Annotations: 1ORV

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1orva1	All beta proteins	8-bladed beta-propeller	DPP6 N-terminal domain-like	DPP6 N-terminal domain-like	Dipeptidyl peptidase IV/CD26, N-terminal domain	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
A	d1orva2	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	DPP6 catalytic domain-like	Dipeptidyl peptidase IV/CD26, C-terminal domain	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
B	d1orvb1	All beta proteins	8-bladed beta-propeller	DPP6 N-terminal domain-like	DPP6 N-terminal domain-like	Dipeptidyl peptidase IV/CD26, N-terminal domain	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
B	d1orvb2	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	DPP6 catalytic domain-like	Dipeptidyl peptidase IV/CD26, C-terminal domain	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
C	d1orvc1	All beta proteins	8-bladed beta-propeller	DPP6 N-terminal domain-like	DPP6 N-terminal domain-like	Dipeptidyl peptidase IV/CD26, N-terminal domain	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
C	d1orvc2	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	DPP6 catalytic domain-like	Dipeptidyl peptidase IV/CD26, C-terminal domain	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
D	d1orvd1	All beta proteins	8-bladed beta-propeller	DPP6 N-terminal domain-like	DPP6 N-terminal domain-like	Dipeptidyl peptidase IV/CD26, N-terminal domain	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
D	d1orvd2	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	DPP6 catalytic domain-like	Dipeptidyl peptidase IV/CD26, C-terminal domain	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF00930,PF18811	e1orvA1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 8-bladed	F: PF00930,PF18811	ECOD (1.6)
A	PF00326	e1orvA2	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: PF00326	ECOD (1.6)
B	PF00930,PF18811	e1orvB1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 8-bladed	F: PF00930,PF18811	ECOD (1.6)
B	PF00326	e1orvB2	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: PF00326	ECOD (1.6)
C	PF00930,PF18811	e1orvC1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 8-bladed	F: PF00930,PF18811	ECOD (1.6)
C	PF00326	e1orvC2	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: PF00326	ECOD (1.6)
D	PF00930,PF18811	e1orvD1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 8-bladed	F: PF00930,PF18811	ECOD (1.6)
D	PF00326	e1orvD2	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: PF00326	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.140.10.30	Mainly Beta	8 Propeller	Methanol Dehydrogenase	Chain A	CATH (4.3.0)
A	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
B	2.140.10.30	Mainly Beta	8 Propeller	Methanol Dehydrogenase	Chain A	CATH (4.3.0)
B	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
C	2.140.10.30	Mainly Beta	8 Propeller	Methanol Dehydrogenase	Chain A	CATH (4.3.0)
C	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
D	2.140.10.30	Mainly Beta	8 Propeller	Methanol Dehydrogenase	Chain A	CATH (4.3.0)
D	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00930	Dipeptidyl peptidase IV (DPP IV) N-terminal region (DPPIV_N)	Dipeptidyl peptidase IV (DPP IV) N-terminal region	-	Repeat
A, B, C, D	PF00326	Prolyl oligopeptidase family (Peptidase_S9)	Prolyl oligopeptidase family	-	Domain
A, B, C, D	PF18811	Dipeptidyl peptidase IV (DPP IV) low complexity region (DPPIV_rep)	Dipeptidyl peptidase IV (DPP IV) low complexity region	-	Repeat

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	dipeptidyl peptidase IV	protein binding binding virus receptor activity exogenous protein binding peptidase activity catalytic activity, acting on a protein dipeptidyl-peptidase activity hydrolase activity exopeptidase activity catalytic activity signaling receptor binding enzyme binding protease binding serine hydrolase activity protein binding binding virus receptor activity exogenous protein binding peptidase activity catalytic activity, acting on a protein dipeptidyl-peptidase activity hydrolase activity exopeptidase activity catalytic activity signaling receptor binding enzyme binding protease binding serine hydrolase activity serine-type peptidase activity serine-type endopeptidase activity endopeptidase activity identical protein binding protein homodimerization activity protein dimerization activity molecular function activator activity molecular function regulator activity signaling receptor regulator activity chemorepellent activity receptor ligand activity signaling receptor activator activity aminopeptidase activity	epithelium migration multicellular organismal process tissue migration endothelial cell migration ameboidal-type cell migration epithelial cell migration cell migration cellular process cell motility cellular response to stimulus negative regulation of locomotion regulation of cell motility regulation of cellular process response to stimulus epithelium migration multicellular organismal process tissue migration endothelial cell migration ameboidal-type cell migration epithelial cell migration cell migration cellular process cell motility cellular response to stimulus negative regulation of locomotion regulation of cell motility regulation of cellular process response to stimulus negative regulation of biological process negative regulation of chemotaxis taxis regulation of immune system process negative regulation of cell migration chemotaxis regulation of biological process regulation of leukocyte chemotaxis regulation of leukocyte migration response to external stimulus neutrophil migration granulocyte migration leukocyte migration negative regulation of leukocyte migration regulation of response to stimulus regulation of locomotion response to chemical negative regulation of response to external stimulus regulation of neutrophil chemotaxis negative regulation of cell motility regulation of neutrophil migration negative regulation of neutrophil chemotaxis negative regulation of leukocyte chemotaxis regulation of response to external stimulus neutrophil chemotaxis regulation of granulocyte chemotaxis negative regulation of cellular process regulation of cell migration myeloid leukocyte migration locomotion cell chemotaxis negative regulation of response to stimulus negative regulation of granulocyte chemotaxis biological regulation regulation of chemotaxis cellular response to chemical stimulus negative regulation of immune system process immune system process granulocyte chemotaxis negative regulation of neutrophil migration leukocyte chemotaxis behavior locomotory behavior exploration behavior locomotory exploration behavior cell population proliferation positive regulation of cell population proliferation regulation of cell population proliferation positive regulation of biological process positive regulation of cellular process T cell activation cell activation lymphocyte activation leukocyte activation cell adhesion response to decreased oxygen levels response to hypoxia response to stress response to oxygen levels response to abiotic stimulus psychomotor behavior motor behavior cell-cell adhesion mediated by integrin regulation of cell adhesion mediated by integrin regulation of cell adhesion regulation of cell-cell adhesion mediated by integrin cell-cell adhesion cell adhesion mediated by integrin regulation of cell-cell adhesion behavioral defense response fear response behavioral fear response defense response multicellular organismal response to stress cellular component disassembly negative regulation of extracellular matrix organization extracellular matrix disassembly regulation of cellular component organization negative regulation of cellular component organization extracellular matrix organization cellular component organization negative regulation of extracellular matrix disassembly cellular component organization or biogenesis regulation of extracellular matrix organization regulation of extracellular matrix disassembly extracellular structure organization external encapsulating structure organization regulation of leukocyte activation regulation of cell activation positive regulation of leukocyte cell-cell adhesion leukocyte cell-cell adhesion positive regulation of cell-cell adhesion positive regulation of lymphocyte activation positive regulation of cell activation positive regulation of leukocyte activation regulation of multicellular organismal process positive regulation of immune system process positive regulation of T cell activation positive regulation of cell adhesion regulation of T cell activation lymphocyte costimulation regulation of leukocyte cell-cell adhesion positive regulation of multicellular organismal process T cell costimulation regulation of lymphocyte activation organic substance metabolic process organonitrogen compound metabolic process proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	cell-cell junction intercellular canaliculus anchoring junction cell junction cellular anatomical entity cell projection cell leading edge plasma membrane bounded cell projection lamellipodium cell periphery apical part of cell membrane plasma membrane plasma membrane region cell-cell junction intercellular canaliculus anchoring junction cell junction cellular anatomical entity cell projection cell leading edge plasma membrane bounded cell projection lamellipodium cell periphery apical part of cell membrane plasma membrane plasma membrane region apical plasma membrane cell surface membrane microdomain membrane raft membrane-bounded organelle intracellular anatomical structure intracellular vesicle intracellular membrane-bounded organelle intracellular organelle cytoplasmic vesicle organelle cytoplasm vesicle endocytic vesicle leading edge membrane lamellipodium membrane cell projection membrane extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR001375	Peptidase S9, prolyl oligopeptidase, catalytic domain	Domain
A, B, C, D	IPR040522	Dipeptidyl peptidase 4, low complexity region	Domain
A, B, C, D	IPR029058	Alpha/Beta hydrolase fold	Homologous Superfamily
A, B, C, D	IPR002471	Peptidase S9, serine active site	Active Site
A, B, C, D	IPR002469	Dipeptidylpeptidase IV, N-terminal domain	Domain

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.