MD1L1_CRIGR
ID MD1L1_CRIGR Reviewed; 717 AA.
AC Q80YF0;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Mitotic spindle assembly checkpoint protein MAD1;
DE AltName: Full=Mitotic arrest deficient 1-like protein 1;
DE Short=MAD1-like protein 1;
GN Name=MAD1L1; Synonyms=MAD1;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Jeang K.-T., Yedavalli V.S.;
RT "Cloning of Hamster mitotic checkpoint protein (MAD1).";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the spindle-assembly checkpoint that prevents
CC the onset of anaphase until all chromosomes are properly aligned at the
CC metaphase plate (By similarity). Forms a heterotetrameric complex with
CC the closed conformation form of MAD2L1 (C-MAD2) at unattached
CC kinetochores during prometaphase, recruits an open conformation of
CC MAD2L1 (O-MAD2) and promotes the conversion of O-MAD2 to C-MAD2, which
CC ensures mitotic checkpoint signaling (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y6D9}.
CC -!- SUBUNIT: Homodimer (By similarity). Dimerizes via its N- and
CC C- terminal regions (By similarity). Heterodimerizes with MAD2L1 in
CC order to form a tetrameric MAD1L1-MAD2L1 core complex (By similarity).
CC Interacts with the closed conformation form of MAD2L1 (C-MAD2) and open
CC conformation form of MAD2L1 (O-MAD2) (By similarity). It is unclear
CC whether MAD1L1 dimerization promotes the conversion of closed to open
CC conformation of MAD2L1 (By similarity). Formation of a heterotetrameric
CC core complex containing two molecules each of MAD1L1 and of MAD2L1
CC promotes binding of another molecule of MAD2L1 to each MAD2L1,
CC resulting in a heterohexamer (By similarity). Perturbation of the
CC original MAD1L1-MAD2L1 structure by the spindle checkpoint may decrease
CC MAD2L1 affinity for MAD1L1 (By similarity). CDC20 can compete with
CC MAD1L1 for MAD2L1 binding, until the attachment and/or tension dampen
CC the checkpoint signal, preventing further release of MAD2L1 on to CDC20
CC (By similarity). Also able to interact with the BUB1/BUB3 complex (By
CC similarity). Interacts with NEK2 (By similarity). Interacts with TTK
CC (By similarity). Interacts with TPR; the interactions occurs in a
CC microtubule-independent manner (By similarity). Interacts with IK (By
CC similarity). Interacts with the viral Tax protein (By similarity).
CC Interacts with PRAP1 (By similarity). {ECO:0000250|UniProtKB:Q9Y6D9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y6D9}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9Y6D9}.
CC Nucleus envelope {ECO:0000250|UniProtKB:Q9Y6D9}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9Y6D9}.
CC Note=Detected at the nucleus envelope during interphase. From the
CC beginning to the end of mitosis, it is seen to move from a diffusely
CC nuclear distribution to the centrosome, to the spindle midzone and
CC finally to the midbody. Detected at kinetochores during prometaphase.
CC Colocalizes with NEK2 at the kinetochore. Colocalizes with IK at
CC spindle poles during metaphase and anaphase.
CC {ECO:0000250|UniProtKB:Q9Y6D9}.
CC -!- PTM: Phosphorylated; by BUB1. Become hyperphosphorylated in late S
CC through M phases or after mitotic spindle damage.
CC {ECO:0000250|UniProtKB:Q9Y6D9}.
CC -!- SIMILARITY: Belongs to the MAD1 family. {ECO:0000305}.
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DR EMBL; AY247792; AAO91656.1; -; mRNA.
DR RefSeq; NP_001233712.1; NM_001246783.1.
DR AlphaFoldDB; Q80YF0; -.
DR SMR; Q80YF0; -.
DR STRING; 10029.NP_001233712.1; -.
DR PRIDE; Q80YF0; -.
DR Ensembl; ENSCGRT00001015679; ENSCGRP00001011447; ENSCGRG00001013089.
DR GeneID; 100689352; -.
DR KEGG; cge:100689352; -.
DR CTD; 8379; -.
DR eggNOG; KOG4593; Eukaryota.
DR GeneTree; ENSGT00390000001316; -.
DR OMA; YMLLGYR; -.
DR OrthoDB; 602490at2759; -.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:1990706; C:MAD1 complex; IEA:Ensembl.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:1990728; C:mitotic spindle assembly checkpoint MAD1-MAD2 complex; IEA:Ensembl.
DR GO; GO:0097431; C:mitotic spindle pole; IEA:Ensembl.
DR GO; GO:0044615; C:nuclear pore nuclear basket; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0043515; F:kinetochore binding; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:Ensembl.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IEA:Ensembl.
DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; IEA:Ensembl.
DR GO; GO:0090235; P:regulation of metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR InterPro; IPR008672; Mad1.
DR PANTHER; PTHR23168; PTHR23168; 1.
DR Pfam; PF05557; MAD; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Cytoplasm; Cytoskeleton; Isopeptide bond; Kinetochore;
KW Mitosis; Nucleus; Phosphoprotein; Ubl conjugation.
FT CHAIN 1..717
FT /note="Mitotic spindle assembly checkpoint protein MAD1"
FT /id="PRO_0000213799"
FT REGION 380..532
FT /note="Necessary for interaction with NEK2"
FT /evidence="ECO:0000250"
FT REGION 540..551
FT /note="Necessary for interaction with MAD2L1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6D9"
FT COILED 46..631
FT /evidence="ECO:0000255"
FT MOTIF 79..82
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6D9"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6D9"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6D9"
FT MOD_RES 61
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6D9"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6D9"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6D9"
FT CROSSLNK 61
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6D9"
SQ SEQUENCE 717 AA; 83152 MW; 60D746C945D15443 CRC64;
MEDLGENTTV LSTLRSLNNF ISQRVEGGSG LDVSTAAPGS LQLQYEQSMQ LEERAEQIRS
KSYLIQMERE KMQMELSHKR ARVELERAAN TSARNYEREV DRNQELLARI RQLQEREAAA
EEKMQEQLER HRLCKQSLDA ASQQLRERED GLAAARETIS SLKGRVSEMQ LNAMDQKVQV
KRLESEKQEL KEQLELQQRK CQEASQKIQE LQASQEERAD HEQKIKDLEQ KLCLQEQDAA
VVKNMKSELL RLPRMERELK RLREENTHLR EMKETNGLLT EELEGLQRKL GRQEKMQEAL
VDLELEKEKL LAKLQSWEKL DQTMGVNLRT PEDLSRFVVE LQQRELTLKE KNNTITSSAR
GLEKAQQQLQ DEVRQVSAQL LEERKKREIH EALARRLQKR IVLLTKERDG MRAILGSYDS
ELTQAEYSAQ LTQRMWEAED MVQKVHAHSS EMETQLSQAL EELGVQKQRA DTLEMELKML
RAQTSSAETS FPFCKEEVDA LRLKVEELEG ERSRLEQEKQ ALEMQMERLT LQGDYNQSRT
KVLHMSLNPA SMARKRQQED HARLQGECER LRGLVHALER GGPIPADLEV ASSLPSSKEV
AELRKQVESA ELKNQRLKEV FQTKIQEFRK VCYTLTGYQI DVTTENQYRL TSRYAEHQSD
CLIFKATGPS GSKMQLLETE FSRSVPELIE LHLLQQDSIP AFLSALTIEL FSRQTSI
