Annotations: 1SAC

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1saca_	All beta proteins	Concanavalin A-like lectins/glucanases	Concanavalin A-like lectins/glucanases	Pentraxin (pentaxin)	Serum amyloid P component (SAP)	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d1sacb_	All beta proteins	Concanavalin A-like lectins/glucanases	Concanavalin A-like lectins/glucanases	Pentraxin (pentaxin)	Serum amyloid P component (SAP)	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d1sacc_	All beta proteins	Concanavalin A-like lectins/glucanases	Concanavalin A-like lectins/glucanases	Pentraxin (pentaxin)	Serum amyloid P component (SAP)	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d1sacd_	All beta proteins	Concanavalin A-like lectins/glucanases	Concanavalin A-like lectins/glucanases	Pentraxin (pentaxin)	Serum amyloid P component (SAP)	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
E	d1sace_	All beta proteins	Concanavalin A-like lectins/glucanases	Concanavalin A-like lectins/glucanases	Pentraxin (pentaxin)	Serum amyloid P component (SAP)	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Pentraxin (pentaxin)	8029051	4002704	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Concanavalin A-like lectins/glucanases	8041430	3000120	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Concanavalin A-like lectins/glucanases	8041430	3000120	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Concanavalin A-like lectins/glucanases	8041430	3000120	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Concanavalin A-like lectins/glucanases	8041430	3000120	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Concanavalin A-like lectins/glucanases	8041430	3000120	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Pentaxin	e1sacA1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Concanavalin A-like lectins/glucanases	F: Pentaxin	ECOD (1.6)
B	Pentaxin	e1sacB1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Concanavalin A-like lectins/glucanases	F: Pentaxin	ECOD (1.6)
C	Pentaxin	e1sacC1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Concanavalin A-like lectins/glucanases	F: Pentaxin	ECOD (1.6)
D	Pentaxin	e1sacD1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Concanavalin A-like lectins/glucanases	F: Pentaxin	ECOD (1.6)
E	Pentaxin	e1sacE1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Concanavalin A-like lectins/glucanases	F: Pentaxin	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.120.200	Mainly Beta	Sandwich	Jelly Rolls		CATH (4.3.0)
B	2.60.120.200	Mainly Beta	Sandwich	Jelly Rolls		CATH (4.3.0)
C	2.60.120.200	Mainly Beta	Sandwich	Jelly Rolls		CATH (4.3.0)
D	2.60.120.200	Mainly Beta	Sandwich	Jelly Rolls		CATH (4.3.0)
E	2.60.120.200	Mainly Beta	Sandwich	Jelly Rolls		CATH (4.3.0)

IMGT Antibody Annotation IMGT Database Homepage

Chain	Protein Name	Description	Organism Name	Gene Allele Name(s)	Domain Name(s)	Receptor Type	Receptor Description	Provenance Source
A, B, C, D, E	Pentraxin (APCS serum amyloid P component, SAP)	APCS (Pr20-223)	Homo sapiens (human)	APCS*01	P-LIKE-DOMAIN APCS (Pr20-223)	RPI	(APCS (Pr20-223))	IMGT (202443-0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E	PF00354	Pentaxin family (Pentaxin)	Pentaxin family	Pentaxins are also known as pentraxins.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E	SERUM AMYLOID P COMPONENT	cation binding ion binding binding calcium ion binding metal ion binding small molecule binding complement component C1q complex binding opsonin binding protein-containing complex binding protein binding complement binding carbohydrate binding unfolded protein binding virion binding cation binding ion binding binding calcium ion binding metal ion binding small molecule binding complement component C1q complex binding opsonin binding protein-containing complex binding protein binding complement binding carbohydrate binding unfolded protein binding virion binding identical protein binding	negative regulation of glycoprotein metabolic process regulation of biological process regulation of protein metabolic process negative regulation of metabolic process biological regulation negative regulation of biological process carbohydrate derivative metabolic process primary metabolic process regulation of macromolecule metabolic process glycoprotein metabolic process regulation of glycoprotein metabolic process regulation of primary metabolic process metabolic process protein metabolic process negative regulation of glycoprotein metabolic process regulation of biological process regulation of protein metabolic process negative regulation of metabolic process biological regulation negative regulation of biological process carbohydrate derivative metabolic process primary metabolic process regulation of macromolecule metabolic process glycoprotein metabolic process regulation of glycoprotein metabolic process regulation of primary metabolic process metabolic process protein metabolic process macromolecule metabolic process regulation of metabolic process negative regulation of protein metabolic process negative regulation of macromolecule metabolic process cellular component organization cellular component biogenesis cellular component assembly chaperone-mediated protein complex assembly protein-containing complex organization protein-containing complex assembly cellular process cellular component organization or biogenesis cellular biosynthetic process cellular metabolic process gene expression macromolecule biosynthetic process protein maturation protein folding biosynthetic process biological process involved in interspecies interaction between organisms modulation by host of viral exo-alpha-sialidase activity modulation by host of symbiont process negative regulation by host of viral exo-alpha-sialidase activity modulation by host of symbiont catalytic activity modulation by host of viral catalytic activity biological process involved in symbiotic interaction modulation by host of viral molecular function modulation by host of viral process negative regulation by host of symbiont catalytic activity biological process involved in interaction with symbiont negative regulation of hydrolase activity negative regulation of exo-alpha-sialidase activity regulation of molecular function regulation of catalytic activity regulation of hydrolase activity regulation of exo-alpha-sialidase activity negative regulation of molecular function negative regulation of catalytic activity negative regulation of viral process regulation of viral process viral process response to stimulus immune response response to other organism defense response defense response to symbiont response to external stimulus response to biotic stimulus immune system process defense response to other organism response to stress innate immune response response to external biotic stimulus negative regulation by host of viral process modulation by host of viral glycoprotein metabolic process negative regulation by host of viral glycoprotein metabolic process wound healing regulation of response to external stimulus negative regulation of response to stimulus negative regulation of wound healing negative regulation of response to wounding regulation of response to wounding regulation of response to stimulus regulation of response to stress negative regulation of response to external stimulus regulation of wound healing response to wounding negative regulation of viral life cycle viral life cycle modulation by symbiont of entry into host biological process involved in interaction with host regulation of viral entry into host cell regulation of viral life cycle symbiont entry into host cell symbiont entry into host negative regulation of viral entry into host cell regulation of biological process involved in symbiotic interaction acute-phase response inflammatory response acute inflammatory response regulation of defense response negative regulation of acute inflammatory response negative regulation of inflammatory response regulation of inflammatory response negative regulation of defense response regulation of acute inflammatory response myeloid leukocyte differentiation regulation of leukocyte differentiation multicellular organismal process regulation of cellular process cellular developmental process regulation of developmental process cell development mononuclear cell differentiation regulation of cell differentiation regulation of cell development multicellular organism development cell differentiation anatomical structure development negative regulation of cellular process regulation of immune system process regulation of multicellular organismal process negative regulation of cell differentiation monocyte differentiation negative regulation of hemopoiesis negative regulation of monocyte differentiation developmental process regulation of multicellular organismal development regulation of monocyte differentiation negative regulation of leukocyte differentiation hemopoiesis regulation of myeloid cell differentiation negative regulation of developmental process regulation of myeloid leukocyte differentiation negative regulation of myeloid cell differentiation negative regulation of myeloid leukocyte differentiation negative regulation of cell development myeloid cell differentiation negative regulation of immune system process regulation of hemopoiesis negative regulation of multicellular organismal process leukocyte differentiation	extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space cellular anatomical entity vesicle extracellular membrane-bounded organelle cell periphery extracellular matrix external encapsulating structure collagen-containing extracellular matrix extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space cellular anatomical entity vesicle extracellular membrane-bounded organelle cell periphery extracellular matrix external encapsulating structure collagen-containing extracellular matrix blood microparticle intracellular organelle intracellular anatomical structure nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E	IPR001759	Pentraxin-related	Family
A, B, C, D, E	IPR030476	Pentaxin, conserved site	Conserved Site
A, B, C, D, E	IPR013320	Concanavalin A-like lectin/glucanase domain superfamily	Homologous Superfamily
A, B, C, D, E	IPR051005	Pentraxin domain-containing protein	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D, E	Pharos: P02743	coronary artery disease liver cancer congestive heart failure Heart Decompensation hepatocellular carcinoma AA amyloidosis pancreatic ductal adenocarcinoma ADan amyloidosis Alzheimer disease heart failure hypotrichosis 2 liver neoplasm ABri amyloidosis medullary thyroid gland carcinoma pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia coronary artery disease liver cancer congestive heart failure Heart Decompensation hepatocellular carcinoma AA amyloidosis pancreatic ductal adenocarcinoma ADan amyloidosis Alzheimer disease heart failure hypotrichosis 2 liver neoplasm ABri amyloidosis medullary thyroid gland carcinoma pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia type 2 diabetes mellitus amyloidosis cerebral amyloid angiopathy, APP-related Finnish type amyloidosis ACys amyloidosis primary cutaneous amyloidosis Creutzfeldt Jacob disease

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), 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 R01GM157729.