ID G3QXL8_GORGO Unreviewed; 732 AA.
AC G3QXL8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Carboxypeptidase X, M14 family member 1 {ECO:0000313|Ensembl:ENSGGOP00000007568.3};
GN Name=CPXM1 {ECO:0000313|Ensembl:ENSGGOP00000007568.3};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000007568.3, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000007568.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000007568.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000007568.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR EMBL; CABD030115286; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004061758.1; XM_004061710.1.
DR AlphaFoldDB; G3QXL8; -.
DR STRING; 9593.ENSGGOP00000007568; -.
DR MEROPS; M14.039; -.
DR Ensembl; ENSGGOT00000007770.3; ENSGGOP00000007568.3; ENSGGOG00000007734.3.
DR GeneID; 101144115; -.
DR KEGG; ggo:101144115; -.
DR CTD; 56265; -.
DR eggNOG; KOG2649; Eukaryota.
DR GeneTree; ENSGT00940000156141; -.
DR HOGENOM; CLU_006722_4_0_1; -.
DR InParanoid; G3QXL8; -.
DR OMA; TDRRPCH; -.
DR OrthoDB; 5490979at2759; -.
DR TreeFam; TF315592; -.
DR Proteomes; UP000001519; Chromosome 20.
DR Bgee; ENSGGOG00000007734; Expressed in heart and 5 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR CDD; cd00057; FA58C; 1.
DR CDD; cd03869; M14_CPX_like; 1.
DR CDD; cd11308; Peptidase_M14NE-CP-C_like; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11532:SF43; CARBOXYPEPTIDASE X1-RELATED; 1.
DR PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 1.
DR Pfam; PF13620; CarboxypepD_reg; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
DR PROSITE; PS50022; FA58C_3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..732
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014172854"
FT DOMAIN 111..272
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 30..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 732 AA; 81593 MW; 00896891FBE2EB63 CRC64;
MWGLLLALAA FAPAVGPALG APRNSGLGLA QPGTTKVPGS IPALHSSPAQ PPAETPNGTS
EQHVRIRVIK KKKVIMKKRK KLTRPTPLVT ARPLVTPTPA GTLNPTEKQE TGCPPLGLES
LRVSDSRLEA SSSQSFGLGP HRGRLNIQSG LEDGDLYDGG WCAEEQDTDP WFQVDAGHPT
RFSGVITQGR NSVWRYDWVT SYKVQFSNDS RTWWGSRNHS SGMDAVFPAN SDPETPVLNL
LPEPQVARFI RLLPQTWLQG GAPCLRAEIL ACPVSDPNDL FLEAPASGSS DPLDFQHHNY
KAMRKLMKQV QEQCPNITRI YSIGKSYQGL KLYVMEMSDQ PGEHELGEPE VRYVAGMHGN
EALGRELLLL LMQFLCHEFL RGNPRVTRLL SEMRIHLLPS MNPDGYEIAY HRGSELVGWA
EGRWNNQSID LNHNFADLNT PLWEAQDDGK VPHIVPNHHL PLPTYYTLPN ATVAPETRAV
IKWMKRIPFV LSANLHGGEL VVSYPFDMTR TPWAARELTP TPDDAVFRWL STVYAGSNLA
MQDTSRRPCH SQDFSVHGNI INGADWHTVP GSMNDFSYLH TNCFEVTVEL SCDKFPHENE
LPQEWENNKD ALLTYLEQVR MGIAGVVRDK DTELGIADAV IAVDGINHDV TTAWGGDYWR
LLTPGDYMVT ASAEGYHSVT RNCRVTFEEG PFPCNFVLTK TPKQRLRELL AAGAKVPPDL
RRRLERLRGQ KD
//
