ID A0A096N6P3_PAPAN Unreviewed; 855 AA.
AC A0A096N6P3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Suppressor of tumorigenicity 14 protein homolog {ECO:0000256|PIRNR:PIRNR036370};
DE EC=3.4.21.109 {ECO:0000256|PIRNR:PIRNR036370};
DE AltName: Full=Serine protease 14 {ECO:0000256|PIRNR:PIRNR036370};
GN Name=ST14 {ECO:0000313|Ensembl:ENSPANP00000008168.2};
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000008168.2, ECO:0000313|Proteomes:UP000028761};
RN [1] {ECO:0000313|Ensembl:ENSPANP00000008168.2, ECO:0000313|Proteomes:UP000028761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT "Whole Genome Assembly of Papio anubis.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPANP00000008168.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Exhibits trypsin-like activity as defined by cleavage of
CC synthetic substrates with Arg or Lys as the P1 site.
CC {ECO:0000256|PIRNR:PIRNR036370}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleaves various synthetic substrates with Arg or Lys at the P1
CC position and prefers small side-chain amino acids, such as Ala and
CC Gly, at the P2 position.; EC=3.4.21.109;
CC Evidence={ECO:0000256|PIRNR:PIRNR036370};
CC -!- SUBUNIT: Interacts with CDCP1. May interact with TMEFF1.
CC {ECO:0000256|PIRNR:PIRNR036370}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|PIRNR:PIRNR036370}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR AlphaFoldDB; A0A096N6P3; -.
DR STRING; 9555.ENSPANP00000008168; -.
DR MEROPS; S01.302; -.
DR Ensembl; ENSPANT00000019454.3; ENSPANP00000008168.2; ENSPANG00000001818.3.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000155418; -.
DR HOGENOM; CLU_006842_19_3_1; -.
DR OMA; PTKWTAF; -.
DR OrthoDB; 5394933at2759; -.
DR Proteomes; UP000028761; Chromosome 12.
DR Bgee; ENSPANG00000001818; Expressed in ascending colon and 42 other cell types or tissues.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0060672; P:epithelial cell morphogenesis involved in placental branching; IEA:Ensembl.
DR GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00112; LDLa; 4.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 4.
DR Gene3D; 3.30.70.960; SEA domain; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR017051; Peptidase_S1A_matripase.
DR InterPro; IPR000082; SEA_dom.
DR InterPro; IPR036364; SEA_dom_sf.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252:SF8; ACROSIN; 1.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00057; Ldl_recept_a; 4.
DR Pfam; PF01390; SEA; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF036370; ST14; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00192; LDLa; 4.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 4.
DR SUPFAM; SSF82671; SEA domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 4.
DR PROSITE; PS50024; SEA; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR036370, ECO:0000256|RuleBase:RU363034};
KW Membrane {ECO:0000256|PIRNR:PIRNR036370, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|PIRNR:PIRNR036370, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000028761};
KW Serine protease {ECO:0000256|PIRNR:PIRNR036370,
KW ECO:0000256|RuleBase:RU363034};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 55..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 86..203
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 214..334
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 340..447
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 615..854
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 656
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036370-1"
FT ACT_SITE 711
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036370-1"
FT ACT_SITE 805
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036370-1"
FT DISULFID 459..477
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 471..486
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 496..514
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 508..523
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 525..537
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 532..550
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 544..559
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 567..579
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 587..602
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 855 AA; 94666 MW; 5642F985D2165F23 CRC64;
MGSNQARKGG GGPKDFGAGL KYSSRHEKVN GLEEGVEFLP VNNVKKVEKH GPGRWVVLAA
VLIGLLLVSL GIGSLVWHLQ YRDVRVQKIF NGYLRITNEN FVDAYENSNS TEFVSLASKV
KDALKLLYSG VPFLGPYHKE SAVTAFSEGS VIAYYWSEFS IPQHLVEEAE RVMAEERVVM
LPPRARSLKS FVVTSVVAFP TDPKTVQRTQ DNSCSFALHA RGVEVMRFTT PGFPDSPYPA
HARCQWALRG DADSVLSLTF RSFDLASCDE RGSDLVTVYN TLSPMEPHAL VQLCGAYPPS
YNLTFLSSQN VLLITLITNT ERRHPGFEAT FFQLPKMSRC GGHLRKAQGT FNSPYYPGHY
PPNIDCTWNI EVPNNQHVKV RFKFFYLLEP GVPTGTCPKD YVEINGEKYC GERSQFVVTS
NSNKITVHFH SDQSYTDTGF LAEYLSYDAS DPCPGQFTCR TGRCIRKEMR CDGWADCTDY
SDELNCSCDA THQFTCKNKF CKPLFWVCDS VNDCGDNSDE QGCSCPAQTF RCSNGKCLSK
SQQCDGKDDC GDGSDEASCP KVNVVTCTKH TYRCLNGLCL SKGNPECDGK KDCSDGSDEK
DCDCGLRSFT RQARVVGGTD ADEGEWPWQV SLHALGQGHV CGASLISPNW LVSAAHCYID
DRGFRYSDPT QWTAFLGLHD QSQRSAPEVQ ERRLKRIISH PSFNDFTFDY DIALLELEKP
VEYSSVVRPI CLPDASHVFP AGKAIWVTGW GHTQYGGTGA LILQKGEIRV INQTTCESLL
PQQITPRMMC VGFLSGGVDS CQGDSGGPLS SVEADGRIFQ AGVVSWGDGC AQRNKPGVYT
RLPLFRDWIK EKTGV
//
