PEP2B_GADMO
ID PEP2B_GADMO Reviewed; 324 AA.
AC P56272;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Pepsin-2B;
DE EC=3.4.23.-;
DE AltName: Full=Pepsin IIB;
OS Gadus morhua (Atlantic cod).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX NCBI_TaxID=8049;
RN [1]
RP PROTEIN SEQUENCE, AND CRYSTALLIZATION.
RC TISSUE=Stomach;
RX PubMed=9761815; DOI=10.1107/s090744499700810x;
RA Karlsen S., Hough E., Olsen R.L.;
RT "Structure and proposed amino-acid sequence of a pepsin from Atlantic cod
RT (Gadus morhua).";
RL Acta Crystallogr. D 54:32-46(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS).
RX PubMed=2113846; DOI=10.1016/0305-0491(90)90382-4;
RA Gildberg A., Olsen R.L., Bjarnason J.B.;
RT "Catalytic properties and chemical composition of pepsins from Atlantic cod
RT (Gadus morhua).";
RL Comp. Biochem. Physiol. 96B:323-330(1990).
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PDB; 1AM5; X-ray; 2.16 A; A=1-324.
DR PDBsum; 1AM5; -.
DR AlphaFoldDB; P56272; -.
DR SMR; P56272; -.
DR MEROPS; A01.055; -.
DR PRIDE; P56272; -.
DR EvolutionaryTrace; P56272; -.
DR Proteomes; UP000694546; Unplaced.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; PTHR47966; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aspartyl protease; Digestion; Direct protein sequencing;
KW Disulfide bond; Hydrolase; Protease; Reference proteome.
FT CHAIN 1..324
FT /note="Pepsin-2B"
FT /id="PRO_0000199516"
FT DOMAIN 14..321
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT REGION 86..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 32
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT DISULFID 45..50
FT /evidence="ECO:0000250"
FT DISULFID 206..209
FT /evidence="ECO:0000250"
FT DISULFID 247..280
FT /evidence="ECO:0000250"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:1AM5"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:1AM5"
FT STRAND 13..20
FT /evidence="ECO:0007829|PDB:1AM5"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:1AM5"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:1AM5"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1AM5"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:1AM5"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1AM5"
FT STRAND 65..74
FT /evidence="ECO:0007829|PDB:1AM5"
FT STRAND 79..94
FT /evidence="ECO:0007829|PDB:1AM5"
FT STRAND 96..106
FT /evidence="ECO:0007829|PDB:1AM5"
FT TURN 110..114
FT /evidence="ECO:0007829|PDB:1AM5"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:1AM5"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1AM5"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1AM5"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:1AM5"
FT STRAND 146..154
FT /evidence="ECO:0007829|PDB:1AM5"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:1AM5"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:1AM5"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:1AM5"
FT TURN 187..190
FT /evidence="ECO:0007829|PDB:1AM5"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:1AM5"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:1AM5"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:1AM5"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:1AM5"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:1AM5"
FT HELIX 227..234
FT /evidence="ECO:0007829|PDB:1AM5"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:1AM5"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:1AM5"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:1AM5"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:1AM5"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:1AM5"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:1AM5"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:1AM5"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:1AM5"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:1AM5"
FT HELIX 301..306
FT /evidence="ECO:0007829|PDB:1AM5"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:1AM5"
FT TURN 313..316
FT /evidence="ECO:0007829|PDB:1AM5"
FT STRAND 317..323
FT /evidence="ECO:0007829|PDB:1AM5"
SQ SEQUENCE 324 AA; 34014 MW; EE3A6097B6941DD7 CRC64;
RVTEQMKNEA DTEYYGVISI GTPPESFKVI FDTGSSNLWV SSSHCSAQAC SNHNKFKPRQ
SSTYVETGKT VDLTYGTGGM RGILGQDTVS VGGGSDPNQE LGESQTEPGP FQAAAPFDGI
LGLAYPSIAA AGAVPVFDNM GSQSLVEKDL FSFYLSGGGA NGSEVMLGGV DNSHYTGSIH
WIPVTAEKYW QVALDGITVN GQTAACEGCQ AIVDTGTSKI VAPVSALANI MKDIGASENQ
GEMMGNCASV QSLPDITFTI NGVKQPLPPS AYIEGDQAFC TSGLGSSGVP SNTSELWIFG
DVFLRNYYTI YDRTNNKVGF APAA
