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
//