ID C3YQW5_BRAFL Unreviewed; 1453 AA.
AC C3YQW5;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=USP domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BRAFLDRAFT_81334 {ECO:0000313|EMBL:EEN57306.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN57306.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN57306.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN57306.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR EMBL; GG666544; EEN57306.1; -; Genomic_DNA.
DR RefSeq; XP_002601294.1; XM_002601248.1.
DR STRING; 7739.C3YQW5; -.
DR eggNOG; KOG1215; Eukaryota.
DR eggNOG; KOG1867; Eukaryota.
DR eggNOG; KOG3509; Eukaryota.
DR InParanoid; C3YQW5; -.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 13.
DR CDD; cd00112; LDLa; 2.
DR CDD; cd02662; Peptidase_C19F; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 2.10.25.10; Laminin; 15.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR10574:SF422; BASEMENT MEMBRANE-SPECIFIC HEPARAN SULFATE PROTEOGLYCAN CORE PROTEIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00053; Laminin_EGF; 14.
DR Pfam; PF00057; Ldl_recept_a; 2.
DR Pfam; PF00443; UCH; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 14.
DR SMART; SM00180; EGF_Lam; 14.
DR SMART; SM01411; Ephrin_rec_like; 6.
DR SMART; SM00192; LDLa; 2.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 14.
DR SUPFAM; SSF57424; LDL receptor-like module; 2.
DR PROSITE; PS01248; EGF_LAM_1; 5.
DR PROSITE; PS50027; EGF_LAM_2; 13.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460}; Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 39..469
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 598..646
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 663..711
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 757..805
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 819..867
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 872..920
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 934..982
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1010..1058
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1062..1110
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1114..1162
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1167..1215
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1225..1273
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1277..1325
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1329..1377
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT REGION 982..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1002
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 524..542
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 536..551
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 560..572
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 567..585
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 579..594
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 616..625
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 681..690
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 775..784
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 837..846
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 890..899
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 952..961
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1028..1037
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1080..1089
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1132..1141
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1185..1194
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1243..1252
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1295..1304
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1347..1356
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1453 AA; 159311 MW; A9A06B505931A3C3 CRC64;
MDPQQWCMLG GSAAAVIAGV YVLWGPENKG RRRKKDLPPG LLNLGNTCFM NVVLQSLAAC
PSFVQWLGDF IDAHISDENY TSYLAYTMVR VMKVLTNQAI VPDPFSPVEV LEALRARRWV
ISSEEQDAHE LFQVLTSTLD EEKTTPPSVV SLFNIGLLQL EEKFCEGGGK RDPAVTRANG
FLPPLSYSGQ DHPFKGLLAS QLRCKQCWHK CPVKYDHFDS LSLSLPADEL GPHTLEGLLQ
QFVMSETVQN VECENCQKAS CPWEEEGASA RTAFIKQLTL GKLPQCMCIH IQRTVWLDNG
TPTKRKDQVL FPEYLDMAAF RYRAGLLGGK AGGVRNGRVP NGILHRGESV PQSPVSSCLS
SPVFPSTPLF SPSRLSCYPS MAMISPFSPA KESVFKSTPF RLVAVIVHLG EVFSGHFVCY
RRAPEGEHGS FSEKWIKTSD MMVRRVLLQE VLGAEVTSAG VSVGISSEKA AQTVRYTHGT
NGSPSPPCRH TSPPMATLLA VIMLFIAAVR SQRPCPDPGR QFQCGDGLCI DRRWVCDRRP
DCKDYADETG CPAQAQPVAC GASQFTCRSG QCVSAAGVCN GRPDCADRSD EVGCGRSTCN
GHSNIRDPAT GYCLNCQHNT QGTQCEFCSP GYYGDARRGT PNDCRPLPGQ TGAVITRRVS
RPCNCHRHAY MCDAQGNCMK CEHNTYGSQC QYCSPGFYGD ARRGTPNDCQ PISDQSGARN
CQHNTRGNNC EHCEDGYAGN AQGGTPYDCQ PVQKIQCYCY RHASSCDANG RCVDCQHNTY
GEHCENCLPG YQGDPKKGTP YDCEVARASD QQQPPSYSCN CHGHARACDS YGRCLDCQHN
TMGYRCETCK PGYTGDATRG SALDCQAQSP PCNCYRHAYN CDQYGTCVNC LHNTDGKNCE
RCKVGYQGDA KRGTPQDCQR VSPPAPPPAR TYQCYCYGHS NQCDQYGRCL NCRHNTYGSR
CENCLPGYQG DAKTGLPNSC TAVSRPAPPP ARAPAPAPPP AQQQPSRRQC YCYGHSNQCD
SNGRCVNCMH NTEGPNCEQC RDGYAGEARR GTPYDCLLVE DCKCYGHSDE CDASGRCLRC
KHNTMGDHCE KCLPGYTGDP RYSTPGDCSA IVPCTCNGHS DACDAEGICL NCKHNTQGDQ
CEVCADGYRG DATRGTPNDC HWAFEPCDCY GHSTECDSRG RCQNCDHNTY GDKCQYCKPG
YVGDGRLGTP DDCQRVTSPI DRVPCFCNRH SDVCDNFGRC LYCQHNTEGD QCERCAMGYF
GDAEEGTAAD CKMLVPCMCH QHANDCDEMG RCIGCLHNTE GDKCERCKDG FMGDATEGTP
DDCRPSIPCK CNGHANDCDS NGKCMNCLHN TRGEFCELCQ IGFYGDPSSG DVDACKECPC
PLTTRENRFA ETCFLDSDNK PTCRNCRRGH QGRDCGKCKP GYMGNPFVMN GGCVRRPSGV
RSQPRRIPVR IIP
//
