RPM1_CAEEL
ID RPM1_CAEEL Reviewed; 3766 AA.
AC Q17551;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=E3 ubiquitin-protein ligase rpm-1 {ECO:0000303|PubMed:10839353};
DE EC=2.3.2.33 {ECO:0000250|UniProtKB:O75592};
DE AltName: Full=Pam/highwire/rpm-1 protein;
DE AltName: Full=Regulator of presynaptic morphology protein 1 {ECO:0000303|PubMed:10839353};
DE AltName: Full=Synapse defective protein 3 {ECO:0000303|PubMed:10839353};
GN Name=rpm-1 {ECO:0000303|PubMed:10839353, ECO:0000312|WormBase:C01B7.6};
GN Synonyms=syd-3 {ECO:0000303|PubMed:10839353};
GN ORFNames=C01B7.6 {ECO:0000312|WormBase:C01B7.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF ARG-3597 AND CYS-3675.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:10839353};
RX PubMed=10839353; DOI=10.1016/s0896-6273(00)81167-8;
RA Zhen M., Huang X., Bamber B., Jin Y.;
RT "Regulation of presynaptic terminal organization by C. elegans RPM-1, a
RT putative guanine nucleotide exchanger with a RING-H2 finger domain.";
RL Neuron 26:331-343(2000).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:10839354};
RX PubMed=10839354; DOI=10.1016/s0896-6273(00)81168-x;
RA Schaefer A.M., Hadwiger G.D., Nonet M.L.;
RT "rpm-1, a conserved neuronal gene that regulates targeting and
RT synaptogenesis in C. elegans.";
RL Neuron 26:345-356(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP PROTEIN SEQUENCE OF 86-99; 341-351; 621-629; 736-749; 834-847; 858-865;
RP 1045-1056; 1084-1093; 1225-1237; 1281-1290; 1426-1434; 1441-1480;
RP 1588-1603; 1961-1988; 2089-2097; 2103-2122; 2171-2183; 2186-2201; 2408-2416
RP AND 2573-2588, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V.;
RL Submitted (MAR-2005) to UniProtKB.
RN [5]
RP FUNCTION, INTERACTION WITH FSN-1; CUL-1 AND SKR-1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15208641; DOI=10.1038/nature02647;
RA Liao E.H., Hung W., Abrams B., Zhen M.;
RT "An SCF-like ubiquitin ligase complex that controls presynaptic
RT differentiation.";
RL Nature 430:345-350(2004).
RN [6]
RP FUNCTION.
RX PubMed=15707898; DOI=10.1016/j.cell.2004.12.017;
RA Nakata K., Abrams B., Grill B., Goncharov A., Huang X., Chisholm A.D.,
RA Jin Y.;
RT "Regulation of a DLK-1 and p38 MAP kinase pathway by the ubiquitin ligase
RT RPM-1 is required for presynaptic development.";
RL Cell 120:407-420(2005).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF CYS-3675.
RX PubMed=21968191; DOI=10.1534/genetics.111.134791;
RA Tulgren E.D., Baker S.T., Rapp L., Gurney A.M., Grill B.;
RT "PPM-1, a PP2Calpha/beta phosphatase, regulates axon termination and
RT synapse formation in Caenorhabditis elegans.";
RL Genetics 189:1297-1307(2011).
RN [8]
RP FUNCTION.
RX PubMed=21670305; DOI=10.1073/pnas.1104830108;
RA Nix P., Hisamoto N., Matsumoto K., Bastiani M.;
RT "Axon regeneration requires coordinate activation of p38 and JNK MAPK
RT pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:10738-10743(2011).
RN [9]
RP INTERACTION WITH RAE-1, AND MUTAGENESIS OF VAL-2084; ILE-2087 AND ARG-2088.
RX PubMed=22357847; DOI=10.1523/jneurosci.2901-11.2012;
RA Grill B., Chen L., Tulgren E.D., Baker S.T., Bienvenut W., Anderson M.,
RA Quadroni M., Jin Y., Garner C.C.;
RT "RAE-1, a novel PHR binding protein, is required for axon termination and
RT synapse formation in Caenorhabditis elegans.";
RL J. Neurosci. 32:2628-2636(2012).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27123983; DOI=10.1371/journal.pgen.1006010;
RA D'Souza S.A., Rajendran L., Bagg R., Barbier L., van Pel D.M., Moshiri H.,
RA Roy P.J.;
RT "The MADD-3 LAMMER kinase interacts with a p38 MAP kinase pathway to
RT regulate the display of the EVA-1 guidance receptor in Caenorhabditis
RT elegans.";
RL PLoS Genet. 12:E1006010-E1006010(2016).
CC -!- FUNCTION: Atypical E3 ubiquitin-protein ligase which specifically
CC mediates ubiquitination of threonine and serine residues on target
CC proteins, instead of ubiquitinating lysine residues (By similarity).
CC Shows esterification activity towards both threonine and serine, with a
CC preference for threonine, and acts via two essential catalytic cysteine
CC residues that relay ubiquitin to its substrate via thioester
CC intermediates (By similarity). Mediates ubiquitination and subsequent
CC proteasomal degradation of target proteins, including dlk-1
CC (PubMed:10839353, PubMed:15707898). Negatively regulates a p38 MAP
CC kinase pathway composed of dlk-1, mkk-4, and pmk-3 that functions
CC presynaptically to regulate synaptic architecture (PubMed:15707898).
CC Has a role during synaptogenesis; regulates neuronal morphology,
CC specifically presynaptic differentiation. May regulate the spatial
CC arrangement of presynaptic terminals or restrict their development
CC (PubMed:10839354, PubMed:15208641, PubMed:15707898, PubMed:21968191).
CC By targeting both dlk-1 and mlk-1 for degradation, may negatively
CC regulate mlk-1/mek-1/kgb-1 and dlk-1/mkk-4/pmk-3 pathways which are
CC involved in axon regeneration after injury (PubMed:21670305). Regulates
CC axon termination in PLM and ALM neurons (PubMed:21968191). May play a
CC role in the formation of muscle connections between the body wall and
CC the motor axons in the dorsal and ventral cord (PubMed:27123983).
CC {ECO:0000250|UniProtKB:O75592, ECO:0000269|PubMed:10839353,
CC ECO:0000269|PubMed:10839354, ECO:0000269|PubMed:15208641,
CC ECO:0000269|PubMed:15707898, ECO:0000269|PubMed:21670305,
CC ECO:0000269|PubMed:21968191, ECO:0000269|PubMed:27123983}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-threonine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-3-O-ubiquitinyl-L-threonine.;
CC EC=2.3.2.33; Evidence={ECO:0000250|UniProtKB:O75592};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:10839353, ECO:0000269|PubMed:15707898}.
CC -!- SUBUNIT: Interacts with rae-1 (PubMed:22357847). Component of an SCF
CC (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex composed of cul-
CC 1, fsn-1, rpm-1 and skr-1 (PubMed:15208641).
CC {ECO:0000269|PubMed:15208641, ECO:0000269|PubMed:22357847}.
CC -!- INTERACTION:
CC Q17551; Q3SWS8: Rae1; Xeno; NbExp=2; IntAct=EBI-6920110, EBI-6920222;
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000269|PubMed:10839353, ECO:0000269|PubMed:10839354,
CC ECO:0000269|PubMed:15208641}. Note=Localizes in periactive zone along
CC dorsal and lateral nerve cords. {ECO:0000269|PubMed:15208641}.
CC -!- TISSUE SPECIFICITY: Expression is seen in the pharynx, coelomocytes and
CC distal tip cell. Most abundant expression is in axons of the nerve ring
CC neuropil. Expression is not seen in body wall muscle, hypodermis or
CC intestine. {ECO:0000269|PubMed:10839353, ECO:0000269|PubMed:10839354}.
CC -!- DEVELOPMENTAL STAGE: First expressed in comma stage embryos and
CC persists through to adulthood. {ECO:0000269|PubMed:10839354}.
CC -!- DOMAIN: The PHR domains are compact beta-sandwich folds composed of 11
CC antiparallel strands and decorated with conserved apical loops. They
CC are likely to play a structural role and mediate interactions with
CC substrates or partners (By similarity). {ECO:0000250|UniProtKB:Q7TPH6}.
CC -!- DOMAIN: The tandem cysteine domain region confers threonine specificity
CC and contains the two essential catalytic cysteine residues that relay
CC ubiquitin. It binds four zinc ions in a C5HC7HC2 configuration.
CC {ECO:0000250|UniProtKB:O75592}.
CC -!- DISRUPTION PHENOTYPE: In mutants, mechanosensory neurons fail to
CC accumulate tagged vesicles, retract synaptic branches and ectopically
CC extend axons (PubMed:10839354). Some motor neurons branch and overgrow,
CC others show altered synaptic organization (PubMed:10839354). Fewer body
CC wall muscle connections to target motor neurons (PubMed:27123983).
CC {ECO:0000269|PubMed:10839354, ECO:0000269|PubMed:27123983}.
CC -!- SIMILARITY: Belongs to the RING-Cys relay (RCR) family. {ECO:0000305}.
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DR EMBL; FO080217; CCD62087.1; -; Genomic_DNA.
DR PIR; T29165; T29165.
DR RefSeq; NP_505267.1; NM_072866.3.
DR SMR; Q17551; -.
DR BioGRID; 44297; 7.
DR ComplexPortal; CPX-958; SCF-rpm-1 ubiquitin ligase complex.
DR IntAct; Q17551; 5.
DR STRING; 6239.C01B7.6; -.
DR iPTMnet; Q17551; -.
DR EPD; Q17551; -.
DR PaxDb; Q17551; -.
DR PeptideAtlas; Q17551; -.
DR PRIDE; Q17551; -.
DR EnsemblMetazoa; C01B7.6.1; C01B7.6.1; WBGene00004457.
DR GeneID; 179259; -.
DR KEGG; cel:CELE_C01B7.6; -.
DR UCSC; C01B7.6; c. elegans.
DR CTD; 179259; -.
DR WormBase; C01B7.6; CE06730; WBGene00004457; rpm-1.
DR eggNOG; KOG1428; Eukaryota.
DR GeneTree; ENSGT00940000167553; -.
DR HOGENOM; CLU_000063_0_0_1; -.
DR InParanoid; Q17551; -.
DR OMA; NKLCILD; -.
DR OrthoDB; 215263at2759; -.
DR PhylomeDB; Q17551; -.
DR BRENDA; 2.3.2.33; 1045.
DR SignaLink; Q17551; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q17551; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00004457; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0031594; C:neuromuscular junction; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0036062; C:presynaptic periactive zone; IDA:WormBase.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:ComplexPortal.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:WormBase.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:WormBase.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:WormBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0010171; P:body morphogenesis; IMP:WormBase.
DR GO; GO:0033563; P:dorsal/ventral axon guidance; IGI:UniProtKB.
DR GO; GO:0040011; P:locomotion; IGI:WormBase.
DR GO; GO:1905869; P:negative regulation of 3'-UTR-mediated mRNA stabilization; IMP:UniProtKB.
DR GO; GO:0030517; P:negative regulation of axon extension; IMP:WormBase.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IMP:UniProtKB.
DR GO; GO:0048692; P:negative regulation of axon extension involved in regeneration; IMP:UniProtKB.
DR GO; GO:0048681; P:negative regulation of axon regeneration; IMP:WormBase.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IMP:UniProtKB.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IMP:UniProtKB.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:UniProtKB.
DR GO; GO:1903753; P:negative regulation of p38MAPK cascade; IMP:UniProtKB.
DR GO; GO:1905490; P:negative regulation of sensory neuron axon guidance; IMP:UniProtKB.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:1905608; P:positive regulation of presynapse assembly; IMP:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IMP:WormBase.
DR GO; GO:1905868; P:regulation of 3'-UTR-mediated mRNA stabilization; IGI:UniProtKB.
DR GO; GO:0048841; P:regulation of axon extension involved in axon guidance; IGI:UniProtKB.
DR GO; GO:1905815; P:regulation of dorsal/ventral axon guidance; IGI:UniProtKB.
DR GO; GO:1905812; P:regulation of motor neuron axon guidance; IGI:UniProtKB.
DR GO; GO:1905606; P:regulation of presynapse assembly; IGI:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; IMP:WormBase.
DR GO; GO:1905489; P:regulation of sensory neuron axon guidance; IGI:UniProtKB.
DR GO; GO:0090128; P:regulation of synapse maturation; IC:ComplexPortal.
DR GO; GO:0050807; P:regulation of synapse organization; IMP:UniProtKB.
DR GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IC:ComplexPortal.
DR Gene3D; 2.130.10.30; -; 2.
DR Gene3D; 2.60.120.820; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR012983; PHR.
DR InterPro; IPR038648; PHR_sf.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF03256; ANAPC10; 1.
DR Pfam; PF08005; PHR; 2.
DR Pfam; PF00415; RCC1; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM01337; APC10; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF50985; SSF50985; 1.
DR PROSITE; PS51284; DOC; 1.
DR PROSITE; PS00626; RCC1_2; 1.
DR PROSITE; PS50012; RCC1_3; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cell projection; Direct protein sequencing; Metal-binding;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..3766
FT /note="E3 ubiquitin-protein ligase rpm-1"
FT /id="PRO_0000055970"
FT REPEAT 631..682
FT /note="RCC1 1"
FT /evidence="ECO:0000255"
FT REPEAT 725..784
FT /note="RCC1 2"
FT /evidence="ECO:0000255"
FT REPEAT 785..836
FT /note="RCC1 3"
FT /evidence="ECO:0000255"
FT REPEAT 838..892
FT /note="RCC1 4"
FT /evidence="ECO:0000255"
FT DOMAIN 2870..3046
FT /note="DOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00614"
FT ZN_FING 3331..3379
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 3517..3568
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 109..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1205
FT /note="PHR domain 1"
FT /evidence="ECO:0000250"
FT REGION 1503..1655
FT /note="PHR domain 2"
FT /evidence="ECO:0000250"
FT REGION 2351..2377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2626..2645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3628..3764
FT /note="Tandem cysteine domain"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT ACT_SITE 3647
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT ACT_SITE 3698
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 3336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 3339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 3361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 3368
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 3517
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 3520
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 3535
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 3537
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 3540
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 3543
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 3564
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 3567
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 3633
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 3636
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 3663
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 3666
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 3675
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 3678
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 3687
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 3690
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 3691
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 3705
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 3708
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 3726
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 3740
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 3746
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 3757
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 3760
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT SITE 3699
FT /note="Important for catalysis"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT SITE 3704
FT /note="Important for catalysis"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT SITE 3712
FT /note="Important for catalysis"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT MUTAGEN 2084
FT /note="V->A: Does not bind rae-1; when associated with A-
FT 2087 and A-2088."
FT /evidence="ECO:0000269|PubMed:22357847"
FT MUTAGEN 2087
FT /note="I->A: Does not bind rae-1; when associated with A-
FT 2084 and A-2088."
FT /evidence="ECO:0000269|PubMed:22357847"
FT MUTAGEN 2088
FT /note="R->A: Does not bind rae-1; and when associated with
FT A-2084 and A-2087."
FT /evidence="ECO:0000269|PubMed:22357847"
FT MUTAGEN 3597
FT /note="R->C: In ky346; total number of the synaptic vesicle
FT GFP puncta is reduced. Overextension of ALM neuron axon
FT which terminates with a hook. PLM neuron axon terminates
FT with a hook. Severe loss of synaptic branch formation in
FT PLM neuron."
FT /evidence="ECO:0000269|PubMed:10839353,
FT ECO:0000269|PubMed:21968191"
FT MUTAGEN 3675
FT /note="C->Y: In ju44; total number of the synaptic vesicle
FT GFP puncta is reduced."
FT /evidence="ECO:0000269|PubMed:10839353"
SQ SEQUENCE 3766 AA; 418058 MW; EAB59E816C5BBF4D CRC64;
MSFFLREIDG ERVCSTSTET SIPEDRKSAR RLRKLLYKCA ENTCKPDILR VPAHCGKLDK
EEEKSKTPLD QQQQINFHDI LNSKFVVGPP SPFALVAIAK SILARFGNPE EVSEKEDGSE
EEAGTSGADE EGKQYKNTDQ LVGASLTCIF EVLEQLSRRD AELCVQALES LLSLIQSMPI
DCLQSENRLS MSAMMHVLKT LREDACPSVS SKATSCLVAL SVACGEPEHL GSTIRSLICM
KKNIRMSADS TYDMIQMPEN LRKLLLKVRR KALGGDNTAN SPPNWAMVDV HEHSVASSFS
LPSLPDSSPS SDTPDDDNRI HSTMACDGTF LYILNYVGLY KLGTGLNETI SGKLYAANQS
LQSSKNVQMY LCNGSLYLRR NYSSCISVID TDSLLDIGEV ILPPSCVQHA LFTDGTYFYS
ATLIANSTLS TIQLNDSFSP SNEPSSRRSH RLTDVKFTIQ GDLQVPHQLP EFLPANLHPQ
TVDLHFTREM AFIQARSGKV YYAGNGTRFG LFETGNNWME LCLPEPIVQI SVGIDTIMFR
SGAGHGWIAS VDDKKRNGRL RRLVPSNRRK IVHVCASGHV YGYVSENGKI FMGGLHTMRV
NVSSQMLNGL DNVMISSLAL GKSHGVAVTR NGHLFTWGLN NMNQCGRVES TSTTSSPRHS
GRQEYQICPI GEHTWLTDTP SVCAQCGLCS ARGVACGRVP RPKGTMCHCG VGESTCLRCG
LCRPCGEVTE PAQPGRAQHV QFSSTAAPQR STLHPSRVIL SQGPHDVKVS SVSCGNFHTV
LLASDRRVFT FGSNCHGQLG VGDTLSKNTP QQVILPSDTV IVQVAAGSNH TILRANDGSV
FTFGAFGKGQ LARPAGEKAG WNAIPEKVSG FGPGFNAFAG WIGADGDSSI IHSHTALLSS
DNILKAQIVA NKTNIFIFPR EVGKDYIVIR RKLNVFEHHA SDYKCWYTSW ATDPKYDMLW
YYNSAEMEIK GYDIFKKSEK SVGDAFDSLT FLAGAEFAVQ VYDSPAYATS MSLGMQLLSA
TFSANVINLS EFWKEKHGER EQDHEKTIMD GYSVANRFDG TGGGWGYSAN SVEAIQFKVS
KEIRLVGVGL YGGRGEYISK LKLYRQIGTE ADELYVEQIT ETDETVYDCG AHETATLLFS
QPIVIQPNHW HVVSAKISGP SSDCGANGKR HVECDGVTFQ FRKSAVSNNG TDVDVGQIPE
LYYQIVGGSE SRDESDSNKQ LSISRDMSNL FSPAALKNVT AEGIGNLLIL LEWALQRVQI
DEDTNNQVEG SAENQWSQER AGFVAILSMK LISRFVRTVY KEKGCHDEPG IDFANKLVNL
HSMLLEFFFS TDMTGYENRP LIKKEEKVVE EGYTLMKCVS EAVKLFISLS HCFMGSRSLM
NAHLIAVMNK GNHEALILTS AIIGSLAKIE RFAHQLLCST TTTERFPMLS SLLLKHFNCE
KETLASLTSF PNILRFLYDQ TFMRNAYENT SSLAEAILVK VSRDLAIPTD DTLMGPVVHQ
TSSRFRRRSA QPTWDMSDGC ADAIAFRVDS EGIKLHGFGI YLPTEPDRRN FVGEIMMLSP
DSSEKWTCLL RVTAEMSSEE KEVGIVRFPE YVLLSPGVTY AVKVNMMKNT KTFCGEGGVT
QVHLLNGARL FFSGCSMSQN GTTVQRGQLP YLIYSILDQS NSLQIKQETI YDTFTLLLRL
MANKIGAAIT EGGALPACCQ HLMSHINPHV MVYMERFPDK ALEMMSTMEQ LIPMVSNLNG
VERVFHSYDS DDSGCDTPYS GIVTTVVESQ HPYKPNTSSS MVLLFEEADY ICVRFSPDCQ
TAQFDDQLTI YLKIDEHSYM PIERCYGSEW PSYPMILPGN CLMFVLDASS AVEGATSEQM
FGYHVTVTGY LVGYNDSTMR LEQDLVWLSA NACRIMTQLP INPSNIEHLS TAEDDTRHLF
EKHGSLLKKG LSLSHSPTLS ELCTKGQPPP AQSADLQFLR EFLSGHTSTS AGFLAKWLPT
GSVVDASKCQ LSLSHDDLIV GKAVTLKLLC KDQYDREVDC PKLQVEVFAS LGHRNPSSTI
HQNLHIGNLP SSLLIHQNPF QPIIVNHTRY MNIAAMPAYA NYSVEEIRLG FMIEELVKDR
VPLKSSDSSL FSGTWTPTTA GKYRIECKVD GSDISHTYTV EVTERPHRAG KGTITKPSGS
RRGAQMTVAR TVSIPFSSDF SGIRMRLGTT LASTSVGVIP RGALVEFIEE MDNDDGKWIR
LTDETALLYG CNQGVGQVWC LAYHRPLQRE LIPLKADTDR EKAVKLRRKE IEKESNGSKH
HSVSIDAKET YILSPNDVLQ VYSTPAPHSM IDGEKIIGPC DLMSSGWLAN RHGVWIKLTG
VEKYVLQKND PSSETSLSFS TNGNDEEDLE RPIERKKTRL PNALTPSVAD CIRAVFAAFV
WHEHLVKDLM AAAAYLRFHQ NLHNIWQSCE IPSCTNAPAA LQPIVKIWRE ICEVVETSVE
QHLIMPPVSN KAMRAETVKP PSRSGGCELC DANITVPLTV HLRMAHPGCG GDCLGYGYNS
NGKFTTGWSG ECGAGGRGQS PWYLLCNTCR SQYLKKTPAG HHQERTRRWR EFRFSTSASD
ARPEVIIRQN AMFLLDLNSR LQTESNSSST ATSGWTINLF PTHLSTPSTM PRSQQKRLDV
PPNNSVHQNS YMKLGYSSDP GPKVNVIMSP PNQGADQSAS LNRPGPSAIN EPAEVLQSPS
AALRTLFSNT NPSTSALLKR PVLAFCVEHH DLKRIKSACV QSVRRAVAFS HAFRVWNWLL
RMVSSEYSVS DIILQYLTTL TSYNRLAEYM FSAKKNSNIL PHPWRLCFLA GPIAADMVTQ
LHAFLHTVSI ILQSAGVDGR LKSLCFKSWT LQLTAQEQDL LILTCNILGT VGGILSDTSI
LDSDNRFVKE MKDITKFADI TASSRQAMVI CLTDESGETF WESGEEDKNR SRSLSVQLDE
SAHGEILSLF IDNARDEGYR ISSIAFKAIL EDGRRKDLTS LTLESAYCGW LKCCIKDISH
IQIQFKGPNP ASRIRQLMIL GYPAKTTGTP RLAPSTSHHL FFSDTQRDAF ALFQAISSQA
FCGELSEDDT LRERVIDLLF SRVQLYPLQN YVYTQVVQAM EKEVELLCDK SKRNYSYCCG
LMSLLVRICD SRGNMDSFGQ RNSVLTSITQ LLIFSPVVVQ RQCLNSLECI FASFTPSNVE
VPKIIRNLLV VVGKVIQLQV RDKAAHTVVT VHLCSSVLNA PQNWRVDKSI DMDIGRQTAV
LVENLCNGTY TPEWSNATKC ELANCLLSLI QMPESVSYTE TLSTGGKSKA VAVVSSKRFW
TAISSLSLIK DKSWLELSER WKTVQDEEDQ EPVLLCENHD DGHTVAQVFC VDCDVALCKE
CFTVMHLHKK NRNHGVKNLV QSSTQHDINI HQGCARMKFL NFLILFHGEA LNGMVEVAAD
TLFPTSTSSI QPAMQSSSAF LGIHPMTCRF CGNNVPVEDQ SLDGTCTHED CVNYAKTACQ
VMHTCNHFCG GIRNEEECLP CMTCKREDAA QDGDDVCVIC FTERLGAAPC IRLGCGHMFH
FHCVRMILER RWNGPRIVFR FMQCPLCIQP IEHSGLQDLI EPLKTIRQEV VDKAKMRLEY
DGLLTTPALT DPRSEFYNQP EEYALDRYMY VLCHKCKKAY FGGESRCQAA LDSSQFNPEE
LLCGGCSDTS GVQVCPRHGV EYLEYKCRFC CSIAVYFCFG TTHFCAPCHD DFQRLMSLPK
HLLPTCPVGP RSTPMEEQTC PLKMKHPPTG DEFAMGCGIC RNISTF
