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Database: UniProt
Entry: A0A3Q1J0A5_ANATE
LinkDB: A0A3Q1J0A5_ANATE
Original site: A0A3Q1J0A5_ANATE 
ID   A0A3Q1J0A5_ANATE        Unreviewed;       397 AA.
AC   A0A3Q1J0A5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Procollagen C-endopeptidase enhancer 2b {ECO:0000313|Ensembl:ENSATEP00000009131.2};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000009131.2, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000009131.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR   AlphaFoldDB; A0A3Q1J0A5; -.
DR   STRING; 64144.ENSATEP00000009131; -.
DR   Ensembl; ENSATET00000009290.2; ENSATEP00000009131.2; ENSATEG00000006332.2.
DR   GeneTree; ENSGT00940000157649; -.
DR   Proteomes; UP000265040; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   CDD; cd00041; CUB; 2.
DR   Gene3D; 2.40.50.120; -; 1.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR001134; Netrin_domain.
DR   InterPro; IPR018933; Netrin_module_non-TIMP.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR008993; TIMP-like_OB-fold.
DR   PANTHER; PTHR24251; OVOCHYMASE-RELATED; 1.
DR   PANTHER; PTHR24251:SF31; PROCOLLAGEN C-ENDOPEPTIDASE ENHANCER 2; 1.
DR   Pfam; PF00431; CUB; 2.
DR   Pfam; PF01759; NTR; 1.
DR   SMART; SM00042; CUB; 2.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR   SUPFAM; SSF50242; TIMP-like; 1.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS50189; NTR; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00059}; Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           39..397
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5030080159"
FT   DOMAIN          48..159
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          169..283
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          315..397
FT                   /note="NTR"
FT                   /evidence="ECO:0000259|PROSITE:PS50189"
FT   DISULFID        169..196
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
SQ   SEQUENCE   397 AA;  43960 MW;  0E37A2DD41CF33EE CRC64;
     MPFMPRNRRK ACSVNPTMWS TCGIFGAWSL LFLTEVCAQS QQRPTFTCGG NITEESGVIG
     SQGYPGVYPP NTKCVWRITV PEGKVVVLSF RFIDLENDNL CRYDYVDVYS GHVNGQRLGR
     FCGTFKPGSL VSMGNKMLLQ MVSDANTAGS GFLAVFSAAH PHERGDQYCG GRLDKPTGTF
     KTPNWPEKDY PAGVTCSWHI VAPKNQIIEV KFEKFDVERD NYCRYDHVSI FNGAEINDAK
     RIGKYCGDSP PGPVYSDGNQ LLIQFLSDLS LTADGFIGHY KFRPKKFPTT TISPTTTTQP
     VTTRPIPLKY SVALCQQKCN RRGTLESNYC SSNFVITGTV ITAVMRGGSM YATVSIINVY
     KEGSLAIQQA GKTMSTKIII LCKKCPFIRR GEDTVCC
//
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