ID A0A1S3NPU5_SALSA Unreviewed; 1331 AA.
AC A0A1S3NPU5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Adipocyte enhancer-binding protein 1 isoform X1 {ECO:0000313|RefSeq:XP_014017265.1};
GN Name=aebp1 {ECO:0000313|RefSeq:XP_014017265.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014017265.1};
RN [1] {ECO:0000313|RefSeq:XP_014017265.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014017265.1};
RG RefSeq;
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 RefSeq; XP_014017265.1; XM_014161790.1.
DR GeneID; 106580579; -.
DR KEGG; sasa:106580579; -.
DR OrthoDB; 5490979at2759; -.
DR Proteomes; UP000087266; Chromosome ssa20.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0032101; P:regulation of response to external stimulus; IEA:UniProt.
DR CDD; cd00057; FA58C; 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; 2.
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:SF48; ADIPOCYTE ENHANCER-BINDING PROTEIN 1; 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; 2.
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; 2.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1331
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010356762"
FT DOMAIN 468..625
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 41..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1223..1243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1331 AA; 152520 MW; 1F384ECF34B82ECE CRC64;
MGGHTAVVCL VLLGLCCVLL LRGGENAGGI VSIGQAVEDR GMDGGMESQD EPAKEQELTE
TQRQTGNAKR ATEEEAVPAR VRRAPEEEEG KGKKKKGKKD KKNKESKADK KLKDKGGRRG
KAPTTPPPTT TTLPPTTTTE VYTEPAPTEP DPYPDFPYLD SEDDYWNPDD DKPATPKTDS
EDEYWNPDDD KPATPKTDSE DEYWNPDDDK PATPKTDSED EYWNPDDDKP ATPETDSEDE
YWNPDDDKPA TPETDSEDEY WNPDDDKPAT PETDSEDEYW NPDDDKPATP EIDSEDEYWN
PDDDKPATPE TDSEDDYWKG EEEEPAGPVV DPENDYWKGE DPTATHTPLV VDGEVDTGDE
DYWEAKYEVP ENLPFPDGKE VVPTEKDDLS YAVTEDSITP PPTYESPWYE EYDYGYSGGE
TKKQEEEEER ERQRKEKERE DRERAQQRRE EEDREKAKKK PPVFKEPKKC PPLGMESHRI
ESDQLLASSM SHHRYSQGRA RLNMQASEDE EDMRGGAWCP NQEDNIHWFE IDARRATEFT
GIITQGRDSR NESDFVTSYY VQFSNDSREW TTMNDGYSDW LFFGNSDKDT PVLNQLAEPI
LARYIRVIPQ SWNGSCCMRL EVLGCPLPDP TSAYQRLQNE VTPVQYLDFR HHNYSDMVTL
MKSVSEECPN ITSMYSLGRS SNGLDIVAMV ISGNPTEHEI GEPEFRYTAG LHGNEATGRE
MVLLLMQYLC KEYRDGNPRV RRLVEGIRTH LVPSLNPDGQ EKALIAGSEL SGWTTGHWTE
DGHDIFHNFP DLNSVLWEAE DKGMVPKLTP NHHVKIPADS VGDDKIAVET QAIISWMENH
PFVLGANFQG GERVVAYPYD NHRLTKAAST SERDRAHSRK KRQYEDEYDR GTDWDRGYDR
EEPEDDDRNR GYQEPEEDRW NRGYQQPEED RWNRGYQEPE EDRQNRGYQQ PEEDRWNRGY
QQPEEDRWNR GYQEPEEDRW NRGYQQPEEE WRGHGYGHRE EEEEDDRGGH QEAEPEDEPR
TTADASFFRW LAISYASTHL SMTYTSHGSC HSDDITGGVG IINRAKWKPI TGSMNDFSYL
HTNCLELSVF LGCDKFPHQT ELVIEWEKNR EAMLTFMEQV HRGIRGVVKD KEGNPITNAT
VSVEGVNHDV TTAVTGDYWR LLNPGEYRVT VRAEGFTPLT KLCVVGYEPG PTTCSFNLAK
SNWDRIKQIM ALHGNKPIRL LSHGNGGTRR NTASNGNSRV VHNNGAAANE PETIRMRQQK
RRLGRLRRLR QQKLMRLTTT LPPTTTPVPT TTEAEPTTAW YDSWLIGEGQ TSAPEGFTDS
ILDYNYEIDD Y
//
