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Database: UniProt
Entry: A0A452DL34_CAPHI
LinkDB: A0A452DL34_CAPHI
Original site: A0A452DL34_CAPHI 
ID   A0A452DL34_CAPHI        Unreviewed;      1920 AA.
AC   A0A452DL34;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Discs large MAGUK scaffold protein 5 {ECO:0000313|Ensembl:ENSCHIP00000000550.1};
GN   Name=DLG5 {ECO:0000313|Ensembl:ENSCHIP00000000550.1};
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000000550.1, ECO:0000313|Proteomes:UP000291000};
RN   [1] {ECO:0000313|Ensembl:ENSCHIP00000000550.1, ECO:0000313|Proteomes:UP000291000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA   Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA   Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA   Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA   Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT   "Polished mammalian reference genomes with single-molecule sequencing and
RT   chromosome conformation capture applied to the Capra hircus genome.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCHIP00000000550.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   EMBL; LWLT01000030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_017897746.1; XM_018042257.1.
DR   Ensembl; ENSCHIT00000000576.1; ENSCHIP00000000550.1; ENSCHIG00000000389.1.
DR   GeneID; 102170667; -.
DR   CTD; 9231; -.
DR   GeneTree; ENSGT00940000155303; -.
DR   OrthoDB; 2877432at2759; -.
DR   Proteomes; UP000291000; Chromosome 28.
DR   Bgee; ENSCHIG00000000389; Expressed in ovary and 17 other cell types or tissues.
DR   GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR   CDD; cd00992; PDZ_signaling; 4.
DR   CDD; cd11860; SH3_DLG5; 1.
DR   Gene3D; 2.30.42.10; -; 4.
DR   Gene3D; 1.10.533.10; Death Domain, Fas; 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; IPR001315; CARD.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR006907; DLG5_N.
DR   InterPro; IPR035537; DLG5_SH3.
DR   InterPro; IPR008145; GK/Ca_channel_bsu.
DR   InterPro; IPR008144; Guanylate_kin-like_dom.
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; PTHR46360; DISKS LARGE HOMOLOG 5; 1.
DR   PANTHER; PTHR46360:SF1; DISKS LARGE HOMOLOG 5; 1.
DR   Pfam; PF16610; dbPDZ_assoc; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF00595; PDZ; 4.
DR   Pfam; PF04822; Takusan; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00228; PDZ; 4.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF47986; DEATH domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 4.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50209; CARD; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS50106; PDZ; 4.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          1..90
FT                   /note="CARD"
FT                   /evidence="ECO:0000259|PROSITE:PS50209"
FT   DOMAIN          620..710
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          705..796
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          1349..1428
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          1502..1583
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          1594..1662
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          1776..1906
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   REGION          116..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          879..1121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1138..1186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1201..1322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1432..1497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          146..264
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          303..358
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          383..599
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        879..898
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1031..1045
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1046..1060
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1085..1112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1153..1171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1245..1271
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1289..1322
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1432..1460
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1478..1494
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1920 AA;  213654 MW;  B160EACB63E7A4DD CRC64;
     MEPQRRELLA QCQQSLAQAM TEVEAVLGLL EAAGALSPGE RRQLDEEAGG AKAELLLKLL
     LAKERDHFHD LRAALEKTQP HLLPILYLNG VVGPPQPAEG AGSTYSVLSI MPSDSESSSS
     LSSVGTTGKA PSPPPVLSDR QVNEKVENLS IQLRLMTRER NELRKRLAFA THGTTFDKRP
     YHRLNPDYER LKIQCVRAMS DLQSLQSQHT NALRRCEEVA KETDFYHTLH SRLLSDQTQL
     KDDVDMLRRE NGQLLRERNL LQQSWEDMKR LHEEDQKEIG DLRAQQQQVL KHNGSSEILN
     KLYDTAMDKL EVVKKDYDAL RKRYSEKVAI HSSDLSRLEQ LEEENQRLLK QTEMLTQQRD
     TAIQLQHQCA LSLRRFEAIH HELNKATAQN KDLQWEMELL QSELTELRTT QAKTAKESEK
     YKEERDAVYS EYKLIMSERD QVISELDKLQ TEVELAESKL KSSTSEKKAA SEEMEALRQI
     KDTVTMDAGR ANKEAEILRK QCKALCQELK EALQEADVAK CRRDWAFQER DKIVAERDSI
     RTLCDNLRRE RDRAVSELAE ALRSLDDTRK QKNDVSRELK ELKEQMESQL EKEARFRQLM
     AHSSHDSAID TDSMEWETEV VEFERETEDI DLKALGFDMA EGVNEPCLPG DCGIFVTKVD
     KGSIADGRLR VNDWLLRIND VDLINKDKKQ AIKALLNGEG AINMVVRRRK SLGGKVVTPL
     HINLSGHKDS GISLENGVYA AAVVPGSPAA KEGSLAVGDR IVAINGIALD NKSLNECESL
     LRSCQDSLTL SLLKVFPQSA SWSGQNIFEN IKDSDKMLSY RAHGPEVQAQ NKRNLMQHNN
     STQTDIFYAD RLEDRKELGP PGGSSSFLHK PFSGGPFSVS PQACPSASER SLSSFRSDAS
     GERGYGPADV RSRRPLLPFE TEVGPCGAAE APLDKAEPDN THSGGTWPKA VLSSMAGPEK
     LSVYRKPKQR KSIFDPNTFK RPQTPPKIDY LLPGSGPAHS PLPSKRVGPL TPPKPPRRGD
     SIKFQHKLET SSESEATLVG SSPSTSPPSA LPPDMDPGDP MHASPPRKAR VRIASSYCPE
     GDRDPSCLPA KKSCDEDLTS QKADELGQKR RRPKSAPIFR PKLAPVVIPA QFLEEQKCTP
     ASGELSPDLQ EWSPYSPGHS SRHSNPPFYP SRASVGTVPR SMAPSTVSSV LRNPIYTVRS
     HRVGPCSSPP IPREVGPHGL HPSVQHQGRL SLDLSPRACS DCSDMRASHG SNSLPSSARL
     GSSSNLQFKA ERIKIPSTPR YPRSVVGSDR GSLSHSECST PPQSPLSVEG LSSCSQPQTS
     AATLPRIAVN PAAPGERRKD RPYVEEPRHV KLQKGSEPLG ISIVSGEKGG VYVSKVTGGS
     IAHQAGLEYG DQLLEFNGIN LRSATEQQAR LIIGQQCDTI TILAQYNPHM HQLSSHSRSS
     SHLDPAGIHS TLQGSGATTP EHPSVIDPLM EQDEGPGTPP AKQSTPSSRT VGDATKKTPE
     PRVVFIKKSQ LELGVHLCGG NLHGVFVAEV EDDSPAKGAD GLVPGDLILE YGGLDVRSKT
     VEEVYVEMLK PKDSVRLKVQ YRPEEFSKVK GLPGDSFYIR ALYERLAEVE PELSFKKDDI
     LYVDDTLPQG SFGSWMAWQL DENAQKIQRG QIPSKYVMDQ EFSRRLSMSE VKDENSAAKT
     LSAAARRSFF RRKHKHKRSG SKDGKDLLAL DTFSNDSIPL FEDSVSLAYQ RVQKVDCTSL
     RPVLILGPFL DVVKEMLVNE APGKFCRCPL EVMKASQQAI ERGVKDCLFV DYKRRSGHFD
     VTTVASIKEI TEKNRHCLLD VAPHAIERLH HMHIYPIVIF IHYKSAKHIK EQRDPIYLKD
     KVTQRHSKEQ FETAQKIEQE YSRYFTGVVQ GGALSSICTQ ILAVVNQEQN KVLWIPACPL
//
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