SCPL2_DICDI
ID SCPL2_DICDI Reviewed; 563 AA.
AC Q54VW1;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Serine carboxypeptidase S10 family member 2;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN ORFNames=DDB_G0280105;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Probable carboxypeptidase. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; AAFI02000035; EAL67279.1; -; Genomic_DNA.
DR RefSeq; XP_641244.1; XM_636152.1.
DR AlphaFoldDB; Q54VW1; -.
DR SMR; Q54VW1; -.
DR STRING; 44689.DDB0229903; -.
DR ESTHER; dicdi-q54vw1; Carboxypeptidase_S10.
DR MEROPS; S10.A68; -.
DR PaxDb; Q54VW1; -.
DR EnsemblProtists; EAL67279; EAL67279; DDB_G0280105.
DR GeneID; 8622375; -.
DR KEGG; ddi:DDB_G0280105; -.
DR dictyBase; DDB_G0280105; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_1_1; -.
DR InParanoid; Q54VW1; -.
DR OMA; EMADQFV; -.
DR PhylomeDB; Q54VW1; -.
DR PRO; PR:Q54VW1; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Zymogen.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..?
FT /evidence="ECO:0000255"
FT /id="PRO_0000331590"
FT CHAIN ?..563
FT /note="Serine carboxypeptidase S10 family member 2"
FT /id="PRO_0000331591"
FT TOPO_DOM 24..529
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 551..563
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 417
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 479
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 563 AA; 63223 MW; 30C6BCACAF815AB8 CRC64;
MNIKIILLSI ILIIQLLLLN NNGGIVESKI NFSKRKQTDR KPNPSPKTYT KEYYDNKYLK
SLKNVKQTPN DFLVTDLPGL DNGILTSFSG LLTTNETSDG NLFFWFFPAN ETVINPMDAP
LLVWLNGGPG CSSMDSVFIE TGPLRFIGDS DNSDKFYINP WSWHNSANML YIDQPFGTGL
SFVSDNDGLV TNDLEINQNF YQFIQEFFQI FSNYSTLPFF ISGESYAGHY IPHMASYILN
MNENLSKDSI KINLQGVAIG NGYTHPTTQI NSYREFGYYA TGIIGQRQYN NYENLNNLCQ
EQLSQGNYNS DECANVFNTL LDDSGSSNTS QVNMYDYRLN DPTAGNNWPL PGINQEFVYL
NRDDVRSAIH ATVTPHQWNE CNDTVNGLLT NQDESSLYLF PELLSNIRVL IYNGQFDVIC
NHVGTTEYLN QIEWDYTQEW SDAPRFTWTS VGTDGSLQSG GYGKTAANLT FVLALGGSHM
YPMNMPSTSF DMITRFLKNK SFNDLPQSIG IDAPSTPKPV PLTLGAWIGI TVGGCAFGFL
VGGLIIYIIM KKSSKNGYYK VIQ
