ID L5KRU3_PTEAL Unreviewed; 656 AA.
AC L5KRU3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=MAGUK p55 subfamily member 2 {ECO:0000313|EMBL:ELK14152.1};
GN ORFNames=PAL_GLEAN10004224 {ECO:0000313|EMBL:ELK14152.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK14152.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000256|ARBA:ARBA00004435}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004202}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC {ECO:0000256|ARBA:ARBA00007014}.
CC -!- SIMILARITY: Belongs to the NPY family. {ECO:0000256|ARBA:ARBA00010022,
CC ECO:0000256|RuleBase:RU000656}.
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DR EMBL; KB030578; ELK14152.1; -; Genomic_DNA.
DR AlphaFoldDB; L5KRU3; -.
DR STRING; 9402.L5KRU3; -.
DR eggNOG; KOG0609; Eukaryota.
DR InParanoid; L5KRU3; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR CDD; cd00071; GMPK; 1.
DR CDD; cd00126; PAH; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd12037; SH3_MPP2; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 6.10.250.900; -; 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; IPR035602; MPP2_SH3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001955; Pancreatic_hormone-like.
DR InterPro; IPR020392; Pancreatic_hormone-like_CS.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23122:SF35; MAGUK P55 SUBFAMILY MEMBER 2; 1.
DR PANTHER; PTHR23122; MEMBRANE-ASSOCIATED GUANYLATE KINASE MAGUK; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00159; Hormone_3; 1.
DR Pfam; PF02828; L27; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR00278; PANCHORMONE.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 2.
DR SMART; SM00309; PAH; 1.
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; 1.
DR PROSITE; PS00265; PANCREATIC_HORMONE_1; 1.
DR PROSITE; PS50276; PANCREATIC_HORMONE_2; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Amidation {ECO:0000256|ARBA:ARBA00022815};
KW Cell junction {ECO:0000256|ARBA:ARBA00022427};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Signal {ECO:0000256|SAM:SignalP};
KW Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..656
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003969561"
FT DOMAIN 164..222
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 244..323
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 329..397
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 454..641
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
SQ SEQUENCE 656 AA; 73186 MW; 2D2A2B2F78AB3EE5 CRC64;
MDATRCCLSL LLLSTCVALL LQPPLGTEGA PLEPVYPGDN ATPEQMAQYA AELRRYINML
TRPRYGKRDK EDMLDFLEWG SPHAAAPRRD IFRALIDFTM PVAATNSETA VCLTAHSFAP
AMQQVLDNLG SLPNATGAAE LDLIFLRGIM ESPIAHERLE ETKLEAVRDN NLELVQEILR
DLAQLAEQSS TAAELARILQ EPHFQSLLET HDSVASKTYE TPPPSPGLDP TFSNQPVPPD
AVRMVGIRKT AGEHLGVTFR VEGGELVIAR ILHGGMVAQQ GLLHVGDIIK EVNGQPVGSD
PRALQELLRS ASGSVILKIL PSYQEPHLPR QVFVKCHFDY DPARDNLIPC KEAGLRFNAG
DLLQIVNQDD ANWWQACHVE GGSAGLIPSQ LLEEKRKAFV KRDLELTPTS GTLCGSLSGK
KKKRMMYLTT KNAEFDRHEL LIYEEVARMP PFRRKTLVLI GAQGVGRRSL KNKLIMWDPD
RYGTTVPYTS RRPKDSEREG QGYSFVSRAE MEADIRAGRY LEHGEYEGNL YGTRIDSIRG
VVAAGKVCVL DVNPQAVKVL RTAEFVPYVV FIEAPDFETL RAMNRAALES GVSTKQLTEA
DLRRTVEESS RIQRGYGHYF DLSLVNSNLE RTFRELQAAM EKLRTEPQWV PVSWVY
//
