MPP7_DANRE
ID MPP7_DANRE Reviewed; 576 AA.
AC Q6P0D7; Q9PWC1; Q9W7F1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=MAGUK p55 subfamily member 7;
DE AltName: Full=Protein humpback;
GN Name=mpp7; Synonyms=dlg3, hmp;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-52, AND
RP MUTAGENESIS OF ARG-453 AND LYS-556.
RX PubMed=10446262; DOI=10.1016/s0925-4773(99)00098-2;
RA Koenig C., Yan Y.L., Postlethwait J., Wendler S., Campos-Ortega J.A.;
RT "A recessive mutation leading to vertebral ankylosis in zebrafish is
RT associated with amino acid alterations in the homologue of the human
RT membrane-associated guanylate kinase DLG3.";
RL Mech. Dev. 86:17-28(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as an important adapter that promotes epithelial cell
CC polarity and tight junction formation. Involved in the assembly of
CC protein complexes at sites of cell-cell contact (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Cell junction, tight junction {ECO:0000250}.
CC Cell junction, adherens junction {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be the ortholog of mammalian DLG3.
CC {ECO:0000305|PubMed:10446262}.
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DR EMBL; AF124435; AAD39392.1; -; mRNA.
DR EMBL; AF124436; AAD39393.1; -; Genomic_DNA.
DR EMBL; BC065660; AAH65660.1; -; mRNA.
DR RefSeq; NP_571051.1; NM_130976.1.
DR RefSeq; XP_009304860.1; XM_009306585.2.
DR AlphaFoldDB; Q6P0D7; -.
DR SMR; Q6P0D7; -.
DR STRING; 7955.ENSDARP00000072380; -.
DR PaxDb; Q6P0D7; -.
DR ABCD; Q6P0D7; 1 sequenced antibody.
DR Ensembl; ENSDART00000170376; ENSDARP00000141751; ENSDARG00000102470.
DR Ensembl; ENSDART00000181711; ENSDARP00000152963; ENSDARG00000102470.
DR GeneID; 30166; -.
DR KEGG; dre:30166; -.
DR CTD; 30166; -.
DR ZFIN; ZDB-GENE-991209-8; mpp7a.
DR eggNOG; KOG0609; Eukaryota.
DR GeneTree; ENSGT00940000156232; -.
DR InParanoid; Q6P0D7; -.
DR OMA; CDMLAAV; -.
DR OrthoDB; 531106at2759; -.
DR PhylomeDB; Q6P0D7; -.
DR TreeFam; TF314263; -.
DR Reactome; R-DRE-9013149; RAC1 GTPase cycle.
DR Reactome; R-DRE-9013404; RAC2 GTPase cycle.
DR Reactome; R-DRE-9013406; RHOQ GTPase cycle.
DR Reactome; R-DRE-9013408; RHOG GTPase cycle.
DR Reactome; R-DRE-9013409; RHOJ GTPase cycle.
DR Reactome; R-DRE-9013423; RAC3 GTPase cycle.
DR PRO; PR:Q6P0D7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 12.
DR Bgee; ENSDARG00000102470; Expressed in early embryo and 31 other tissues.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0071896; P:protein localization to adherens junction; IBA:GO_Central.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR014775; L27_C.
DR InterPro; IPR004172; L27_dom.
DR InterPro; IPR036892; L27_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF02828; L27; 2.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 2.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF101288; SSF101288; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS51022; L27; 2.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Cell junction; Membrane; Reference proteome; Repeat; SH3 domain;
KW Tight junction.
FT CHAIN 1..576
FT /note="MAGUK p55 subfamily member 7"
FT /id="PRO_0000320030"
FT DOMAIN 10..64
FT /note="L27 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 65..122
FT /note="L27 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 139..220
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 228..298
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 368..560
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT MUTAGEN 453
FT /note="R->H: In hmp; leads to vertebral ankylosis; when
FT associated with N-556."
FT /evidence="ECO:0000269|PubMed:10446262"
FT MUTAGEN 556
FT /note="K->N: In hmp; leads to vertebral ankylosis; when
FT associated with H-453."
FT /evidence="ECO:0000269|PubMed:10446262"
FT CONFLICT 173
FT /note="A -> V (in Ref. 1; AAD39392)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="P -> A (in Ref. 1; AAD39392)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 576 AA; 65192 MW; 3A30CDB533E45B80 CRC64;
MPALSSRSGS EMGLYELLSV LPSQLQPHVE SPDDRSFLHA MFGERSLHSL VKIHEKLQCY
EDCAPTPVLD SAGSLAADLT EELQARSASN EIRELVKLLS KPHVKSLLSV HDTVAKKSYD
PELPPLPDDI DDEEDSVKII RLVKNKEPLG ATIKKDEHTG AILVARILRG GAADRSGLIH
VGDELKEVNG IPVDDKKPEE IIRILSQSQG AITFKVVPGI KDEAQSKEPK MFIKALFDYN
PAEDKAIPCK EAGLGFKKGD ILQVMSQDDA TWWQAKLEGD GNLRAGLIPS KHFQERRLAV
WRPTPVMTLQ RTSSKRFSGL RRSFRLSRRD KKTNKSMYEC KKSEQYDTAD VPTYEEVTTY
RRKHGDRHRL VVLVGPTGVG LNELKRKLLI SDTQHFSVTI PHTSRSKRHQ ESEGVEYHFI
SKNLFEADIQ NNKFIEHGEY KGNYYGTSFD SVRSVLSKNK VCLLDVQPHT LKHLRTAEFK
PYVVFVKPPC IERLRETRRN AKVISGKDDK TSSKAFSEED FLEMISASQM MENQYGHLFE
KVIVNDDLTV AFSELKQALK KVETEAHWVP ISWTHS
