Search Results
Overview
| Uniprot ID | P04279 |
|---|---|
| Protein Name | Semenogelin-1 |
| Gene Name | SEMG1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 110 | SQQLLHNKQEGRDHD |
| 153 | QGNSPSGKGISSQYS |
| 173 | LWVHGLSKEQTSVSG |
| 183 | TSVSGAQKGRKQGGS |
| 186 | SGAQKGRKQGGSQSS |
| 205 | TEELVANKQQRETKN |
| 217 | TKNSHQNKGHYQNVV |
| 233 | VREEHSSKVQTSLCP |
| 245 | LCPAHQDKLQHGSKD |
| 265 | DELLVYNKNQHQTKN |
| 271 | NKNQHQTKNLNQDQQ |
| 285 | QHGRKANKISYQSSS |
| 345 | EHSQKANKISYQSSS |
| 367 | YGENGVQKDVSQRSI |
| 380 | SIYSQTEKLVAGKSQ |
| 385 | TEKLVAGKSQIQAPN |
| 404 | PWHGENAKGESGQST |
| 423 | DLLSHEQKGRHQHGS |
| 44 | SQFPHGQKGQHYSGQ |
| 60 | GKQQTESKGSFSIQY |
| 92 | YDLNALHKTTKSQRH |
Function
Predominant protein in semen. It participates in the formation of a gel matrix entrapping the accessory gland secretions and ejaculated spermatozoa. Fragments of semenogelin and/or fragments of the related proteins may contribute to the activation of progressive sperm movements as the gel-forming proteins are fragmented by KLK3/PSA
Protein Sequence
10
MKPNIIFVLS
20
LLLILEKQAA
30
VMGQKGGSKG
40
RLPSEFSQFP
50
HGQKGQHYSG
60
QKGKQQTESK
70
GSFSIQYTYH
80
VDANDHDQSR
90
KSQQYDLNAL
100
HKTTKSQRHL
110
GGSQQLLHNK
120
QEGRDHDKSK
130
GHFHRVVIHH
140
KGGKAHRGTQ
150
NPSQDQGNSP
160
SGKGISSQYS
170
NTEERLWVHG
180
LSKEQTSVSG
190
AQKGRKQGGS
200
QSSYVLQTEE
210
LVANKQQRET
220
KNSHQNKGHY
230
QNVVEVREEH
240
SSKVQTSLCP
250
AHQDKLQHGS
260
KDIFSTQDEL
270
LVYNKNQHQT
280
KNLNQDQQHG
290
RKANKISYQS
300
SSTEERRLHY
310
GENGVQKDVS
320
QSSIYSQTEE
330
KAQGKSQKQI
340
TIPSQEQEHS
350
QKANKISYQS
360
SSTEERRLHY
370
GENGVQKDVS
380
QRSIYSQTEK
390
LVAGKSQIQA
400
PNPKQEPWHG
410
ENAKGESGQS
420
TNREQDLLSH
430
EQKGRHQHGS
440
HGGLDIVIIE
450
QEDDSDRHLA
460
QHLNNDRNPL
FT
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0001669 | acrosomal vesicle |
| Biological Process | GO:0031640 | killing of cells of another organism |
| Biological Process | GO:0090281 | negative regulation of calcium ion import |
| Biological Process | GO:1901318 | negative regulation of flagellated sperm motility |
| Biological Process | GO:1900005 | positive regulation of serine-type endopeptidase activity |
| Biological Process | GO:0048240 | sperm capacitation |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005576 | extracellular region |
| Cellular Component | GO:0005615 | extracellular space |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0032991 | protein-containing complex |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0019731 | antibacterial humoral response |
| Biological Process | GO:0061844 | antimicrobial humoral immune response mediated by antimicrobial peptide |
| Biological Process | GO:0050817 | coagulation |
| Biological Process | GO:0007320 | insemination |
Reference
[1] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.