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Database: UniProt
Entry: W5Q8C3_SHEEP
LinkDB: W5Q8C3_SHEEP
Original site: W5Q8C3_SHEEP 
ID   W5Q8C3_SHEEP            Unreviewed;       722 AA.
AC   W5Q8C3;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOARP00000018965.1};
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:ENSOARP00000018965.1, ECO:0000313|Proteomes:UP000002356};
RN   [1] {ECO:0000313|Ensembl:ENSOARP00000018965.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   AlphaFoldDB; W5Q8C3; -.
DR   SMR; W5Q8C3; -.
DR   PaxDb; 9940-ENSOARP00000018965; -.
DR   Ensembl; ENSOART00000019233.1; ENSOARP00000018965.1; ENSOARG00000017674.1.
DR   eggNOG; KOG3607; Eukaryota.
DR   HOGENOM; CLU_012714_4_0_1; -.
DR   OMA; FGHCKRE; -.
DR   Proteomes; UP000002356; Unplaced.
DR   Bgee; ENSOARG00000017674; Expressed in testis and 16 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   PANTHER; PTHR11905:SF140; A DISINTEGRIN AND METALLOPEPTIDASE DOMAIN 6-RELATED; 1.
DR   PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..722
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004870366"
FT   DOMAIN          223..401
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          411..497
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50214"
FT   DOMAIN          637..670
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DISULFID        469..489
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT   DISULFID        660..669
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   722 AA;  80546 MW;  5C6731513702FFF8 CRC64;
     QTSLSSAPML AEGRVTLRAA LWLLGLWAVL APAQCSRDRP SWRYISTEVV IPRKELHQGK
     GAQGLGWLSY SLRFGGQRHV IHMRRKRLFW PGHLMVTQDD QGVLRADHPF VPEDCYYFGY
     LEEVPFSTVT INTCYGGLQG YMKLDDLTYE VSPLKHSPEF EHTVSQMVAD ASAMGLMRRP
     GYEEERGPLL PPANITEAPR LSSKLYTFHE AHMKGALQST NAFYRTTNNV SKTVQSMLEM
     SSIIDAVYRG LETRFYISVI HVYDVRDPVS TGSLRPGSAY FQFYSRTIYS VFRPHTAVIF
     STVEPPDGAY VPNLHTFCHE GNLLPIATSG KNTLTTALYA CFLLGRSIGL YYDSEDCVCQ
     RRTTCIMNGY QSLTDAFSNC SYENLQNDLR NGLNTCMFQT DMAYYNRSLT RDRCGNREVE
     TGEQCDCGSF KECYGNPCCD HLCSFTAAST CDTETCCTNC TFSKPGTLCR PIRSMCDLPE
     YCRGISKTCP RDVFMQQGTP CGEEGYCFNG SCTDRTVHCK EIFGRGALSG PSHCYNVNTK
     GFRYGFCKRI TWSAGFIACT RQDMLCGRLQ CANVSFLPPL QEHVGFHQEH TTLGLCFGLD
     QHRGQGTVDY GHVRDGTLCA PGTYCFDNYC NGSLSRINYT CLPQKCSSRG VCNSEGNCHC
     HLGWAPPLCE TTGDGGSEDS GPPPKVFRSV QHDETILVYV RLVFGRLYAL TAAVLFGVAT
     NV
//
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