ID A0A1S3FZI4_DIPOR Unreviewed; 633 AA.
AC A0A1S3FZI4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=SH3 domain-containing kinase-binding protein 1 isoform X3 {ECO:0000313|RefSeq:XP_012881968.1};
GN Name=Sh3kbp1 {ECO:0000313|RefSeq:XP_012881968.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012881968.1};
RN [1] {ECO:0000313|RefSeq:XP_012881968.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012881968.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_012881968.1; XM_013026514.1.
DR AlphaFoldDB; A0A1S3FZI4; -.
DR GeneID; 105993305; -.
DR CTD; 30011; -.
DR OrthoDB; 2972088at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd12052; SH3_CIN85_1; 1.
DR CDD; cd12055; SH3_CIN85_2; 1.
DR CDD; cd12057; SH3_CIN85_3; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 3.
DR InterPro; IPR035770; CIN85_SH3_1.
DR InterPro; IPR035771; CIN85_SH3_2.
DR InterPro; IPR035772; CIN85_SH3_3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14167; SH3 DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR14167:SF6; SH3 DOMAIN-CONTAINING KINASE-BINDING PROTEIN 1; 1.
DR Pfam; PF14604; SH3_9; 3.
DR PRINTS; PR00499; P67PHOX.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 3.
DR SUPFAM; SSF50044; SH3-domain; 3.
DR PROSITE; PS50002; SH3; 3.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000313|RefSeq:XP_012881968.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000313|RefSeq:XP_012881968.1}.
FT DOMAIN 11..70
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 110..169
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 279..340
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 171..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 577..629
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 174..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 633 AA; 69824 MW; BC63F1671EBB6049 CRC64;
MVELRGTPRS QEGVEAIVEF DYQAQHDDEL TISVGEVITN IRKEDGGWWE GQINGRRGLF
PDNFVREIKK DVKKDLLTSK APEKPMHDVS SGNPLLSSET VLRTNKRGER RRRRCQVAFS
YLPQNDDELE LKVGDIIEVV GEVEEGWWEG VLNGKTGMFP SNFIKELSGE SDELGISQDE
QLSKSSLRET TGSESDGGDS SSTKSEGANG SMATAAIQPK KVKGVGFGDI FKDKPIKLRP
RSIEVENDFL PMEKTIGKKL PPPVATLDPS KTEMDSKTKT KDYCKVIFPY EAQNDDELTI
KEGDILTLIN KDCIDAGWWE GELNGRRGVF PDNFVKLLPP DFDKEGSRPK KPPPPSAPIM
KQGAGTTERK HEMKKIPPER PETLPNRTEE KERPEREPKL DLQKPSVPAI PPKKPRPPKS
NSLSRPSALP PKRPERPVGP LTHTRGDGPK IDLVGSSLSG ILDKDLSDRG NDIDLEGFDS
VVSSTEKLSH PTTSRPKATG RRPPSQSLTS VSDNKASLPP KPGSMAAGSG PASLTSLASV
PLSSSLGAPG HRANSPSLFS MEGKPKMEPI ASGQAAVEEL RTQVRELRSI IETMKDQQKR
EIKQLLSELD EEKKIRLRLQ MEVNEIKKAL QSK
//