ID A0A1S3IWD8_LINUN Unreviewed; 1170 AA.
AC A0A1S3IWD8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 12 isoform X2 {ECO:0000313|RefSeq:XP_013402378.1};
GN Name=LOC106168005 {ECO:0000313|RefSeq:XP_013402378.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013402378.1};
RN [1] {ECO:0000313|RefSeq:XP_013402378.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26383154;
RA Luo Y.J., Takeuchi T., Koyanagi R., Yamada L., Kanda M., Khalturina M.,
RA Fujie M., Yamasaki S.I., Endo K., Satoh N.;
RT "The Lingula genome provides insights into brachiopod evolution and the
RT origin of phosphate biomineralization.";
RL Nat. Commun. 6:8301-8301(2015).
RN [2] {ECO:0000313|RefSeq:XP_013402378.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR RefSeq; XP_013402378.1; XM_013546924.1.
DR AlphaFoldDB; A0A1S3IWD8; -.
DR EnsemblMetazoa; XM_013546924.1; XP_013402378.1; LOC106168005.
DR GeneID; 106168005; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
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:SF250; ADAM METALLOPROTEASE; 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 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.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1170
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010182607"
FT TRANSMEM 743..766
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 222..419
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 425..513
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 704..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..837
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..947
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..992
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1034
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 359
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 368
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 374..398
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 376..381
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 485..505
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 1170 AA; 129037 MW; 9E408DF4A680CE7C CRC64;
MGWGWKWMCC VAVLKLLYHR SHCDVSEGNV RNGRQKATEE FSYFEKVVPV IRTRRSARDA
VTWAENQHLD EVEVVVEAFN KTFTLDLKLN KNLFGDKFVE KHTTNGKPVV RRYKDHKNHH
CFYHGKIRHE EESLIALSTC DGLSGLFQDG TEQYYIQPVA GSTGFHHHVF RASDRHEQHL
RCGTGDHAHD FPSFYHSSLN SKHLHRLRRA IRGPYNSGKK TRYVELFLVS DHRQFDMHGK
NVAKVIQRSK EIGNIVSALY NELDIYVALV GVEVWDSGDK IIVDQDADVT LNNFLSYRKT
FLNPHFPNDN GQLITGGVFA NRILGKASQT PMCSFRYSGG VVRDHSELPG PVGTTVAHEM
GHNFGMTHDN LSVCKCPEQR CIMAATTGSG NPTKWSSCSK KELQEAFDIG MDYCLRNKPT
RLFGSPTCGN GFVEDGEQCD CGLPEECKNK CCNASSCTLM TNATCATGTC CNLQTCQMKP
MATECRPVAG ECDLPEFCSG NSEDCPADVF VQNGRSCKSG QSYCYQGKCT THDAQCKLLW
GSTGQVSPPV CYTRLNTRGS EFGNCGYSWI HDNYTACKQE DTMCGMLHCQ HQNEKLMFWR
EALSRLLPYT TLDVNGVRIK CKSAILDVGL NDLDPGMTPD GAKCGEDKLC VNQTCMSFDQ
LGVAPCPEDC NQNGICNSNN NCHCEVGLAP PLCNTPGYGG SVDSGPASSN KDSIVTSTVA
QSTESSDTAI RPTEIPPQGD NSLMIGLLIF FLLIVPLLVI GGFFAYRYRE QLKVWWGQKA
SAAYKYKDAA PPKSSRRSES SVKSPSKPRP PPSIAAVEAQ SVQERPPPPP APVPKDPVNR
QPSTGSAKMP ISNPVLQSTT NRTPSFKDAK FIEKPRVIVR PTVYANLPDS ENSDEDSGYV
TGGKPARPPK PWSENSDQSS ANQNQPPPRP SVPPVKFQPP PNRPSQLTRP NQLPTKPLKP
PTRQQQPLKP PSLPQAQSKP VPLRPAPPAP LSPIADTDAS ESPSEPQVGI VSAMKQKFKF
DNSNNNNSNT DLDSDPLYEP PPKPWTDQST GENIYEVIPG DEEAPLNGRS KAPEKPSRSV
KPMFQPRARP ASVQFRSQPQ TLTEFKPRPV SAREPEVSRG VSVKDRIAKL SQENSEGSGP
AKPVQRSKSG VAKPSIPPKP RKRPDSVAQC
//
