CATH Superfamily 3.30.60.30
The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was: waiting to be named.
FunFam 3303: Kazal-type serine proteinase inhibitor
Please note: GO annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.
There are 3 GO terms relating to "molecular function"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
| GO Term | Annotations | Evidence |
|---|---|---|
|
Serine-type endopeptidase inhibitor activity GO:0004867
Stops, prevents or reduces the activity of serine-type endopeptidases, enzymes that catalyze the hydrolysis of nonterminal peptide bonds in a polypeptide chain; a serine residue (and a histidine residue) are at the active center of the enzyme.
|
3 | G1N8Y5 (/IDA) P85000 (/IDA) Q5GMQ7 (/IDA) |
|
Protease binding GO:0002020
Interacting selectively and non-covalently with any protease or peptidase.
|
2 | G1N8Y5 (/IPI) Q5GMQ7 (/IPI) |
|
Acrosin binding GO:0032190
Interacting selectively and non-covalently with acrosin, a protein that is found in the acrosomes of sperm and possesses protease and carbohydrate binding activities.
|
2 | G1N8Y5 (/IPI) Q5GMQ7 (/IPI) |
There are 0 GO terms relating to "biological process"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
There are 5 GO terms relating to "cellular component"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
| GO Term | Annotations | Evidence |
|---|---|---|
|
Extracellular space GO:0005615
That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
|
3 | G1N8Y5 (/IDA) P85000 (/IDA) Q5GMQ7 (/IDA) |
|
Cell GO:0005623
The basic structural and functional unit of all organisms. Includes the plasma membrane and any external encapsulating structures such as the cell wall and cell envelope.
|
3 | G1N8Y5 (/IDA) P85000 (/IDA) Q5GMQ7 (/IDA) |
|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
2 | G1N8Y5 (/IDA) Q5GMQ7 (/IDA) |
|
Serine protease inhibitor complex GO:0097180
A heterodimeric protein complex that contains a serine protease inhibitor and a protease; formation of the complex inhibits serine protease activity.
|
2 | G1N8Y5 (/IDA) Q5GMQ7 (/IDA) |
|
Sperm cytoplasmic droplet GO:0097598
A small amount of cytoplasm surrounded by a cell membrane that is generally retained in spermatozoa after spermiogenesis, when the majority of the cytoplasm is phagocytosed by Sertoli cells to produce \residual bodies\. Initially, the droplet is located at the neck just behind the head of an elongated spermatid. During epididymal transit, the cytoplasmic droplet migrates caudally to the annulus at the end of the midpiece; the exact position and time varies by species. The cytoplasmic droplet consists of lipids, lipoproteins, RNAs, a variety of hydrolytic enzymes, receptors, ion channels, and Golgi-derived vesicles. The droplet may be involved in regulatory volume loss (RVD) at ejaculation, and in most species, though not in humans, the cytoplasmic droplet is lost at ejaculation. Note that the cytoplasmic droplet is distinct from \excessive residual cytoplasm\ that sometimes remains in epididymal spermatozoa, particularly when spermiogenesis has been disrupted.
|
2 | G1N8Y5 (/IDA) Q5GMQ7 (/IDA) |
