ID V9KV54_CALMI Unreviewed; 474 AA.
AC V9KV54;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Growth arrest-specific 7 {ECO:0000313|EMBL:AFP02889.1};
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFP02889.1};
RN [1] {ECO:0000313|EMBL:AFP02889.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Intestine {ECO:0000313|EMBL:AFP02889.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
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DR EMBL; JW870371; AFP02889.1; -; mRNA.
DR RefSeq; XP_007887041.1; XM_007888850.1.
DR AlphaFoldDB; V9KV54; -.
DR GeneID; 103175691; -.
DR KEGG; cmk:103175691; -.
DR CTD; 100333627; -.
DR OrthoDB; 5491246at2759; -.
DR CDD; cd07649; F-BAR_GAS7; 1.
DR CDD; cd11829; SH3_GAS7; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR037957; GAS7_F-BAR.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR23065:SF57; GROWTH ARREST-SPECIFIC PROTEIN 7; 1.
DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF00397; WW; 1.
DR Pfam; PF16623; WW_FCH_linker; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..61
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 76..109
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 196..454
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT REGION 104..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 54472 MW; 7B95F8FE88191EE6 CRC64;
MAGVWCRTLY AFTGEQHQQG LRFGAGEILR VTQVLDGGWW EGEKNGIRGW FPASYVEILE
KPGSISPQTI EEMANIPLPQ GWQCYMSPQG RKYYVNTYTN ETTWERPASA PGTPKTPISQ
MNSLPTVNGF HSSSNLSHQS DTSHVALRKT SSDPQSPGPG SPTRRQSKES SITINCVTFP
NADTMSEQQL LKPGDWSYCD YFWADRKDSQ SNSTIAGFDI ILVKQLKGKQ MQKEIAEFIR
ERIKIEEDYA KNLAKLSQSP LAAMEEGTLG ESWVQVKKSL SDEAEVHLKF SSKLQSEVEK
PLLSFRENFK KDMKKFDHHI SDLRKQLVSR YTAVEKARKA LAERQKDLEF KTQQLENKSS
NKTEEDIKKA RRKSTQAGDD LMRCVDLYNQ TQSKWFEEMV TTTLELERLE VERIEMIRQH
LCQYTQLRHE TDMFNQSTIE PVDQLLQKVD PSKDRELWVK ENKTGHIRPA DMEL
//
