ID M7ASX5_CHEMY Unreviewed; 930 AA.
AC M7ASX5;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Sortilin {ECO:0000313|EMBL:EMP28476.1};
DE Flags: Fragment;
GN ORFNames=UY3_14429 {ECO:0000313|EMBL:EMP28476.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP28476.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000256|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; KB563455; EMP28476.1; -; Genomic_DNA.
DR AlphaFoldDB; M7ASX5; -.
DR STRING; 8469.M7ASX5; -.
DR eggNOG; KOG3511; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IEA:UniProtKB-UniRule.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd03753; proteasome_alpha_type_5; 1.
DR Gene3D; 2.10.70.80; -; 1.
DR Gene3D; 3.30.60.270; -; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR033812; Proteasome_alpha_type_5.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR031777; Sortilin_C.
DR InterPro; IPR031778; Sortilin_N.
DR InterPro; IPR006581; VPS10.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR12106:SF23; SORTILIN; 1.
DR PANTHER; PTHR12106; SORTILIN RELATED; 1.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF15902; Sortilin-Vps10; 1.
DR Pfam; PF15901; Sortilin_C; 1.
DR SMART; SM00602; VPS10; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|PROSITE-
KW ProRule:PRU00808}; Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 841..862
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 215..829
FT /note="VPS10"
FT /evidence="ECO:0000259|SMART:SM00602"
FT REGION 897..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EMP28476.1"
SQ SEQUENCE 930 AA; 102399 MW; B725EC4974AC0765 CRC64;
LGSTAIGIQT SEGVCLAVEK RITSSLMEPS SIEKIVEIDS HIGCAMSGLI ADAKTLIDKA
RVETQNHWFT YNEIMTVESV TQAVSNLALQ FGEEDADPGA MSRPFGVALL FGGVDEKGPQ
LFHMDPSGTF VQCDAKAIGS ASEGAQSSLQ EVYHKSMTLK EAIKSSLIIL KQVMEEKLNA
TNIEYVFDDF SGTVSLSWVG DSTGVILVLT TFKLPLLFVS FKQSKLYRSE DYGKTFIDIT
KLINHTFIRT ELGMAIGPES SGKVILTGDM PVPGGSRGGK IFRSSDYAKN FAQTDLPFQP
QSQVIYHPQN SDNLLLLSTE NSLWVSRNFG EKWEEIHKAV CLAKWGPNTT IFFTTYLNDS
CKTDLGFLEL KKTSDFGKSF KTIGNKIYSF GLGGRFLFTS VVTEKGNTRR IHVSTDQGET
WNMAQLPSVG QEQFFSILAA NEDMVFMHVD DPGDTGCGTI YTSDDRGLIY SKSLERHLYT
GIGSETDFTN VTSLRGVYIT SVLSEDRSIQ SVITFDQGGE WLPLRTPVNA KCNSAAKNKE
ECSLYIYALY GISLNHNVPM LPLSEPNVVG TVIAHGSVGD AISVVSPDVY VSDDGGYTWA
RVLEGPHHYA ILDSGGIIVA IEHSLEPINV IKFSTDEGQC WHKYTFSKEP IYFTGLASEP
GARSMNVSLW GYRDSVLPRK WVSYTIDFSR LLSRQCEEED YTIWLAHSSE PGSRTDGCVL
GYKEQYLRLR KSSVCQNGRD YVMIKQPSVC PCTLEDYLCD FGYFRPENQS VCVEQPELKG
HDLEFCLYGR QELLTTRGYR KIPGDKCSGG KSPSREVTDL KRKCTSNLLT PSQLSATSSS
APVILAAVGV MLLTIIAGVL IIKKYVCGGR FLVHRYSVLQ QHAEANGVEG VDALEAASPA
NKGGYHDDSD EDKQPPAMDL PGLRYASMDP
//
