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Database: UniProt
Entry: A0A452GL49_9SAUR
LinkDB: A0A452GL49_9SAUR
Original site: A0A452GL49_9SAUR 
ID   A0A452GL49_9SAUR        Unreviewed;       721 AA.
AC   A0A452GL49;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000002514.1};
OS   Gopherus agassizii (Agassiz's desert tortoise).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Testudinidae; Gopherus.
OX   NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000002514.1, ECO:0000313|Proteomes:UP000291020};
RN   [1] {ECO:0000313|Proteomes:UP000291020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28562605;
RA   Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA   Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT   "The Agassiz's desert tortoise genome provides a resource for the
RT   conservation of a threatened species.";
RL   PLoS ONE 12:e0177708-e0177708(2017).
RN   [2] {ECO:0000313|Ensembl:ENSGAGP00000002514.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; A0A452GL49; -.
DR   Ensembl; ENSGAGT00000002875.1; ENSGAGP00000002514.1; ENSGAGG00000000634.1.
DR   Proteomes; UP000291020; Unassembled WGS sequence.
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   Gene3D; 2.10.25.10; Laminin; 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   InterPro; IPR034027; Reprolysin_adamalysin.
DR   PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR   PANTHER; PTHR11905:SF114; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 11; 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; PS00022; EGF_1; 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, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        682..705
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          186..385
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          391..478
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50214"
FT   DOMAIN          620..657
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        450..470
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT   DISULFID        647..656
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   721 AA;  78643 MW;  3440AFAEAD860D0B CRC64;
     PAPSITLIGR SPPEAGRWGS SQPEGGPWLV ASEITHPSRL VGQSTGGEVQ KHQLDTRVRN
     APRGGGSPFV HLAQVSFLIH AFGSAFTLDL ELNHHLLSSS YVERHYGQDG NSSHSTGAGE
     HCYYQVPPWA WGAGPLPHLI QRMPAPRPAQ GCTEPGEWRM QAPLPMTQWP LSCVRRAQHT
     VHSETKYIEL VVVNDHHLFE QMRRSGILTS NFAKSVVNLA DMLYKEQLNT RIVLVAMETW
     ASEDKIHVGE DSLQTLSEFM RYRTEALPEQ SDAAHLFSGR TFQSSRSGSA YVGGICSLTR
     GGGVNEYGNV GAMAVTLAQT LGQNVGMMWN KQRRAAGDCR CPDSWLGCIM EDTGYYLPRK
     FSRCSIEEYS QFLQEGGGSC LFNKPLKLLD PPECGNGFVQ AGEECDCGSL VECAKGGGNC
     CKKCTLTHDA MCSDGLCCKG CKYERRGTPC REAVNECDIP ESCTGDSSQC PPNLHKLDGY
     FCDHEQGRCY GGRCKTRDRQ CNALWGRAAA DRFCYEKLNV EGTERGSCGR KGLAWVQCSK
     QDVLCGYLLC TNITGVPRLG ELSGEITTMT FYHQNRYVDC RGGHVELVDG SDLSYVEDGT
     PCGPGMLCLD HKCLPAAAFN FSACPSSWDG MICFDHGVCS NEGKCICHAD WTGKDCSVYD
     RIPEPKPTGE TERYKGPSGT NIIIGSIAGA VLVAAIVLGG TGWGFKNIRR GRYDPAQPGL
     G
//
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