGVLQNLEDE RTRMIDNAND VLITPLERFR
KEQIGAAKEA KKKYDKETEK YCTVLEKHLS LSAKKKESHL HEADNQVDHV RQHFYEVSLE
YVFKVQEVQE RKMFEFVEPL LAFLQGLFTY YHHGYELAKD FNHFKTDLTI SIQNTRNRFE
STRSEVESLM KKMKENPHEH KNISPHTMEG YLFVLEKRSF VSTWVKYYCT YQRESKRLTL
VLFDQKSGGK TGEEESVVLK SCIRRKTDSI EKRFCFDVET VDRPGVMITM QALSEEDRRL
WMEAMDGREP VYNLNRDSQN EGMAQLDVIG FNVMKKFIYA IETRGIDEQG LYRIVGVSSR
VQKLLSLAMD PKTCADVELE SSEWEIKTIT SAIKHYLRIL PAPLMTYQYQ RSFIKAAKLD
NPEARVQEIH SIVHRLPEKN HQMLELLTKH LANVASHHQQ NLMTVANLGV VFGPTLLRPQ
EETVAAIMDI KFQNIVVEIL IENHERIFKE TPVPGAGQNS SQTSFSRRKS TESKAPSCSE
RPLTLFHTPT HSEKDRAVDK RNSMQVNSEP QPALSSLTCN STHNWNKFIN LSSGDGEQDG
LLQARQSRSN SHQIPRTRGS SISTSPASPS STSPRSPSWP MFSAPSSPQS ASCTSSESSP
LSPPLRKARA LYACKAEHDS ELSFIAGMIF ENVHPSREPG WLEGTLDGRT GLIPENYVEF
M
//
