ACAP2_RAT
ID ACAP2_RAT Reviewed; 770 AA.
AC Q5FVC7;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2;
DE AltName: Full=Centaurin-beta-2;
DE Short=Cnt-b2;
GN Name=Acap2; Synonyms=Centb2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAH90073.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:AAH90073.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP INTERACTION WITH RAB35, AND SUBCELLULAR LOCATION.
RX PubMed=23572513; DOI=10.1242/jcs.117846;
RA Kobayashi H., Fukuda M.;
RT "Rab35 establishes the EHD1-association site by coordinating two distinct
RT effectors during neurite outgrowth.";
RL J. Cell Sci. 126:2424-2435(2013).
CC -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 6
CC (ARF6). {ECO:0000250|UniProtKB:Q15057}.
CC -!- ACTIVITY REGULATION: GAP activity stimulated by phosphatidylinositol
CC 4,5-bisphosphate (PIP2) and phosphatidic acid.
CC {ECO:0000250|UniProtKB:Q15057}.
CC -!- SUBUNIT: Interacts with RAB35 (GTP-bound form); the interaction is
CC direct and probably recruits ACAP2 to membranes. Interacts with
CC MICALL1; the interaction is indirect through RAB35.
CC {ECO:0000269|PubMed:23572513}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:23572513};
CC Peripheral membrane protein {ECO:0000269|PubMed:23572513}.
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DR EMBL; BC090073; AAH90073.1; -; mRNA.
DR RefSeq; NP_001029178.1; NM_001034006.2.
DR RefSeq; XP_017459763.1; XM_017604274.1.
DR AlphaFoldDB; Q5FVC7; -.
DR SMR; Q5FVC7; -.
DR STRING; 10116.ENSRNOP00000030250; -.
DR iPTMnet; Q5FVC7; -.
DR PhosphoSitePlus; Q5FVC7; -.
DR jPOST; Q5FVC7; -.
DR PaxDb; Q5FVC7; -.
DR PRIDE; Q5FVC7; -.
DR GeneID; 619382; -.
DR KEGG; rno:619382; -.
DR UCSC; RGD:1562939; rat.
DR CTD; 23527; -.
DR RGD; 1562939; Acap2.
DR VEuPathDB; HostDB:ENSRNOG00000001730; -.
DR eggNOG; KOG0521; Eukaryota.
DR HOGENOM; CLU_012513_0_1_1; -.
DR InParanoid; Q5FVC7; -.
DR OrthoDB; 751525at2759; -.
DR PhylomeDB; Q5FVC7; -.
DR TreeFam; TF318315; -.
DR PRO; PR:Q5FVC7; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001730; Expressed in esophagus and 19 other tissues.
DR ExpressionAtlas; Q5FVC7; baseline and differential.
DR Genevisible; Q5FVC7; RN.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; ISO:RGD.
DR GO; GO:0005096; F:GTPase activator activity; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0030029; P:actin filament-based process; ISO:RGD.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR045258; ACAP1/2/3-like.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR23180; PTHR23180; 2.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Coiled coil; Endosome; GTPase activation; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..770
FT /note="Arf-GAP with coiled-coil, ANK repeat and PH domain-
FT containing protein 2"
FT /id="PRO_0000306387"
FT DOMAIN 6..226
FT /note="BAR"
FT /evidence="ECO:0000255"
FT DOMAIN 266..361
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 399..520
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REPEAT 632..661
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 665..694
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 698..727
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT ZN_FING 414..437
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 371..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15057"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQK5"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15057"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQK5"
FT MOD_RES 734
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q15057"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15057"
SQ SEQUENCE 770 AA; 87230 MW; B803C7C69B7FE1CA CRC64;
MKMTVDFEEC LKDSPRFRAA LEEVEGDVAE LELKLDKLVK LCIAMIDTGK AFCAANKQFM
NGIRDLAQYS SNDAVVETSL TKFSDSLQEM INFHTILFDQ TQRSIKAQLQ NFVKEDLRKF
KDAKKQFEKV SEEKENALVK NAQVQRNKQH EVEEAANILT ATRKCFRHIA LDYVLQINVL
QSKRRSEILK SMLSFMYAHL AFFHQGYDLF SELGPYMKDL GAQLDRLVVD AAKEKREMEQ
KHSTIQQKDF SSDDSKLEYN VDAANGIVME GYLFKRASNA FKTWNRRWFS IQNNQLVYQK
KFKDSPTVVV EDLRLCTVKH CEDIERRFCF EVVSPTKSCM LQADSEKLRQ AWIKAVQTSI
ATAYREKGDE SEKLDKKSSP STGSLDSGSE SKEKLLKGES ALQRVQCIPG NTSCCDCGLA
DPRWASINLG ITLCIECSGI HRSLGVHFSK VRSLTLDTWE PELLKLMCEL GNDVINRVYE
AKLEKMGVKK PQPGQRQEKE AYIRAKYVER KFVDKYSTLL SPSEQEKRII SKSCEDQRLS
HTRVSVHTPV KSNDSGIQQC SDDGRESLPS TVSANSLYEP EGERQESSVF LDSKHLNPGL
QLYRASYEKN LPKMAEALAH GADVNWANSD ENQATPLIQA VLGGSLVTCE FLLQNGANVN
QRDVQGRGPL HHATVLGHTG QVCLFLKRGA NQHATDEEGK DPLSIAVEAA NADIVTLLRL
ARMNEEMRES EGLYGQPGDE TYQDIFRDFS QMASNNPEKL NRFQQDSQKF
