ID A0A1A9ZHJ3_GLOPL Unreviewed; 503 AA.
AC A0A1A9ZHJ3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|RuleBase:RU361183, ECO:0000256|RuleBase:RU369076};
DE Includes:
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
DE Includes:
DE RecName: Full=Protein zwilch {ECO:0000256|RuleBase:RU369076};
OS Glossina pallidipes (Tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=7398 {ECO:0000313|EnsemblMetazoa:GPAI014831-PA, ECO:0000313|Proteomes:UP000092445};
RN [1] {ECO:0000313|Proteomes:UP000092445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAEA {ECO:0000313|Proteomes:UP000092445};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GPAI014831-PA}
RP IDENTIFICATION.
RC STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPAI014831-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- FUNCTION: Essential component of the mitotic checkpoint, which prevents
CC cells from prematurely exiting mitosis. Required for the assembly of
CC the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its
CC function related to the spindle assembly machinery is proposed to
CC depend on its association in the mitotic RZZ complex.
CC {ECO:0000256|RuleBase:RU369076}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01211,
CC ECO:0000256|RuleBase:RU361183};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
CC -!- SUBUNIT: Component of the RZZ complex. {ECO:0000256|RuleBase:RU369076}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000256|RuleBase:RU369076}.
CC -!- SIMILARITY: Belongs to the ZWILCH family.
CC {ECO:0000256|RuleBase:RU369076}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01211}.
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DR AlphaFoldDB; A0A1A9ZHJ3; -.
DR STRING; 7398.A0A1A9ZHJ3; -.
DR EnsemblMetazoa; GPAI014831-RA; GPAI014831-PA; GPAI014831.
DR VEuPathDB; VectorBase:GPAI014831; -.
DR Proteomes; UP000092445; Unassembled WGS sequence.
DR GO; GO:1990423; C:RZZ complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:UniProtKB-UniRule.
DR GO; GO:0034501; P:protein localization to kinetochore; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR018630; Zwilch.
DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR PANTHER; PTHR10127:SF850; METALLOENDOPEPTIDASE; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF09817; Zwilch; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51864; ASTACIN; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|RuleBase:RU369076};
KW Cell division {ECO:0000256|RuleBase:RU369076};
KW Centromere {ECO:0000256|RuleBase:RU369076};
KW Chromosome {ECO:0000256|RuleBase:RU369076};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Kinetochore {ECO:0000256|RuleBase:RU369076};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metalloprotease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183}; Mitosis {ECO:0000256|RuleBase:RU369076};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT DOMAIN 308..421
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT ACT_SITE 403
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 412
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 503 AA; 56102 MW; 7F6BAFB78F2A4591 CRC64;
MGLISAKAIT TQSLLKDHFF AVGVEGTSIE TEIENIYQIK NNITIRGCWS TVSPLPPLID
LSTCDVILKF RTDGCHPLTD DFLNQLRILI SIREDILSFK KSEDSDIIRE PVYRCGIGIE
ISEVRENINK AMLEMAEILP THSTECDIED VIQNAKLRRF NDLTDNLWEI LKRCSSYKYL
KLAFNVLFQS AARSNIVEGL SFRIRLSETM TKLLLLTLCA IFEQFRTIPL PLTDIDDNIV
EIDSVHYLEE PENLRYIIDL SFFGTNIYGV PDEATAQLVA NYSATESSVN PEELGSNLEG
DILMPEDQLL TKNGIFAPNG VVPFEIGSNY NARELSVIEH ALEQFHSYTC VRFVPRTGQD
NDYVSIANGN SGCWSTVGRT GGRQEVNLQS PGCLLKSGAA IHELMHALGF LHEQNRQERD
DCHTRPLADV MGQRNSFSAF DIEKLNKMYD CGYLSPPPVS GPDAVSNGIE SNVVNSFVGG
FLTGLALAEE KVDVSIKRVI SRG
//
