GRIP2_XENLA
ID GRIP2_XENLA Reviewed; 1083 AA.
AC A8E0R9; A2Q054; A8JL03;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Glutamate receptor-interacting protein 2;
DE Short=xGRIP2;
DE Short=xGRIP2.1;
GN Name=grip2 {ECO:0000312|EMBL:CAN52354.1};
GN Synonyms=grip2.1 {ECO:0000303|PubMed:17936745};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAF45467.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Ovary {ECO:0000312|EMBL:BAF45467.1};
RX PubMed=17320814; DOI=10.1016/j.bbrc.2007.02.059;
RA Kaneshiro K., Miyauchi M., Tanigawa Y., Ikenishi K., Komiya T.;
RT "The mRNA coding for Xenopus glutamate receptor interacting protein 2
RT (XGRIP2) is maternally transcribed, transported through the late pathway
RT and localized to the germ plasm.";
RL Biochem. Biophys. Res. Commun. 355:902-906(2007).
RN [2] {ECO:0000305, ECO:0000312|EMBL:ABO36653.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Oocyte {ECO:0000269|PubMed:17936745};
RX PubMed=17936745; DOI=10.1016/j.ydbio.2007.09.012;
RA Tarbashevich K., Koebernick K., Pieler T.;
RT "XGRIP2.1 is encoded by a vegetally localizing, maternal mRNA and functions
RT in germ cell development and anteroposterior PGC positioning in Xenopus
RT laevis.";
RL Dev. Biol. 311:554-565(2007).
RN [3] {ECO:0000305, ECO:0000312|EMBL:CAN52354.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Egg {ECO:0000269|PubMed:17924960};
RX PubMed=17924960; DOI=10.1111/j.1432-0436.2007.00229.x;
RA Kirilenko P., Weierud F.K., Zorn A.M., Woodland H.R.;
RT "The efficiency of Xenopus primordial germ cell migration depends on the
RT germplasm mRNA encoding the PDZ domain protein Grip2.";
RL Differentiation 76:392-403(2008).
CC -!- FUNCTION: Plays an important role in primordial germ cell (PGC)
CC maintenance and efficiency of PGC migration.
CC {ECO:0000269|PubMed:17924960, ECO:0000269|PubMed:17936745}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17320814,
CC ECO:0000269|PubMed:17936745}.
CC -!- TISSUE SPECIFICITY: Enriched in the mitochondrial cloud of stage I
CC oocytes, before becoming concentrated at the tip of the vegetal cortex
CC in stage II oocytes. Expression becomes localized to the germ plasm of
CC stage III-IV oocytes and early cleavage stages. At the tailbud stage,
CC localizes to the migrating primordial germ cells (PGCs) until PGC
CC migration is complete (stage 40), at which point expression disappears.
CC In the adult, expressed in the brain, ovary, eye, muscle, spinal cord
CC and very weakly in adipocytes. {ECO:0000269|PubMed:17320814,
CC ECO:0000269|PubMed:17924960, ECO:0000269|PubMed:17936745}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally. Prominent in the egg and
CC during early cleavage stages. Expression decreases slightly between
CC neurula and late tailbud stage before elevating again at the tadpole
CC stages. {ECO:0000269|PubMed:17320814, ECO:0000269|PubMed:17924960,
CC ECO:0000269|PubMed:17936745}.
CC -!- SIMILARITY: Belongs to the GRIP2 family. {ECO:0000305}.
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DR EMBL; AB290863; BAF45467.1; -; mRNA.
DR EMBL; EF139240; ABO36653.1; -; mRNA.
DR EMBL; AM712310; CAN52354.1; -; mRNA.
DR RefSeq; NP_001091382.1; NM_001097913.1.
DR AlphaFoldDB; A8E0R9; -.
DR SMR; A8E0R9; -.
DR PRIDE; A8E0R9; -.
DR GeneID; 100037236; -.
DR KEGG; xla:100037236; -.
DR CTD; 100037236; -.
DR Xenbase; XB-GENE-866534; grip2.L.
DR OrthoDB; 65191at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 100037236; Expressed in egg cell and 9 other tissues.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0032019; C:mitochondrial cloud; IDA:UniProtKB.
DR GO; GO:0045495; C:pole plasm; IDA:UniProtKB.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IEA:InterPro.
DR GO; GO:0007281; P:germ cell development; IMP:UniProtKB.
DR GO; GO:0008354; P:germ cell migration; IMP:UniProtKB.
DR Gene3D; 2.30.42.10; -; 7.
DR InterPro; IPR043545; GRIP1/2.
DR InterPro; IPR030029; GRIP2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR46227; PTHR46227; 1.
DR PANTHER; PTHR46227:SF4; PTHR46227:SF4; 1.
DR Pfam; PF00595; PDZ; 6.
DR Pfam; PF17820; PDZ_6; 1.
DR SMART; SM00228; PDZ; 7.
DR SUPFAM; SSF50156; SSF50156; 7.
DR PROSITE; PS50106; PDZ; 7.
PE 2: Evidence at transcript level;
KW Cytoplasm; Developmental protein; Reference proteome; Repeat.
FT CHAIN 1..1083
FT /note="Glutamate receptor-interacting protein 2"
FT /id="PRO_0000334504"
FT DOMAIN 58..141
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 156..244
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 258..342
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 468..555
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 569..652
FT /note="PDZ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 667..749
FT /note="PDZ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 974..1056
FT /note="PDZ 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 408..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..965
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 41
FT /note="A -> V (in Ref. 2; ABO36653)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="K -> R (in Ref. 2; ABO36653)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="S -> G (in Ref. 3; CAN52354)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="S -> N (in Ref. 2; ABO36653)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="S -> F (in Ref. 1; BAF45467)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="S -> N (in Ref. 2; ABO36653)"
FT /evidence="ECO:0000305"
FT CONFLICT 673
FT /note="Y -> C (in Ref. 2; ABO36653)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1083 AA; 118461 MW; 8610588A33F5B388 CRC64;
MHFFQTILRW KTAKGQKSVT FKKDDGPYSK GNKDPAGNDL ALVSRRQSIP EEFRGVTIVE
LIKKEGSTLG LTISGGTDKD GKPRVSNLRP GGLAARSDQL NIGDYIKSVN GINLTKLRHE
EIISLLKNVG ERVVLEVEYE LPPGTPDNSS AIIPKTIEIT LCKEGNSFGF VMRGGAHEDW
HKSRALVVTY VRPGGPADRE GTLKVGDRLL CVDGISLHNI THTDALSILR QCSQEGVFQI
EYDVALMDTV TNASGPLLVE IAKTPGSTLG ISLSTGTHRN KQVIVIDKVK PASVVDRCGA
LHPGDHILSI DGTSTEHCTQ MEATQLLASI IENVKLEILP AHHSRLPLRP PETVKVQKSD
HHHCWDPCVN YCHTPHPGHC KTPTWNPTSN QDYCKSLVAA NFSSSSVAGT PGFSSQNSNT
LPRTVHPMSP RTTMNRRRQK RKDHKSSLSL ASSTVGPGGQ IIHTESTEII LRGDPLNGFG
IQLQGGIFAT ETLSSPPLIR FIEPDSPAER CGLLQVGDRL LSINGILTED GTLEEANQLL
RDAALSNKVA LEIEFDVAES VVPSSGTFHV KLPKRKGVEL GITISSSRKP GEPLIISDIK
KGSVAHRTGT LEPGDKLLAI DNIRLDNCSM EDAVQILRQC EDLVKLKIRK DEDNSDEQET
SGAIIYTVEL KRYGGPLGIT ISGTEEPFDP IVISGLTKRG LAERTGAIHI GDRILAINNI
SLKGKPLSEA IHLLQMAGET VTLKIKKQTE RIFPQRLSDS MNEGSDPEDD LTDSQKTSKL
SEIYSTTVPS VDSALESWDG SGIDAGYGSQ GTYVPQAVGI SLHPHEWRTS RQKSNTPPVE
HRKSYPFLDG SFNEQDWEKP TRYPSQPNGL ETDHDDSFWR VFGEALEDLE TCGQSELLRE
IEASIMTGSV QDLGLDSSQI LLENSSQGGH VLFRRGSHHI SSNSPKKENK LSQDARSKKE
EVHNAQSLTT ELLKVTVQKD MDTDDFGFSV SDGLLEKGVY VNMIRPGGPA DRSGLKTYDQ
ILQVNHVRTR DFDCCLTVPL LSDAGDRLDL VISRGLSIKA EEMGVEQIKG PLRMETQTST
KTL
