ID A0A2Y9IHT8_ENHLU Unreviewed; 1069 AA.
AC A0A2Y9IHT8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Caprin-2 isoform X1 {ECO:0000313|RefSeq:XP_022347818.1, ECO:0000313|RefSeq:XP_022347826.1};
GN Name=LOC111139754 {ECO:0000313|RefSeq:XP_022347818.1,
GN ECO:0000313|RefSeq:XP_022347826.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022347826.1};
RN [1] {ECO:0000313|RefSeq:XP_022347818.1, ECO:0000313|RefSeq:XP_022347826.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022347818.1,
RC ECO:0000313|RefSeq:XP_022347826.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the caprin family.
CC {ECO:0000256|ARBA:ARBA00007950}.
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DR RefSeq; XP_022347818.1; XM_022492110.1.
DR RefSeq; XP_022347826.1; XM_022492118.1.
DR STRING; 391180.A0A2Y9IHT8; -.
DR KEGG; elk:111139754; -.
DR OrthoDB; 5403347at2759; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR001073; C1q_dom.
DR InterPro; IPR028816; Caprin.
DR InterPro; IPR022070; Caprin-1_C.
DR InterPro; IPR041637; Caprin-1_dimer.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR PANTHER; PTHR22922:SF5; CAPRIN-2; 1.
DR PANTHER; PTHR22922; GPI-ANCHORED PROTEIN P137; 1.
DR Pfam; PF00386; C1q; 1.
DR Pfam; PF12287; Caprin-1_C; 1.
DR Pfam; PF18293; Caprin-1_dimer; 1.
DR PRINTS; PR00007; COMPLEMNTC1Q.
DR SMART; SM00110; C1Q; 1.
DR SUPFAM; SSF49842; TNF-like; 1.
DR PROSITE; PS50871; C1Q; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Protein synthesis inhibitor {ECO:0000256|ARBA:ARBA00023193};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 935..1069
FT /note="C1q"
FT /evidence="ECO:0000259|PROSITE:PS50871"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 73..141
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 29..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1069 AA; 119407 MW; A0225FDE1B530F1E CRC64;
MVQLSSSPFG YQSPSGGSEE GREGNMKSAK PQVNHSQHGE SQRAMSPLQS ALSSAASPSQ
AYETYIDNGL ICLKHKIRNI EKKKLKLEDY KDRLKNGEQL NPDQLEAVEK YEEVLHNLEF
AKELQKTFSG LSQDLLKAQK KAQRREHMLK LEAEKKKLRT ILQVQYVLQN LTQEHVQKDF
KGGLNGAVYL PLKELDYLIK FSKLTCPERN ESLSVEDQME QSSLYFWDLL EGSEKAVVGT
TYKHMKDLLS KLLNSGYFES IPVPKNAKEK EVSLEEEMLI KSEKKKQLLK TESVKESESL
MELAQPEIQP QEFLNRRYMT EVDYSSKQDE EQSWEADYAR KPNLPKCWDM LTEPDGQEKK
QESFKSWEPS VKHQEVSKPA VSLEQRKQDP KLRSTLQEEQ KKQDVSKPKP APSQWKQEAP
KSKTGYIQEE QKKQETPKPW PVQLQKEQDP KKQPPKSWTP SVQNDQDITK SWTTTVCEDQ
DSRQPETPKS WENNVESQKQ PLTPQSQISP KSWGVASASL IPNDQLLPRK FNTEPKDVPK
PMHQPVGSSS TLPKDPVLRK EKLQDLMTQI QGTCNFMQES ILDFDKPSSA IPSSQPPSTT
PGSPVASTEQ NLSSQSDFLQ EPLQAAASSV TCSSNACLVA TDQASSGSET EFMTSETPEA
AVPPSKQPSS LASPNPPMSK GSEQGFQSPP ASSSSVTINT APFQAMQTVF NVNAPLPPRK
EQEIKESPYS SGYNQSFTTA STQTPPQCQL PAIHVEQTVL SQETAANYPD GTIQVSNGSL
AFYPAQTNVF PRPSQPFVNS RGSVRGCTRG GRLLTNSYRS PGGYKGFDTY RGPPSITNGN
YSQLQFQARE YPGTPYSQRD NFQQCYKRGG TSGGPRTNSR AGWSDSSQVS SPERDNETFN
SGDSGQGDSR SMTPVDVPVT NPAATILPVH VYPLPQQMRV AFSAARTSNL APGTLDQPIV
FDLLLNNLGE TFDLQLGRFN CPVNGTYVFI FHMLKLAVNV PLYVNLMKNE EVLVSAYAND
GAPDHETASN HAILQLFQGD QIWLRLHRGA IYGSSWKYST FSGYLLYQD
//
