Annotations: 4MZV

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	EUF08377	e4mzvA3	A: a+b two layers	X: Alpha-beta plaits	H: Ferredoxin-like domain of receptor-type protein tyrosine phosphatase (From Topology)	T: Ferredoxin-like domain of receptor-type protein tyrosine phosphatase	F: EUF08377	ECOD (1.6)
A	Thyroglobulin_1	e4mzvA2	A: few secondary structure elements	X: Thyroglobulin type-1 domain (From Topology)	H: Thyroglobulin type-1 domain (From Topology)	T: Thyroglobulin type-1 domain	F: Thyroglobulin_1	ECOD (1.6)
A	EUF08757	e4mzvA1	A: few secondary structure elements	X: N-terminal domain of EpCAM (From Topology)	H: N-terminal domain of EpCAM (From Topology)	T: N-terminal domain of EpCAM	F: EUF08757	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF21283	EPCAM/Trop-2, C-terminal (EPCAM-Trop-2_C)	EPCAM/Trop-2, C-terminal	EpCAM (epithelial cell adhesion molecule, also known as Trop-1) and Trop-2 (also known as tumor-associated calcium signal transducer 2, TACSTD2) are transmembrane glycoproteins that belong to the tumour-associated calcium signal transducer (TACSTD) f ...	EpCAM (epithelial cell adhesion molecule, also known as Trop-1) and Trop-2 (also known as tumor-associated calcium signal transducer 2, TACSTD2) are transmembrane glycoproteins that belong to the tumour-associated calcium signal transducer (TACSTD) family. They are evolutionarily related and both are implicated in signaling triggered by proteolytic cleavage within the ectodomain [1,3]. They share an overall similar structure but differ in their dimers formation. They consist of an ectodomain with an N-terminal, thyroglobulin type-1 (TY, Pfam:PF00086) and C-terminal domains. This entry represents the C-terminal domain of EpCAM and Trop-2, which has an alpha+beta fold [1-3].	Domain
A	PF00086	Thyroglobulin type-1 repeat (Thyroglobulin_1)	Thyroglobulin type-1 repeat	Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation [2]. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.	Domain
A	PF18635	Epithelial cell adhesion molecule, N-terminal domain (EpCAM_N)	Epithelial cell adhesion molecule, N-terminal domain	EpCAM (epithelial cell adhesion molecule), a stem and carcinoma cell marker, is a cell surface protein involved in homotypic cell-cell adhesion via intercellular oligomerization and proliferative signalling via proteolytic cleavage. Structure analysi ...	EpCAM (epithelial cell adhesion molecule), a stem and carcinoma cell marker, is a cell surface protein involved in homotypic cell-cell adhesion via intercellular oligomerization and proliferative signalling via proteolytic cleavage. Structure analysis indicate that it is composed of three domains: N-domain, Thyroglobulin type-1A (TY) domain and the C-terminal domain. This entry represents the small and compact disulphide-rich N-terminal domain of 39 amino-acid residues [1]. Trop-2 (also known as tumor-associated calcium signal transducer 2, TACSTD2) is also included in this entry, as they are evolutionarily related and both are implicated in signaling triggered by proteolytic cleavage within the ectodomain [1-3]. They share an overall similar structure but differ in their dimers formation.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Epithelial cell adhesion molecule	protein-containing complex binding binding cell adhesion molecule binding cadherin binding involved in cell-cell adhesion cadherin binding protein binding cell adhesion mediator activity cell-cell adhesion mediator activity	regulation of biological process cell population proliferation regulation of cellular process positive regulation of cell population proliferation regulation of cell population proliferation biological regulation positive regulation of biological process cellular process positive regulation of cellular process ureteric bud development developmental process multicellular organismal process mesonephric epithelium development epithelium development regulation of biological process cell population proliferation regulation of cellular process positive regulation of cell population proliferation regulation of cell population proliferation biological regulation positive regulation of biological process cellular process positive regulation of cellular process ureteric bud development developmental process multicellular organismal process mesonephric epithelium development epithelium development kidney epithelium development mesonephros development tube development animal organ development tissue development renal system development multicellular organism development anatomical structure development kidney development mesonephric tubule development system development regulation of cell adhesion negative regulation of biological process negative regulation of cell adhesion cell adhesion cell-cell adhesion negative regulation of cell-cell adhesion mediated by cadherin cell-cell adhesion mediated by cadherin negative regulation of cell-cell adhesion negative regulation of cellular process regulation of cell-cell adhesion regulation of cell-cell adhesion mediated by cadherin cellular response to stimulus regulation of biosynthetic process response to stimulus signaling regulation of macromolecule metabolic process gene expression macromolecule biosynthetic process cell communication regulation of gene expression signal transduction involved in regulation of gene expression biosynthetic process regulation of macromolecule biosynthetic process metabolic process signal transduction macromolecule metabolic process regulation of metabolic process stem cell differentiation cellular developmental process cell differentiation regulation of stem cell proliferation positive regulation of stem cell proliferation stem cell proliferation positive regulation of DNA-templated transcription RNA metabolic process positive regulation of macromolecule biosynthetic process regulation of primary metabolic process nucleobase-containing compound metabolic process RNA biosynthetic process nucleic acid biosynthetic process positive regulation of metabolic process DNA-templated transcription regulation of RNA metabolic process transcription by RNA polymerase II positive regulation of biosynthetic process positive regulation of macromolecule metabolic process regulation of nucleobase-containing compound metabolic process regulation of RNA biosynthetic process regulation of transcription by RNA polymerase II positive regulation of nucleobase-containing compound metabolic process primary metabolic process positive regulation of transcription by RNA polymerase II nucleobase-containing compound biosynthetic process nucleic acid metabolic process positive regulation of RNA metabolic process positive regulation of RNA biosynthetic process regulation of DNA-templated transcription	cell periphery cellular anatomical structure apical part of cell membrane plasma membrane plasma membrane region apical plasma membrane extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space cell periphery cellular anatomical structure apical part of cell membrane plasma membrane plasma membrane region apical plasma membrane extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle cell surface cell-cell junction apical junction complex bicellular tight junction tight junction anchoring junction cell junction basal part of cell basal plasma membrane basolateral plasma membrane lateral plasma membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR043406	Transmembrane glycoprotein EPCAM/Trop-2	Family
A	IPR049420	EPCAM/Trop-2, C-terminal	Domain
A	IPR041630	Epithelial cell adhesion molecule N-terminal domain	Domain
A	IPR036857	Thyroglobulin type-1 superfamily	Homologous Superfamily
A	IPR000716	Thyroglobulin type-1	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: P16422	Lynch syndrome congenital diarrhea 5 with tufting enteropathy colorectal cancer, hereditary nonpolyposis, type 8 ovarian cancer prostate cancer Lynch syndrome 1 carcinoma sarcomatoid carcinoma Mammary Neoplasms, Experimental pancreatic intraductal papillary-mucinous neoplasm invasive ductal breast carcinoma psoriasis liver disease lung carcinoma acute myeloid leukemia Lynch syndrome congenital diarrhea 5 with tufting enteropathy colorectal cancer, hereditary nonpolyposis, type 8 ovarian cancer prostate cancer Lynch syndrome 1 carcinoma sarcomatoid carcinoma Mammary Neoplasms, Experimental pancreatic intraductal papillary-mucinous neoplasm invasive ductal breast carcinoma psoriasis liver disease lung carcinoma acute myeloid leukemia astrocytic tumor malignant glioma breast carcinoma mammary neoplasms, animal nasopharyngeal carcinoma pancreatic ductal adenocarcinoma pancreatic neoplasm interstitial cystitis prostate disease large cell medulloblastoma lung adenocarcinoma lung disease atypical teratoid rhabdoid tumor malignant mesothelioma breast disease malignant pancreatic neoplasm ductal breast carcinoma in situ nephrosclerosis glioblastoma ovarian disease pancreatic intraductal papillary-mucinous carcinoma periodontitis intestinal disease undifferentiated carcinoma lung cancer malignant ependymoma Barrett esophagus cancer medulloblastoma esophageal adenocarcinoma oligodendroglioma hereditary breast carcinoma ovarian neoplasm

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A	PCA	Parent Component: GLN RESID: AA0031 PSI-MOD : 2-pyrrolidone-5-carboxylic acid (Gln) MOD:00040 , 2-pyrrolidone-5-carboxylic acid (Glu) MOD:00420

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.