ID G1TAG6_RABIT Unreviewed; 638 AA.
AC G1TAG6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=Neuroendocrine convertase 2 {ECO:0000256|ARBA:ARBA00039626};
DE EC=3.4.21.94 {ECO:0000256|ARBA:ARBA00039000};
DE AltName: Full=Prohormone convertase 2 {ECO:0000256|ARBA:ARBA00042708};
DE AltName: Full=Proprotein convertase 2 {ECO:0000256|ARBA:ARBA00042083};
GN Name=PCSK2 {ECO:0000313|Ensembl:ENSOCUP00000013658.2};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000013658.2, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000013658.2, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000013658.2,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000013658.2}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000013658.2};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- FUNCTION: Serine endopeptidase which is involved in the processing of
CC hormone and other protein precursors at sites comprised of pairs of
CC basic amino acid residues. Responsible for the release of glucagon from
CC proglucagon in pancreatic A cells. {ECO:0000256|ARBA:ARBA00037494}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of protein hormones and neuropeptides from their
CC precursors, generally by hydrolysis of -Lys-Arg-|- bonds.;
CC EC=3.4.21.94; Evidence={ECO:0000256|ARBA:ARBA00036323};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000256|ARBA:ARBA00004398}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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DR EMBL; AAGW02052478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02052479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02052480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02052481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02052482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02052483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02052484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02052485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02052486; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02052487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002711007.1; XM_002710961.3.
DR AlphaFoldDB; G1TAG6; -.
DR SMR; G1TAG6; -.
DR STRING; 9986.ENSOCUP00000013658; -.
DR MEROPS; S08.073; -.
DR PaxDb; 9986-ENSOCUP00000013658; -.
DR Ensembl; ENSOCUT00000015895.4; ENSOCUP00000013658.2; ENSOCUG00000015893.4.
DR GeneID; 100358339; -.
DR KEGG; ocu:100358339; -.
DR CTD; 5126; -.
DR eggNOG; KOG3526; Eukaryota.
DR GeneTree; ENSGT00940000156965; -.
DR HOGENOM; CLU_002976_4_4_1; -.
DR InParanoid; G1TAG6; -.
DR OMA; FHCEAGT; -.
DR OrthoDB; 5474719at2759; -.
DR TreeFam; TF314277; -.
DR Proteomes; UP000001811; Chromosome 4.
DR Bgee; ENSOCUG00000015893; Expressed in frontal cortex and 9 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0030141; C:secretory granule; IEA:Ensembl.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0034230; P:enkephalin processing; IEA:Ensembl.
DR GO; GO:0030070; P:insulin processing; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; IEA:Ensembl.
DR GO; GO:0016540; P:protein autoprocessing; IEA:Ensembl.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.30.70.850; Peptidase S8, pro-domain; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR034182; Kexin/furin.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR032815; S8_pro-domain.
DR InterPro; IPR038466; S8_pro-domain_sf.
DR PANTHER; PTHR42884:SF13; NEUROENDOCRINE CONVERTASE 2; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF16470; S8_pro-domain; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..638
FT /note="Neuroendocrine convertase 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003423064"
FT DOMAIN 461..597
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT ACT_SITE 167
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 208
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 384
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 638 AA; 70499 MW; 4A7CBA63D8CE079D CRC64;
MQGGSISRWQ AAAGLLLCAT VFASSERAVF TNHFLVELHK GGEEEARQVA AEHGFGVRKL
PFTDGLYHFY HNGLAKAKRR RSLHHKQQLE RDPRVKMALQ QEGFDRKKRG YRDINEIDIN
MNDPLFTKQW YLINTGQADG TPGLDLNVAE AWELGYTGKG VTIGIMDDGI DYLHPDLASN
YNAEASYDFS SNDPYPYPRY TDDWFNSHGT RCAGEVSAAA NNNICGVGVA YNSKVAGIRM
LDQPFMTDII EASSISHMPQ LIDIYSASWG PTDNGKTVDG PRELTLQAMA DGVNKGRGGK
GSIYVWASGD GGSYDDCNCD GYASSMWTIS INSAINDGRT ALYDESCSST LASTFSNGRK
RNPEAGVATT DLYGNCTLRH SGTSAAAPEA AGVFALALEA NLGLTWRDMQ HLTVLTSKRN
QLHDEVHQWR RNGVGLEFNH LFGYGVLDAG AMVKMAKDWK TVPERFHCVG GSVQDPEKIP
PTGKLVLTLT TDACEGKENF VRYLEHVQAV ITVNATRRGD LNINMTSPMG TKSILLSRRP
RDDDSKVGFD KWPFMTTHTW GEDARGTWTL ELGFVGSTPQ KGVLKEWTLM LHGTQSAPYI
DQVVRDYQSK LAMSKKEELE EELDEAVERS LQSILSKN
//