SEMG1_SAGOE
ID SEMG1_SAGOE Reviewed; 615 AA.
AC O77733;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Semenogelin-1;
DE AltName: Full=Semenogelin I;
DE Short=SGI;
DE Flags: Precursor;
GN Name=SEMG1;
OS Saguinus oedipus (Cotton-top tamarin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Saguinus.
OX NCBI_TaxID=9490;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=9692899; DOI=10.1046/j.1432-1327.1998.2550045.x;
RA Lundwall A.;
RT "The cotton-top tamarin carries an extended semenogelin I gene but no
RT semenogelin II gene.";
RL Eur. J. Biochem. 255:45-51(1998).
CC -!- FUNCTION: Predominant protein in semen. It participates in the
CC formation of a gel matrix entrapping the accessory gland secretions and
CC ejaculated spermatozoa. Fragments of semenogelin and/or fragments of
CC the related proteins may contribute to the activation of progressive
CC sperm movements as the gel-forming proteins are fragmented by KLK3/PSA
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Occurs in disulfide-linked complexes. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- PTM: Transglutaminase substrate. {ECO:0000250}.
CC -!- PTM: Rapidly cleaved after ejaculation by KLK3/PSA, resulting in
CC liquefaction of the semen coagulum and the progressive release of
CC motile spermatozoa. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the semenogelin family. {ECO:0000305}.
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DR EMBL; AJ002153; CAA05213.1; -; Genomic_DNA.
DR AlphaFoldDB; O77733; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050817; P:coagulation; IEA:InterPro.
DR GO; GO:1901318; P:negative regulation of flagellated sperm motility; IEA:InterPro.
DR InterPro; IPR008836; Semenogelin.
DR Pfam; PF05474; Semenogelin; 3.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Pyrrolidone carboxylic acid; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..615
FT /note="Semenogelin-1"
FT /id="PRO_0000032355"
FT REGION 24..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 238
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 615 AA; 68118 MW; F2D7E0A05B60399D CRC64;
MKPIIFLVLS LLLILEKQAA VMGQKGGSKG RLPSESSQFP HGQKGQQYCA RKDKQHAESK
RSVSIEHTYH VDIPDHDQTR TSKQYDLNAQ NKRIKSEKHA AGSQEPFNHK QEGREHGKSK
GDFHVLIIHH KRGHAPHGTQ NPSQDQGNST SGKGISSQDS NTKERLLALG LGKEQDSVSG
TQRNGTQGGS QSSPVLQTED PVHNKKPETQ NSLQNKGSSP NVNETKQKHS SKVQSPLCSA
QEDRLQHGSK DVFSKNQNQT RNPNQDQEHG QKAHNRSCQC SSTEERRPNH GEKGIQKDAS
KGSTSNQTED KMHDKSQKQV TTPSQEDGHR ANKTSSQSSG TEERRPNHGE KGIQKDASKG
STSNQTEDKM HDKSQKQVTT PSQEDGHRAN KTSSQSSGTE ERRPNHGEKG IQKDASKGST
SNQTEDKMHD KSQKQVTTPS QEDGHRANKT SSQSSGTEER RPNHGEKGIQ KDASKGSTSN
KTEDKMHDKS QKQVTTPSQE DGHRANKTSS QSSGTEERRP NHGEKGIQKD ASKGSSSNKT
EDEKHDKSQK QVTTPSQDQQ SGQDADEEED LLSHYQKDRH QHRSYGGLDI VIVEHEADDD
DRLTHHDNNQ NSIFT
