GOLM2_PONAB
ID GOLM2_PONAB Reviewed; 436 AA.
AC Q5R5X4;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Protein GOLM2 {ECO:0000305};
DE AltName: Full=Cancer susceptibility candidate gene 4 protein homolog;
DE Short=CASC4;
DE AltName: Full=Golgi membrane protein 2 {ECO:0000305};
GN Name=GOLM2; Synonyms=CASC4 {ECO:0000250|UniProtKB:Q6P4E1};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GOLM family. {ECO:0000305}.
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DR EMBL; CR860727; CAH92842.1; -; mRNA.
DR RefSeq; NP_001126659.1; NM_001133187.1.
DR AlphaFoldDB; Q5R5X4; -.
DR SMR; Q5R5X4; -.
DR STRING; 9601.ENSPPYP00000007285; -.
DR GeneID; 100173659; -.
DR KEGG; pon:100173659; -.
DR CTD; 113201; -.
DR eggNOG; ENOG502QTYH; Eukaryota.
DR InParanoid; Q5R5X4; -.
DR OrthoDB; 913812at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR026141; CASC4.
DR InterPro; IPR026139; GOLM1/CASC4.
DR PANTHER; PTHR15896; PTHR15896; 1.
DR PANTHER; PTHR15896:SF11; PTHR15896:SF11; 1.
DR PRINTS; PR02084; GOLM1CASC4.
PE 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Membrane; Phosphoprotein; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..436
FT /note="Protein GOLM2"
FT /id="PRO_0000291845"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..436
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 193..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 35..195
FT /evidence="ECO:0000255"
FT COMPBIAS 222..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..421
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q6P4E1"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P4E1"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P4E1"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P4E1"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P4E1"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P4E1"
SQ SEQUENCE 436 AA; 49417 MW; 5160C98996AC6A03 CRC64;
MVGFGANRRA GRLPSLVLVV LLVVIVVLAF NYWSISSRHV LLQEEVAELQ GQVQRTEVAR
GRLEKRNSGL LLLVDTHKKQ IDQKEADYGR LSSRLQAREG LGKRCEDDKV KLQNNISYQM
ADIHHLKEQL AELRQEFLRQ EDQLQDYRKN NTYLVKRLEY ESFQCGQQIK ELRAQHEENI
KKLADQFLQE QKQEAHKIQS NDGKELDIND QVVPKNIPKV AENVADKNEE PSSNHIPHGK
EQIKRGGDAG MPGIEENDLA KVDDLPPALR KPPISVSQHE SHQTISHIPT GQPLSPNMPP
DSHVNHNGNP GTSKQNPSSP LQRLIPGSNL DSEPRIQTDI LKQATKDRVS DFHKLKQSRF
FDENESPVDP QHGSKLADYN GDDGNVGEYE ADKQAELAYN EEEDGDGGEE DVQDDEEREL
QMDPADYGKQ HFNDVL