CSKI2_XENLA
ID CSKI2_XENLA Reviewed; 1205 AA.
AC Q6DD51;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Caskin-2;
GN Name=caskin2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; BC077777; AAH77777.1; -; mRNA.
DR RefSeq; NP_001086927.1; NM_001093458.1.
DR AlphaFoldDB; Q6DD51; -.
DR SMR; Q6DD51; -.
DR GeneID; 446762; -.
DR KEGG; xla:446762; -.
DR CTD; 446762; -.
DR Xenbase; XB-GENE-17346434; caskin2.S.
DR OrthoDB; 75723at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 446762; Expressed in lung and 18 other tissues.
DR CDD; cd09497; SAM_caskin1_2_repeat1; 1.
DR CDD; cd09498; SAM_caskin1_2_repeat2; 1.
DR CDD; cd12063; SH3_Caskin2; 1.
DR Gene3D; 1.10.150.50; -; 2.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR027013; Caskin-1/2.
DR InterPro; IPR035497; Caskin1/2_SAM_1.
DR InterPro; IPR035498; Caskin1/2_SAM_2.
DR InterPro; IPR035499; Caskin2_SH3.
DR InterPro; IPR032117; Caskin_C.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR24174:SF7; PTHR24174:SF7; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF16632; Caskin-tail; 1.
DR Pfam; PF00536; SAM_1; 2.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00454; SAM; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF47769; SSF47769; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50105; SAM_DOMAIN; 2.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW ANK repeat; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..1205
FT /note="Caskin-2"
FT /id="PRO_0000066985"
FT REPEAT 48..77
FT /note="ANK 1"
FT REPEAT 81..110
FT /note="ANK 2"
FT REPEAT 114..143
FT /note="ANK 3"
FT REPEAT 147..176
FT /note="ANK 4"
FT REPEAT 188..217
FT /note="ANK 5"
FT REPEAT 220..249
FT /note="ANK 6"
FT DOMAIN 281..347
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 468..531
FT /note="SAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 537..601
FT /note="SAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 377..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..910
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1205 AA; 130919 MW; 324995AB0385DA6F CRC64;
MGRENELIQA VKSGDVGAVQ KFLAKFRTPK SKLLGSTKRL NVNHQDADGF SALHHAALSG
NSELLLLLLE MQASVDIKDG NGMRPLHYAA WQGQPEPVRL LLRASASVNA ASHDGQIPLH
LAAQYGHYEV SETLLQHQSN PCHVNKGKKT PLDLACEFGR VKVVQLLLNS HLCVSLLEGT
SKDPTDPNFT TPLHLAAKNG HLEVIRLLLK LGIEINKVTK MGTALHEAAL CGKTEVVKLL
IENGVDVNIR NTYNQTALDI VNQFTTTHAS IDIKQLLREA SGILKVRALK DFWNAHDPTA
LNIRAGDLIT VLEQHPDGRW KGHIHDPQKG TDRVGFFPPS IVEVISKRLG STLSRNITVP
SHQHLAKTVL TLPIQHSPGS QLGINPDTSV AGDRHSVGSE SSVRSAGSGQ SCEGQQINTA
LLIENAQTMD FGSENLQNCQ TFPGPVSGHH LSTILPVEKN PGDYLQGKDA EQIFCWLRGF
QMETYVGNFI SAGYDLPTIM RVTPEDLTAI GVTKPGHRKM ISTEIGKLIV ADGLPQQIPV
DLWDWLSQLG LPEYHKQLSE NGYESLSTVT ELTWEGLQEI GIHRLGHQKK LLLGVKRLLD
LQKGYPIGGT LRRRILGSQD TVAVVEPPEN GDLPVTPKLL TFQGAELSQE LQSALTRGNE
QLCTGRRSFS QESISSRSQG SGHSQESASS YPVLPVHLQG VDLNLPERNH PEGTDQILQN
HWVPNGCLIQ PEPPAPPPKP ALKKRSLSAC RYALSDGEPE EEEEKKIATA GTGTLSTYAT
LTRRPGRSCL TNGKPEKKVQ RSQSFAVRAR RKGPPPPPPK RLSSMSSAEG QSPEGQSSVK
TIAAQLKDIG RGTGFSASTS KATDTEVLEG SGTRRRTVSE SAAGLGGRLS LPLTTKKDEE
EERKEEPISS QHSSSESIPF AEEGNLTIKQ RPKPPGAKLE QDATSELSPT QESQLQSAEA
QRHLESSAVL AKPVTVVLAQ ARPQIAAKPQ IGPKPDTGAR APPATSIPKN EEHDFNLTES
DTVKRRPKVK EKEEESPKAP LANNSPSLIP SQEPLTQDTL IAKIADIDKR LLSLGEVEDS
VKKTGIDTRS TGVSISQTHL VISGPQQVLQ KPSRAVTGPL FPAGSILWDE ESEASSREQT
CIPQQSISNS DKGPPVFTSS LQNTEELQDT RGKSCRETVQ LTKNILDDIS TMFDDLAEQL
EAMLD
