ID V8PBU3_OPHHA Unreviewed; 380 AA.
AC V8PBU3;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Src kinase-associated phosphoprotein 1 {ECO:0000256|ARBA:ARBA00039670};
DE Flags: Fragment;
GN Name=Skap1 {ECO:0000313|EMBL:ETE71372.1};
GN ORFNames=L345_02813 {ECO:0000313|EMBL:ETE71372.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE71372.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE71372.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE71372.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SKAP family.
CC {ECO:0000256|ARBA:ARBA00005864}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETE71372.1}.
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DR EMBL; AZIM01000379; ETE71372.1; -; Genomic_DNA.
DR AlphaFoldDB; V8PBU3; -.
DR Proteomes; UP000018936; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd12044; SH3_SKAP1; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035765; SKAP1_SH3.
DR InterPro; IPR037781; SKAP_fam.
DR PANTHER; PTHR15129:SF1; SRC KINASE-ASSOCIATED PHOSPHOPROTEIN 1; 1.
DR PANTHER; PTHR15129; SRC-ASSOCIATED ADAPTOR PROTEIN; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:ETE71372.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000313|EMBL:ETE71372.1}.
FT DOMAIN 316..377
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE71372.1"
SQ SEQUENCE 380 AA; 43318 MW; 1210BF71F34AE105 CRC64;
MAEIPGCSHW GVPTPMVPGF PPPLVPMYQQ ARTGGMVPNP ALALGAQLMP IAMQQWFTQM
IRQGLMGGTQ QAITPTQLGA IPVITHCSKH NTSQTLKQSV VLQPYSLVSS EEYLSDYSIE
EVYSQTELNI SHAWILSPPS EKVHLRNGDK GKPHADNVLI RDRQAGIGHI NVNIHSGRFL
SMSQTCYDSK IFGSEWQKRW CVLDNTAFYY YANEKSKQPK GIFAIESYHA QLAPYLRKDS
RRDCCFELTS PDKRTYEEEE ENENNTNKEE AYDDMESFNT PSVTFNQDST LDLDKEETMV
QGKEGIYEVL PGFIRRYANY YQGLWNCTGG HPDELSFQRG DLIYIISKEY NMYGWWVGEL
NNMVGIVPRN YLMPAYDLEE
//
