ID W5PKA9_SHEEP Unreviewed; 2066 AA.
AC W5PKA9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=F5/8 type C domain-containing protein {ECO:0000259|PROSITE:PS50022};
GN Name=F5 {ECO:0000313|Ensembl:ENSOARP00000010880.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000010880.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000010880.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000010880.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000010880.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; AMGL01021362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01021363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01021364; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01021365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01021366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01021367; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9940.ENSOARP00000010880; -.
DR PaxDb; 9940-ENSOARP00000010880; -.
DR Ensembl; ENSOART00000011038.1; ENSOARP00000010880.1; ENSOARG00000010135.1.
DR eggNOG; ENOG502QSUG; Eukaryota.
DR HOGENOM; CLU_000948_0_0_1; -.
DR Proteomes; UP000002356; Chromosome 12.
DR Bgee; ENSOARG00000010135; Expressed in uterus and 54 other cell types or tissues.
DR ExpressionAtlas; W5PKA9; baseline.
DR GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR CDD; cd04226; CuRO_1_FV_like; 1.
DR CDD; cd14453; CuRO_2_FV_like; 1.
DR CDD; cd14450; CuRO_3_FV_like; 1.
DR CDD; cd14454; CuRO_4_FV_like; 1.
DR CDD; cd14451; CuRO_5_FV_like; 1.
DR CDD; cd14455; CuRO_6_FV_like; 1.
DR CDD; cd00057; FA58C; 2.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 5.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR024715; Factor_5/8-like.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR PANTHER; PTHR46806:SF9; COAGULATION FACTOR V; 1.
DR PANTHER; PTHR46806; F5/8 TYPE C DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07732; Cu-oxidase_3; 2.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR PIRSF; PIRSF000354; Factors_V_VIII; 2.
DR SMART; SM00231; FA58C; 2.
DR SUPFAM; SSF49503; Cupredoxins; 6.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR PROSITE; PS01285; FA58C_1; 2.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 2.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000354-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW Signal {ECO:0000256|SAM:SignalP};
KW Sulfation {ECO:0000256|ARBA:ARBA00022641}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..2066
FT /note="F5/8 type C domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004869487"
FT DOMAIN 1694..1848
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1853..1986
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 703..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1175..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..980
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1023
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 167..193
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 248..329
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 499..525
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 602..683
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 1512..1538
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 1694..1848
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
SQ SEQUENCE 2066 AA; 234155 MW; 10CBC4D3D079B091 CRC64;
MFLACPGFWV LVVLGTSWAG WGNLGAEAAR LRQFYVAAQS IRWNYRPEST HLSSKPFETS
FKKIVYREYE AYFQKEKPQS RTSGLLGPTL YAEVGDIMKV HFKNKAHKPL SIHPQGIKYS
KFSEGASYSD HTLPMEKMDD AVAPGQEYTY EWSISEDSGP THDDPPCLTH IYYSYVNLVE
DFNSGLIGPL LICKKGALTE DGIQKMFDKQ HVLMFAVFDE SKSWNQTSSL MYTVNGYVNG
TIPDITVCAH DHISWHLIGM SSGPELFSIH FNGQVLEQNR RKISAITLVS ATSTTANMTV
SPEGRWTIAS LIPKHFQAGM QAYIDIKNCA KKTRNPRKLT RDQRRHIKRW EYFIAAEEVI
WDYAPIIPAS MDKKYRSLHL DNFSNRIGKH YKKVVYKQYQ DDSFTKRLED PSSEGDGILG
PIIRAQVRDT LKIVFKNMAS RAYSIYPHGV TFSPYDDEVN ASSTSGSNTM IRAVQPGETY
TYKWNILESD EPTENDAQCL TRPYYSNVDV TRDLASGLIG LLLICKSRSL DKRGIQRAAD
IEQQAVFAVF DENKSWYIED NIYKFCENPE KVKRDDPKFY ESNIMSTING YVPESIPTLG
FCFDDTVQWH FCSVGTQNDL LTIHFTGHSF IYGKRHEDTL TLFPMQGESV TVTMDNVGTW
MLTTMNSNPR SKKLRLRFRD AKCIRNDDDD SYEIIYEPSG STAMTTRKMH DSSEIKDEND
ADSDYQEELA SILGLRSFRN SSLNQEKDEL NLTALALEKD SEFIPPSTNR DLGSNSSSPR
NVSRLIANNF AEPLKTLLHL EAPAAGPALE HAGLDKNSTL NPPMAEHSSP YSEDHREDLP
LSDVTGISLL PFGTGFKNQK PAKHQRFQVG RGRAAKHRFS QTESPAHKTR THLSQDNSSS
SRMGLWEDIP SDLLLLQQKD PSKILNGEWY LVSEKGSYEI IQDANENKTV NKLPNSPQNA
SRTWGENIPF KNSHGKQSGH PTFLVTRRKP LQDRQDRRNS RLKEGLPLIR TRRKKKEEKP
AYHVPLSPRS FQPLRGEVNA SFSDRRHNHS LLLHASNETY LSIDLNQTFP SMNLSLAASL
PDHDQTSPND TSQTSSPPDL NLTVSPEEHY QTFPIQDSDP THSTTAHSNR SPPTQPSQIP
NYDLRNQAIP TDVSQIFPSL EPEVWQTATS LDLSQPSISP DLGQMAPTPD LSQESLSPDL
GQTDLSPDLS QESLSPDLGR TALSPDLSQE SLSPDLGQLD LKQTSPPLDL DQTSHTSESS
QSLSLPEFGQ TFPYADIGQM PSPPPDSTLN NTFIPEEFNP LVVVGLSRDD GDYIEIIPGQ
KEESSEEDYG EFEFVAYNDP YQTDLRTDIS SSRNPDNIAA WYLRSNNGNR KNYYIAAEEI
SWDYSKFVQS EDTDDVPEHT VFKKVVFRKY LDSTFTKLDP QGEYEEHLGI LGPVIRAEVD
DVIQVRFKNL ASRPYSLHAH GLSYEKSSEG KTYEDDSPEW FKEDNAIQPN STYTYVWHAT
TRSGPENPGS ACRAWAYYSA VNPEKDIHSG LIGPLLICRK GTLHKETNMP VDMREFVLLF
MVFDEKKSWY YDKKPTRSWR HTSSEVKNSH EFHAINGMIY NLPGLRMYEQ EWVRLHLLNL
GGSRDIHVVH FHGQTLLENG TQQHQLGVWP LMPGSFKTLE MKASKPGWWL LDTEVGEIQR
AGMQTPFLIV DRECKMPMGL STGLIADSQI QASEFWGYWE PKLARLNNGG SYNAWIAEKL
STEFNPQPWI QVDMQKEVLL TGIQTQGAKH YLKPYYTTEF CVAYSSDQKN WRIFKGNSTK
NVMYFGGNSD ASTIKENQID PPVVARYIRI SPTRSYNKPA LRLELQGCEV NGCSTPLGME
SGKIENKQIT ASSFKKSWWG NYWGPFLARL NAQGRVNAWQ AKANNNNQWL QIDLLKIKKI
TAIVTQGCKS LSSEMYVKSY TIHYSDQGMD WKPYREKSSM VDKIFEGNNN VRGHVKNFFS
PPIISRSSMK YIQYGLTRTW CCCFLCSLPQ TTSAISLSFC SRDSALLLRG SCCSMPRDCW
PFSSWNSSMA SPLPLKLPTT PTSTVW
//
