ID G1SP03_RABIT Unreviewed; 557 AA.
AC G1SP03;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 5-like {ECO:0008006|Google:ProtNLM};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000004748.4, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000004748.4, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000004748.4}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000004748.4};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBUNIT: Interacts with TEX101. {ECO:0000256|ARBA:ARBA00038664}.
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; G1SP03; -.
DR SMR; G1SP03; -.
DR PaxDb; 9986-ENSOCUP00000004748; -.
DR Ensembl; ENSOCUT00000005474.4; ENSOCUP00000004748.4; ENSOCUG00000005475.4.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000162784; -.
DR HOGENOM; CLU_012714_4_3_1; -.
DR InParanoid; G1SP03; -.
DR TreeFam; TF314733; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000005475; Expressed in testis and 8 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 CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF28; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 5; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF01421; Reprolysin; 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; PS00427; DISINTEGRIN_1; 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};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 508..525
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 120..304
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 316..405
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 438..472
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 260..265
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 462..471
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 557 AA; 62884 MW; 3047225114A4E27B CRC64;
MNNNFSISFL SSMSIVYYYD KNDTQHHTPL KSQMDCNYNG YVSGFPNSLV TLNTCSGLRG
TVQFKNISYG IEPMEAVSGF AHMIYEEKTD PSVIHLVEND THGWLYASWN EVRKYPEVSF
NYIGSDTKTV TQRIIQIIGL ANTMLTPLKL TLVITAIEIW SNKNRIPTTE EPYLTLYRFL
EWKRKHLEFR SHDFAFLFSF KKQPMLLGAS LPEKICNKDF AAGVAVYPEG FSLESYTVII
VQLLGLSLGL NYDSVDSCYC SGDVCTMMPT AIFSKGIKDF STCSLDDFKY ISSQSGLHCL
QSDPFEMPVY KQDRPRKICG NSIMELDEQC DCGNIKNCTH KKCCDPTTCT LKSGKQCGSG
DCCTKDCKVK PMGVKCRDPV DKQCDFPEFC NGRLPNCMPD TYVRNGEYCD GGDSFCHDGL
CKSTTRQFSC RLAEFRKNRT LCDTSSHCNG HGICNNFEHC HCEKGYTPPH CKPKTGEFGS
TDDGHFNKDG RSYVVGKHAT FEKKHLHLIL YITLPVLIII GAVLMKQDKI RELCYRGETE
SDRQVESERN SVASGIN
//
