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VIGLN_PONAB
ID   VIGLN_PONAB             Reviewed;        1268 AA.
AC   Q5R439;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Vigilin;
DE   AltName: Full=High density lipoprotein-binding protein;
DE            Short=HDL-binding protein;
GN   Name=HDLBP;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Appears to play a role in cell sterol metabolism. It may
CC       function to protect cells from over-accumulation of cholesterol (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
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DR   EMBL; CR861421; CAH93477.1; -; mRNA.
DR   AlphaFoldDB; Q5R439; -.
DR   SMR; Q5R439; -.
DR   STRING; 9601.ENSPPYP00000014936; -.
DR   eggNOG; KOG2208; Eukaryota.
DR   InParanoid; Q5R439; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1370.10; -; 14.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   Pfam; PF00013; KH_1; 14.
DR   SMART; SM00322; KH; 14.
DR   SUPFAM; SSF54791; SSF54791; 12.
DR   PROSITE; PS50084; KH_TYPE_1; 14.
PE   2: Evidence at transcript level;
KW   Acetylation; Cholesterol metabolism; Cytoplasm; HDL; Lipid metabolism;
KW   Lipid transport; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   RNA-binding; Steroid metabolism; Sterol metabolism; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q00341"
FT   CHAIN           2..1268
FT                   /note="Vigilin"
FT                   /id="PRO_0000269566"
FT   DOMAIN          158..229
FT                   /note="KH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          230..302
FT                   /note="KH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          303..371
FT                   /note="KH 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          372..442
FT                   /note="KH 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          443..514
FT                   /note="KH 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          515..588
FT                   /note="KH 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          589..660
FT                   /note="KH 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          661..734
FT                   /note="KH 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          735..807
FT                   /note="KH 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          808..880
FT                   /note="KH 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          881..979
FT                   /note="KH 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          980..1059
FT                   /note="KH 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          1060..1134
FT                   /note="KH 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          1135..1209
FT                   /note="KH 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   REGION          910..947
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1237..1268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        928..947
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00341"
FT   MOD_RES         8
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00341"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00341"
FT   MOD_RES         31
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00341"
FT   MOD_RES         35
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1A6"
FT   MOD_RES         295
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         296
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         317
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00341"
FT   MOD_RES         437
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00341"
FT   MOD_RES         645
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1A6"
FT   MOD_RES         991
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VDJ3"
FT   MOD_RES         1247
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00341"
FT   MOD_RES         1252
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00341"
SQ   SEQUENCE   1268 AA;  141302 MW;  99FA3284EE40B5C4 CRC64;
     MSSVAVLTQE SFAEHRSGLV PQQIKVATLN SEEESDPPTY KDAFPPLPEK AACLESAQEP
     AGAWGNKIRP IKASVITQVF HVPLEERKYK DMNQFGEGEQ AKICLEIMQR TGAHLELSLA
     KDQGLSIMVS GKLDAVMKAR KDIVARLQTQ ASATVAIPKE HHRFVIGKNG EKLQDLELKT
     ATKIQIPRPD DPSNQIKITG TKEGIEKARH EVLLISAEQD ERAVERLEVE KAFHPFIAGP
     YNRLVGEIMQ ETGTRINIPP PSVNRTEIVF TGEKEQLAQA VARIKKIYEE KKKKTTTIAV
     EVKKSQHKYV IGPKGNSLQE ILERTGVSVE IPPSDSISET VILRGEPEKL GQALTEVYAK
     ANSFTVSSVA APSWLHRFII GKKGQNLAKI TQQMPKVHIE FTEGEDKITL EGPTEDVSVT
     QEHIEGMVKD LINRMDYVEI NIDHKFHRHL IGKSGANINR IKDQYKVSVR IPPDSEKSNL
     IRIEGDPQGV QQAKRELLEL ASRMENERTK DLIIEQRFHR TIIGQKGERI REIRDKFPEV
     IINFPDPAQK SDIVQLRGPK NEVEKCTKYM QKMVADLVEN SYSISVPIFK QFHKNIIGKG
     GANIKKIREE SNTKIDLPAE NSNSETIIIT GKRANCEAAR SRILSIQKDL ANIAEVEVSI
     PAKLHNSLIG TKGRLIRSIM EECGGVHIHF PVEGSGSDTV VIRGPSSDVE KAKKQLLHLA
     EEKQTKSFTV DIRAKPEYHK FLIGKGGGKI RKVRDSTGAR VIFPAAEDKD QDLITIIGKE
     DAVREAQKEL EALIQNLDNV VEDSMLVDPK HHRHFVIRRG QVLREIAEEY GGVMVSFPRS
     GTQSDKVTLK GAKGCVEAAK KRIQEIIEDL EAQVTLECAI PQKFHRSVMG PKGSRIQQIT
     RDFSVQIKFP DREENPVHST EPAVQENGDE AGEGREAKDS DPGSPRRCDI IIISGRKEKC
     EAAKEALEAL VPVTVEVEVP FDLHRYVIGQ KGSGIRKMMD EFEVNIHVPA PELQSDIIAI
     TGLAANLDRA KAGLLERVKE LQAEQEDRAL RSFKLSVTVD PKYHPKIIGR KGAVITQIRL
     EHDVNIQFPD KGDGNQPQDQ ITITGYEKNT EAARDAILRI VGELEQMVSE DVPLDHRVHA
     RIIGARGKAI RKIMDEFKVD IRFPQSGAPD PNCVTVTGLP ENVEEAIDHI LNLEEEYLAD
     VVDSEALQVY MKPPVHEEAK APSRGFVVRD APWAASSSEK APDMSSSEEF PSFGAQVAPK
     TLPWGPKR
 
 
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