eF-site ID 2gbc-AB PDB Code 2gbc Chain A, B click to enlarge Title Native DPP-IV (CD26) from Rat Classification HYDROLASE Compound Dipeptidyl peptidase 4 Source ORGANISM_COMMON: Norway rat; ORGANISM_SCIENTIFIC: Rattus norvegicus; Sequence A:  RRTYTLADYLKNTFRVKSYSLRWVSDSEYLYKQENNILLF NAEHGNSSIFLENSTFEIFGDSISDYSVSPDRLFVLLEYN YVKQWRHSYTASYSIYDLNKRQLITEEKIPNNTQWITWSQ EGHKLAYVWKNDIYVKIEPHLPSHRITSTGKENVIFNGIN DWVYEEEIFGAYSALWWSPNGTFLAYAQFNDTGVPLIEYS FYSDESLQYPKTVWIPYPKAGAVNPTVKFFIVNTDSLSST TTTIPMQITAPASVTTGDHYLCDVAWVSEDRISLQWLRRI QNYSVMAICDYDKTTLVWNCPTTQEHIETSATGWCGRFRP AEPHFTSDGSSFYKIVSDKDGYKHICQFQKDRKPEQVCTF ITKGAWEVISIEALTSDYLYYISNEYKEMPGGRNLYKIQL TDHTNKKCLSCDLNPERCQYYSVSLSKEAKYYQLGCRGPG LPLYTLHRSTDQKELRVLEDNSALDKMLQDVQMPSKKLDF IVLNETRFWYQMILPPHFDKSKKYPLLIDVYAGPCSQKAD AAFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINK RLGTLEVEDQIEAARQFLKMGFVDSKRVAIWGWSYGGYVT SMVLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTP EDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQS AQISKALVDAGVDFQAMWYTDEDHGIASSTAHQHIYSHMS HFLQQCFSLR B:  RRTYTLADYLKNTFRVKSYSLRWVSDSEYLYKQENNILLF NAEHGNSSIFLENSTFEIFGDSISDYSVSPDRLFVLLEYN YVKQWRHSYTASYSIYDLNKRQLITEEKIPNNTQWITWSQ EGHKLAYVWKNDIYVKIEPHLPSHRITSTGKENVIFNGIN DWVYEEEIFGAYSALWWSPNGTFLAYAQFNDTGVPLIEYS FYSDESLQYPKTVWIPYPKAGAVNPTVKFFIVNTDSLSST TTTIPMQITAPASVTTGDHYLCDVAWVSEDRISLQWLRRI QNYSVMAICDYDKTTLVWNCPTTQEHIETSATGWCGRFRP AEPHFTSDGSSFYKIVSDKDGYKHICQFQKDRKPEQVCTF ITKGAWEVISIEALTSDYLYYISNEYKEMPGGRNLYKIQL TDHTNKKCLSCDLNPERCQYYSVSLSKEAKYYQLGCRGPG LPLYTLHRSTDQKELRVLEDNSALDKMLQDVQMPSKKLDF IVLNETRFWYQMILPPHFDKSKKYPLLIDVYAGPCSQKAD AAFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINK RLGTLEVEDQIEAARQFLKMGFVDSKRVAIWGWSYGGYVT SMVLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTP EDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQS AQISKALVDAGVDFQAMWYTDEDHGIASSTAHQHIYSHMS HFLQQCFSLR Description (1)  Dipeptidyl peptidase 4, EC 3.4.14.5, Dipeptidyl peptidase IV, DPP IV, T-cell activation antigen CD26, GP110 glycoprotein, Bile canaliculus domain-specific membrane glycoprotein, Contains: Dipeptidyl peptidase 4 membrane form (Dipeptidyl peptidase IV membrane form); Dipeptidyl peptidase 4 soluble form (Dipeptidyl peptidase IV soluble form); Dipeptidyl peptidase 4 60 kDa soluble form (Dipeptidyl peptidase IV 60 kDa soluble form) Functional site 1) chain A residue 631 type ACT_SITE sequence S description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 2) chain A residue 709 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 3) chain A residue 741 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 4) chain B residue 631 type ACT_SITE sequence S description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 5) chain B residue 709 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 6) chain B residue 741 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 source Swiss-Prot : SWS_FT_FI1 7) chain A residue 83 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16768443 source Swiss-Prot : SWS_FT_FI2 8) chain B residue 521 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16768443 source Swiss-Prot : SWS_FT_FI2 9) chain A residue 90 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16768443 source Swiss-Prot : SWS_FT_FI2 10) chain A residue 227 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16768443 source Swiss-Prot : SWS_FT_FI2 11) chain A residue 319 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16768443 source Swiss-Prot : SWS_FT_FI2 12) chain A residue 521 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16768443 source Swiss-Prot : SWS_FT_FI2 13) chain B residue 83 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16768443 source Swiss-Prot : SWS_FT_FI2 14) chain B residue 90 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16768443 source Swiss-Prot : SWS_FT_FI2 15) chain B residue 227 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16768443 source Swiss-Prot : SWS_FT_FI2 16) chain B residue 319 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16768443 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 323-337 type prosite sequence MAICDYDKTTLVWNC description WD_REPEATS_1 Trp-Asp (WD) repeats signature. MAICdyDkTTLVWNC source prosite : PS00678 18) chain A residue 606-636 type prosite sequence DQIEAARQFLKMGFVDSKRVAIWGWSYGGYV description PRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DqieAarqFlkmgfvdskrvaiwGwSyGGYV source prosite : PS00708 19) chain A residue 148 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 217 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 686 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 22) chain B residue 148 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 23) chain B residue 217 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 24) chain B residue 686 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250 source Swiss-Prot : SWS_FT_FI3

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