ID F1RZL4_PIG Unreviewed; 819 AA.
AC F1RZL4;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=ADAM metallopeptidase domain 9 {ECO:0000313|Ensembl:ENSSSCP00000016755.2};
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 9 {ECO:0000313|EMBL:HDA31627.1, ECO:0000313|EMBL:HDA55231.1};
GN Name=ADAM9 {ECO:0000313|Ensembl:ENSSSCP00000016755.2,
GN ECO:0000313|VGNC:VGNC:95969};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000016755.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000016755.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000016755.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HDA31627.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000016755.2}
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 EMBL; DQIR01076151; HDA31627.1; -; Transcribed_RNA.
DR EMBL; DQIR01076152; HDA31628.1; -; Transcribed_RNA.
DR EMBL; DQIR01099755; HDA55231.1; -; Transcribed_RNA.
DR EMBL; DQIR01199562; HDB55039.1; -; Transcribed_RNA.
DR RefSeq; XP_001925699.2; XM_001925664.4.
DR STRING; 9823.ENSSSCP00000016755; -.
DR MEROPS; M12.209; -.
DR PaxDb; 9823-ENSSSCP00000016755; -.
DR Ensembl; ENSSSCT00000017216.5; ENSSSCP00000016755.2; ENSSSCG00000015808.5.
DR GeneID; 397344; -.
DR KEGG; ssc:397344; -.
DR CTD; 8754; -.
DR VGNC; VGNC:95969; ADAM9.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000156239; -.
DR HOGENOM; CLU_012714_4_1_1; -.
DR OMA; DFTVFTY; -.
DR OrthoDB; 5406290at2759; -.
DR TreeFam; TF314733; -.
DR Proteomes; UP000008227; Chromosome 15.
DR Bgee; ENSSSCG00000015808; Expressed in ovary and 43 other cell types or tissues.
DR Genevisible; F1RZL4; SS.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005518; F:collagen binding; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0043236; F:laminin binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR GO; GO:0033631; P:cell-cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IBA:GO_Central.
DR GO; GO:0031293; P:membrane protein intracellular domain proteolysis; IEA:Ensembl.
DR GO; GO:0042117; P:monocyte activation; IEA:Ensembl.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:0051549; P:positive regulation of keratinocyte migration; IEA:Ensembl.
DR GO; GO:0034241; P:positive regulation of macrophage fusion; IEA:Ensembl.
DR GO; GO:0050714; P:positive regulation of protein secretion; IEA:Ensembl.
DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0010042; P:response to manganese ion; IEA:Ensembl.
DR GO; GO:0034612; P:response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
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; IPR018358; Disintegrin_CS.
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:SF136; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 9; 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; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 1: Evidence at protein level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Integrin {ECO:0000313|EMBL:HDA31627.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1RZL4};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..819
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014571258"
FT TRANSMEM 699..718
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 212..406
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 414..501
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 640..674
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 730..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..819
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 348
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 365..370
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 473..493
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 664..673
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 819 AA; 90512 MW; 251A0B4A26EAFB47 CRC64;
MGLGAGSLSG SLGFQWLLFL GLVSPALGAA RSGFQQTSHL SSYEIITPWR LTRERREAPR
PSSEQVSYVI QAEGKEHIIH LERNKDLLPK DFVVYTYNNE GALISDYPDI QNHCHYRGYV
EGIYNSSIAL SDCFGLRGLL HIENVSYGIE PLQNSSHFEH VFYRMDDVHR EPVKCGVSNK
DIEEEIVKDE EEEPPSVTQL LRRRRAVLPQ TRYVELFIVV DKERYDMMGR NQTAVREEMI
RLANYLDSMY IMLNIRIVLV GLEIWTNGNL INIIGGAGDV LGNFVQWREK FLITRRRHDS
AQLVLKKGFG GTAGMAFVGT VCSRSHAGGI NVFGQITVET FASIVAHELG HNLGMNHDDG
RDCYCGAKSC IMNSGASGSR NFSTCSAEDF EKLTLNKGGN CLLNIPKPDE AYSAPFCGNK
LVDPGEECDC GTPKECELDP CCEGSTCKLK SSAECAYGDC CQDCWFLPGG TLCRGKTNEC
DVPEYCNGSS QFCQPDVFIQ NGYPCQNNKA YCYNGMCQYY DAQCQVIFGS KAKAAPRDCF
IDVNSKGDRF GNCGFSGNEY KKCATGNALC GKLQCENVQE MPVFGIVPAI IQTPGRGTKC
WGVDFQLGSD VPDPGMVNEG TRCDVGKICR NFQCVNASVL NYDCDIQKKC HGHGVCNSNK
NCHCDNGWAP PYCDTTGYGG SVDSGPTYNE KNTALRDGLL VFFFVIVPLT VLAAFIFIKR
DQLRRSYFRK KRSQTNESHG KNQAKAPRQP ASVPGHASSV TPPREVPIYA NRFPVPTYAA
KQPQQFPSRP PPPQPKVSSQ GNLIPARPAP PPPLYSSLT
//
