ID   CRLD2_BOVIN             Reviewed;         496 AA.
AC   A6QLZ7;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Cysteine-rich secretory protein LCCL domain-containing 2;
DE   Flags: Precursor;
GN   Name=CRISPLD2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal spinal cord;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Promotes matrix assembly. {ECO:0000250}.
CC   -!- SUBUNIT: Binds to heparin, dermatan sulfate and chondroitin sulfate.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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DR   EMBL; BC148143; AAI48144.1; -; mRNA.
DR   RefSeq; NP_001093769.1; NM_001100299.1.
DR   AlphaFoldDB; A6QLZ7; -.
DR   SMR; A6QLZ7; -.
DR   STRING; 9913.ENSBTAP00000028221; -.
DR   PaxDb; A6QLZ7; -.
DR   Ensembl; ENSBTAT00000028221; ENSBTAP00000028221; ENSBTAG00000021176.
DR   GeneID; 505329; -.
DR   KEGG; bta:505329; -.
DR   CTD; 83716; -.
DR   VEuPathDB; HostDB:ENSBTAG00000021176; -.
DR   VGNC; VGNC:27715; CRISPLD2.
DR   eggNOG; KOG3017; Eukaryota.
DR   GeneTree; ENSGT00940000157410; -.
DR   HOGENOM; CLU_042287_0_0_1; -.
DR   InParanoid; A6QLZ7; -.
DR   OMA; VNTCQRM; -.
DR   OrthoDB; 1528782at2759; -.
DR   TreeFam; TF316148; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000021176; Expressed in ureter and 103 other tissues.
DR   ExpressionAtlas; A6QLZ7; baseline and differential.
DR   GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0030133; C:transport vesicle; IEA:Ensembl.
DR   GO; GO:0005539; F:glycosaminoglycan binding; IBA:GO_Central.
DR   GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR   GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
DR   Gene3D; 2.170.130.20; -; 2.
DR   Gene3D; 3.40.33.10; -; 1.
DR   InterPro; IPR018244; Allrgn_V5/Tpx1_CS.
DR   InterPro; IPR014044; CAP_domain.
DR   InterPro; IPR035940; CAP_sf.
DR   InterPro; IPR001283; CRISP-related.
DR   InterPro; IPR004043; LCCL.
DR   InterPro; IPR036609; LCCL_sf.
DR   PANTHER; PTHR10334; PTHR10334; 1.
DR   Pfam; PF00188; CAP; 1.
DR   Pfam; PF03815; LCCL; 2.
DR   PRINTS; PR00837; V5TPXLIKE.
DR   SMART; SM00603; LCCL; 2.
DR   SMART; SM00198; SCP; 1.
DR   SUPFAM; SSF55797; SSF55797; 1.
DR   SUPFAM; SSF69848; SSF69848; 2.
DR   PROSITE; PS01010; CRISP_2; 1.
DR   PROSITE; PS50820; LCCL; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..496
FT                   /note="Cysteine-rich secretory protein LCCL domain-
FT                   containing 2"
FT                   /id="PRO_0000363884"
FT   DOMAIN          60..200
FT                   /note="SCP"
FT   DOMAIN          283..378
FT                   /note="LCCL 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00123"
FT   DOMAIN          384..487
FT                   /note="LCCL 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00123"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        289..307
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00123"
FT   DISULFID        311..331
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00123"
FT   DISULFID        390..412
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00123"
FT   DISULFID        416..439
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00123"
SQ   SEQUENCE   496 AA;  55581 MW;  25764FBB1605BAD9 CRC64;
     MSCVLTGVVP LGLVLLLCGA QGFFLPNVTQ LEKLLSKYQG DQPHSRTRRA ISRADREEIL
     TLHNKLRGQV SPPASNMEYM TWDEELEKSA VAWARECIWE HGPTSLLVSI GQNLAVHWGR
     PRSPGSHVQS WYDEVKDYTY PYPHECNPWC PERCSGPMCT HYTQIVWATT NRIGCAVNTC
     PRMNVWGDVW ENAVYLVCNY FPKGNWIGEA PYKTGQPCSE CPGKYRGGCK NNLCYQETYG
     QETETDDMNE VEAAPIPDEK HVWVTPRVIK PKKPKKDSPV NYMTQVVKCD TKMKDKCKGS
     TCNRYQCPAG CLHSGAKIFG TLFYESASSI CRAAIHYGIL DDRGGLVDVT RNGKVPFFVK
     SERNGVQSLS KYKASSSFTV SKVKVQDLDC YTTVAQLCPY EKPGTHCPRV RCPAHCKDEP
     SYWAPVFGSN IYADTSSICK TAVHAGVIRN ESGGYVDVMP VDKKKTYVAS LRNGVQSESL
     RTPRDGKAFR IFAVRQ