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Database: UniProt
Entry: G1TYG9_RABIT
LinkDB: G1TYG9_RABIT
Original site: G1TYG9_RABIT 
ID   G1TYG9_RABIT            Unreviewed;       636 AA.
AC   G1TYG9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 2.
DT   24-JAN-2024, entry version 74.
DE   SubName: Full=Membrane palmitoylated protein 4 {ECO:0000313|Ensembl:ENSOCUP00000022133.2};
GN   Name=MPP4 {ECO:0000313|Ensembl:ENSOCUP00000022133.2};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000022133.2, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000022133.2, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000022133.2,
RC   ECO:0000313|Proteomes:UP000001811};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSOCUP00000022133.2}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000022133.2};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the MAGUK family.
CC       {ECO:0000256|ARBA:ARBA00007014}.
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DR   EMBL; AAGW02042203; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_017198522.1; XM_017343033.1.
DR   AlphaFoldDB; G1TYG9; -.
DR   SMR; G1TYG9; -.
DR   STRING; 9986.ENSOCUP00000022133; -.
DR   Ensembl; ENSOCUT00000029372.2; ENSOCUP00000022133.2; ENSOCUG00000012470.4.
DR   GeneID; 100349491; -.
DR   KEGG; ocu:100349491; -.
DR   CTD; 58538; -.
DR   eggNOG; KOG0609; Eukaryota.
DR   GeneTree; ENSGT00940000156444; -.
DR   HOGENOM; CLU_001715_5_0_1; -.
DR   InParanoid; G1TYG9; -.
DR   OrthoDB; 2873706at2759; -.
DR   TreeFam; TF314263; -.
DR   Proteomes; UP000001811; Chromosome 7.
DR   Bgee; ENSOCUG00000012470; Expressed in blood and 2 other cell types or tissues.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005912; C:adherens junction; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   CDD; cd00071; GMPK; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   CDD; cd12034; SH3_MPP4; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 1.10.287.650; L27 domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 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; IPR035600; MPP4_SH3.
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   PANTHER; PTHR23122:SF34; MAGUK P55 SUBFAMILY MEMBER 4; 1.
DR   PANTHER; PTHR23122; MEMBRANE-ASSOCIATED GUANYLATE KINASE MAGUK; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF02828; L27; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00569; L27; 2.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF101288; L27 domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 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   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          23..77
FT                   /note="L27"
FT                   /evidence="ECO:0000259|PROSITE:PS51022"
FT   DOMAIN          79..136
FT                   /note="L27"
FT                   /evidence="ECO:0000259|PROSITE:PS51022"
FT   DOMAIN          153..234
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          241..311
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          426..615
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          569..620
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   636 AA;  72422 MW;  8C25293DFD564168 CRC64;
     MIQSDRGAAP PDKDRKLSSA AKSENGLSHI LRLVLRELSL FYSRDVNGVC LLYDLLHSPW
     LQALLKVYDC LQEFQEKKLA PATHHAQALS REVLELLREA PNSPENQELR RILQAPHSKA
     LLSAHDTVAQ KDFEPLLPPL PDNIPESEEA MRIVCLVKNQ QPLGATIKRH ELTGDILVAR
     VIHGGLVERS GLLYAGDKLV EVNGISVEGL DPEQVIHILA MSRGTIMFKV VPVSDPPVNS
     QKMVYVRAMT DYWPQEDPAI PCMDAGLPFR KGDILQIVDQ NDALWWQARK ITDLATCAGL
     IPSKPLLKRK QREFWWSQPY QPHTCSKSTI LISMEEEDDM KIDEKCVEAD EETFESEELS
     EDKEEFVGYG EKFFIAGFRR SMRLCRRKSH LSQLRATVCC TGGCYSAVGA PYEEVVRYQR
     RPADKHRLIV LVGPSGVGVN ELRRQLIEFN PGHFQSAVPH TTRSKKSYEI NGREYHYVSR
     ETFESLIYSH RMLEYGEYKG HLYGTSVDAV QAVLDEGKVC VMDLEPQDIQ MARTQDLKPY
     VIFIKPSNMN CMKQSRKNAK IITDYFVDMK FKDEDLQEME DLAQKMEAQF GQFFDYVIVN
     DNLQDACARL LSVVQKAQEE PQWVPATWIS SDTESS
//
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